Ligand source activities (1 row/activity)



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Ligands (move mouse cursor over ligand name to see structure) Receptor Activity Chemical information
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 Activity
Type		 Activity
Relation		 Activity
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 DOI
10353365 83279 None 1 Human Functional pEC50 = 10.1 10.1 13 3
Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells
ChEMBL 219 2 3 4 -1.8 N[C@@]1(C(=O)O)C[S+]([O-])[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm060917u
CHEMBL218710 83279 None 1 Human Functional pEC50 = 10.1 10.1 13 3
Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells
ChEMBL 219 2 3 4 -1.8 N[C@@]1(C(=O)O)C[S+]([O-])[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm060917u
117972056 142220 None 0 Human Functional pEC50 = 9.4 9.4 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 405 5 0 4 5.2 Fc1ccc(C2CC(Oc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)C2)cc1 10.1016/j.bmc.2016.11.018
CHEMBL3883435 142220 None 0 Human Functional pEC50 = 9.4 9.4 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 405 5 0 4 5.2 Fc1ccc(C2CC(Oc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)C2)cc1 10.1016/j.bmc.2016.11.018
117971665 142313 None 0 Human Functional pEC50 = 9.4 9.4 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 415 5 0 4 5.8 FC(F)(F)c1c(O[C@H]2CC[C@H](c3ccccc3)CC2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
CHEMBL3884532 142313 None 0 Human Functional pEC50 = 9.4 9.4 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 415 5 0 4 5.8 FC(F)(F)c1c(O[C@H]2CC[C@H](c3ccccc3)CC2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
117971685 142300 None 0 Human Functional pEC50 = 9.3 9.3 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 387 5 0 4 5.0 FC(F)(F)c1c(OC2CC(c3ccccc3)C2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
CHEMBL3884187 142300 None 0 Human Functional pEC50 = 9.3 9.3 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 387 5 0 4 5.0 FC(F)(F)c1c(OC2CC(c3ccccc3)C2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
1395 2528 None 14 Rat Functional pEC50 = 9.2 9.2 -7 4
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 217 2 3 4 -1.2 O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O 10.1021/jm000346k
9837317 2528 None 14 Rat Functional pEC50 = 9.2 9.2 -7 4
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 217 2 3 4 -1.2 O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O 10.1021/jm000346k
CHEMBL121053 2528 None 14 Rat Functional pEC50 = 9.2 9.2 -7 4
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 217 2 3 4 -1.2 O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O 10.1021/jm000346k
1395 2528 None 14 Human Functional pEC50 = 9.2 9.2 3 4
Agonist activity at mGLUR2 expressed in CHO cellsAgonist activity at mGLUR2 expressed in CHO cells
ChEMBL 217 2 3 4 -1.2 O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O 10.1016/j.bmcl.2012.01.039
9837317 2528 None 14 Human Functional pEC50 = 9.2 9.2 3 4
Agonist activity at mGLUR2 expressed in CHO cellsAgonist activity at mGLUR2 expressed in CHO cells
ChEMBL 217 2 3 4 -1.2 O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O 10.1016/j.bmcl.2012.01.039
CHEMBL121053 2528 None 14 Human Functional pEC50 = 9.2 9.2 3 4
Agonist activity at mGLUR2 expressed in CHO cellsAgonist activity at mGLUR2 expressed in CHO cells
ChEMBL 217 2 3 4 -1.2 O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O 10.1016/j.bmcl.2012.01.039
71131322 123473 None 0 Human Functional pEC50 = 9.2 9.2 43 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 334 5 4 6 0.3 N[C@@]1(C(=O)O)C[C@H](Sc2nnc(C(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616857 123473 None 0 Human Functional pEC50 = 9.2 9.2 43 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 334 5 4 6 0.3 N[C@@]1(C(=O)O)C[C@H](Sc2nnc(C(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
90098428 123472 None 0 Human Functional pEC50 = 9.2 9.2 60 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 352 4 4 6 0.4 N[C@@]1(C(=O)O)C[C@H](Sc2nnc(C(F)(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616856 123472 None 0 Human Functional pEC50 = 9.2 9.2 60 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 352 4 4 6 0.4 N[C@@]1(C(=O)O)C[C@H](Sc2nnc(C(F)(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
68109941 156213 None 0 Human Functional pEC50 = 9.0 9.0 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 504 6 2 5 6.5 O[C@]1(C2CC2)CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4063313 156213 None 0 Human Functional pEC50 = 9.0 9.0 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 504 6 2 5 6.5 O[C@]1(C2CC2)CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
1395 2528 None 14 Rat Functional pEC50 = 8.9 8.9 -7 4
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 217 2 3 4 -1.2 O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O 10.1021/jm000346k
9837317 2528 None 14 Rat Functional pEC50 = 8.9 8.9 -7 4
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 217 2 3 4 -1.2 O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O 10.1021/jm000346k
CHEMBL121053 2528 None 14 Rat Functional pEC50 = 8.9 8.9 -7 4
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 217 2 3 4 -1.2 O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O 10.1021/jm000346k
123289788 142324 None 0 Human Functional pEC50 = 8.9 8.9 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 421 6 0 4 5.5 FC(F)(F)c1c(OCC2CC2c2ccc(Cl)cc2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
CHEMBL3884636 142324 None 0 Human Functional pEC50 = 8.9 8.9 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 421 6 0 4 5.5 FC(F)(F)c1c(OCC2CC2c2ccc(Cl)cc2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
117972250 142399 None 4 Human Functional pEC50 = 8.9 8.9 32 2
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 421 6 0 4 5.5 FC(F)(F)c1c(OC[C@H]2C[C@@H]2c2ccc(Cl)cc2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
CHEMBL3885379 142399 None 4 Human Functional pEC50 = 8.9 8.9 32 2
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 421 6 0 4 5.5 FC(F)(F)c1c(OC[C@H]2C[C@@H]2c2ccc(Cl)cc2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
134130172 142246 None 0 Human Functional pEC50 = 8.8 8.8 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 405 6 0 4 5.0 Fc1ccc(C2CC2COc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1 10.1016/j.bmc.2016.11.018
CHEMBL3883634 142246 None 0 Human Functional pEC50 = 8.8 8.8 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 405 6 0 4 5.0 Fc1ccc(C2CC2COc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1 10.1016/j.bmc.2016.11.018
117968349 142287 None 0 Human Functional pEC50 = 8.7 8.7 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 429 6 0 4 6.0 FC(F)(F)c1c(OCC2(c3ccccc3)CCCCC2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
CHEMBL3884094 142287 None 0 Human Functional pEC50 = 8.7 8.7 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 429 6 0 4 6.0 FC(F)(F)c1c(OCC2(c3ccccc3)CCCCC2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
1393 1539 None 42 Human Functional pEC50 = 8 8.0 2 6
Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm040222y
1396 1539 None 42 Human Functional pEC50 = 8 8.0 2 6
Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm040222y
213056 1539 None 42 Human Functional pEC50 = 8 8.0 2 6
Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm040222y
CHEMBL8759 1539 None 42 Human Functional pEC50 = 8 8.0 2 6
Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm040222y
117968551 142310 None 0 Human Functional pEC50 = 8 8.0 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 393 6 0 4 5.0 CC(COc1ccn2c(CC3CC3)nnc2c1C(F)(F)F)c1ccc(F)cc1 10.1016/j.bmc.2016.11.018
CHEMBL3884343 142310 None 0 Human Functional pEC50 = 8 8.0 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 393 6 0 4 5.0 CC(COc1ccn2c(CC3CC3)nnc2c1C(F)(F)F)c1ccc(F)cc1 10.1016/j.bmc.2016.11.018
146036859 174651 None 5 Human Functional pEC50 = 8 8.0 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 293 2 0 3 3.8 Brc1cccc2c1nnn2CC1CCCCC1 10.1021/acs.jmedchem.8b00161
CHEMBL4556144 174651 None 5 Human Functional pEC50 = 8 8.0 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 293 2 0 3 3.8 Brc1cccc2c1nnn2CC1CCCCC1 10.1021/acs.jmedchem.8b00161
68108471 82680 None 0 Human Functional pEC50 = 8 8.0 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 436 4 0 4 5.4 Fc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/jm3010724
CHEMBL2179326 82680 None 0 Human Functional pEC50 = 8 8.0 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 436 4 0 4 5.4 Fc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/jm3010724
156020355 178133 None 0 Human Functional pEC50 = 8 8.0 104 2
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 396 5 0 5 4.7 COc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1 10.1021/acs.jmedchem.0c01058
CHEMBL4646835 178133 None 0 Human Functional pEC50 = 8 8.0 104 2
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 396 5 0 5 4.7 COc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1 10.1021/acs.jmedchem.0c01058
67060140 167493 None 0 Rat Functional pEC50 = 8.0 8.0 26 2
Positive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis
ChEMBL 362 4 0 5 3.7 Cc1cccc(-c2ccc(OC[C@@H]3Cn4c(C)cc(=O)nc4O3)cc2)c1C 10.1016/j.bmcl.2018.08.022
CHEMBL4295230 167493 None 0 Rat Functional pEC50 = 8.0 8.0 26 2
Positive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis
ChEMBL 362 4 0 5 3.7 Cc1cccc(-c2ccc(OC[C@@H]3Cn4c(C)cc(=O)nc4O3)cc2)c1C 10.1016/j.bmcl.2018.08.022
71135411 123464 None 0 Human Functional pEC50 = 8.0 8.0 5 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 298 4 4 6 -0.3 Cc1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
CHEMBL3616848 123464 None 0 Human Functional pEC50 = 8.0 8.0 5 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 298 4 4 6 -0.3 Cc1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
57459497 83935 None 0 Human Functional pEC50 = 8.0 8.0 - 1
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 442 4 0 5 5.0 COc1ccc(F)cc1C1CCN(c2ccn3c(CC(F)(F)F)nnc3c2Cl)CC1 10.1021/jm300912k
CHEMBL2206439 83935 None 0 Human Functional pEC50 = 8.0 8.0 - 1
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 442 4 0 5 5.0 COc1ccc(F)cc1C1CCN(c2ccn3c(CC(F)(F)F)nnc3c2Cl)CC1 10.1021/jm300912k
44361501 119368 None 0 Rat Functional pEC50 = 7 7.0 - 1
Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells
ChEMBL 217 5 4 4 -1.2 N[C@H](C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1CC(=O)O 10.1021/jm030967o
CHEMBL343994 119368 None 0 Rat Functional pEC50 = 7 7.0 - 1
Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells
ChEMBL 217 5 4 4 -1.2 N[C@H](C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1CC(=O)O 10.1021/jm030967o
70683631 74614 None 0 Human Functional pEC50 = 7 7.0 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 384 6 0 4 5.4 CC(C)CCn1ccc(-c2ccc(OC3CCCC3)c(Cl)c2)c(C#N)c1=O 10.1021/jm2016864
CHEMBL2029795 74614 None 0 Human Functional pEC50 = 7 7.0 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 384 6 0 4 5.4 CC(C)CCn1ccc(-c2ccc(OC3CCCC3)c(Cl)c2)c(C#N)c1=O 10.1021/jm2016864
70689929 74634 None 0 Human Functional pEC50 = 7 7.0 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 387 6 0 5 5.2 Cc1ccc(Oc2ccc(-c3ccn(CCC(C)C)c(=O)c3C#N)cc2)c(C)n1 10.1021/jm2016864
CHEMBL2029813 74634 None 0 Human Functional pEC50 = 7 7.0 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 387 6 0 5 5.2 Cc1ccc(Oc2ccc(-c3ccn(CCC(C)C)c(=O)c3C#N)cc2)c(C)n1 10.1021/jm2016864
70689930 74638 None 0 Human Functional pEC50 = 7 7.0 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 393 6 0 5 5.3 CCCCn1ccc(-c2ccc(Oc3cccnc3C)c(Cl)c2)c(C#N)c1=O 10.1021/jm2016864
CHEMBL2029817 74638 None 0 Human Functional pEC50 = 7 7.0 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 393 6 0 5 5.3 CCCCn1ccc(-c2ccc(Oc3cccnc3C)c(Cl)c2)c(C#N)c1=O 10.1021/jm2016864
66785101 158137 None 0 Human Functional pEC50 = 7 7.0 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 422 6 0 5 5.9 CCc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)ccn1 10.1021/acs.jmedchem.7b00669
CHEMBL4085882 158137 None 0 Human Functional pEC50 = 7 7.0 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 422 6 0 5 5.9 CCc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)ccn1 10.1021/acs.jmedchem.7b00669
71136186 152158 None 0 Human Functional pEC50 = 7 7.0 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 431 3 0 6 3.5 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3cccnc3)nc21 nan
CHEMBL3967432 152158 None 0 Human Functional pEC50 = 7 7.0 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 431 3 0 6 3.5 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3cccnc3)nc21 nan
151031 158385 None 5 Rat Functional pEC50 = 4 4.0 - 1
Activity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulationActivity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulation
ChEMBL 160 2 3 4 -0.9 NC(C(=O)O)C1CC(O)=NO1 10.1021/jm701394a
59951973 158385 None 5 Rat Functional pEC50 = 4 4.0 - 1
Activity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulationActivity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulation
ChEMBL 160 2 3 4 -0.9 NC(C(=O)O)C1CC(O)=NO1 10.1021/jm701394a
CHEMBL408899 158385 None 5 Rat Functional pEC50 = 4 4.0 - 1
Activity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulationActivity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulation
ChEMBL 160 2 3 4 -0.9 NC(C(=O)O)C1CC(O)=NO1 10.1021/jm701394a
168298834 192802 None 0 Human Functional pEC50 = 7 7.0 - 1
Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding
ChEMBL 372 7 0 6 3.8 CCCCn1cnn2c(-c3ccc(OCC4CC4)c(Cl)c3)cnc2c1=O 10.1021/acs.jmedchem.2c00969
CHEMBL5219313 192802 None 0 Human Functional pEC50 = 7 7.0 - 1
Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding
ChEMBL 372 7 0 6 3.8 CCCCn1cnn2c(-c3ccc(OCC4CC4)c(Cl)c3)cnc2c1=O 10.1021/acs.jmedchem.2c00969
11951272 67251 None 0 Human Functional pEC50 = 6 6.0 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 475 12 1 6 6.4 CCCc1c(OCCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
CHEMBL187939 67251 None 0 Human Functional pEC50 = 6 6.0 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 475 12 1 6 6.4 CCCc1c(OCCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
59234239 114623 None 0 Human Functional pEC50 = 7.0 7.0 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 349 5 0 4 4.2 CC(C)CCn1ccc(N2CCC(c3ccccc3)CC2)c(C#N)c1=O 10.1021/jm500496m
CHEMBL3337502 114623 None 0 Human Functional pEC50 = 7.0 7.0 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 349 5 0 4 4.2 CC(C)CCn1ccc(N2CCC(c3ccccc3)CC2)c(C#N)c1=O 10.1021/jm500496m
57459640 82669 None 0 Human Functional pEC50 = 7.0 7.0 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 366 4 0 4 4.7 Clc1c(N2CCC(c3ccccc3)CC2)ccn2c(CC3CC3)nnc12 10.1021/jm3010724
CHEMBL2179314 82669 None 0 Human Functional pEC50 = 7.0 7.0 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 366 4 0 4 4.7 Clc1c(N2CCC(c3ccccc3)CC2)ccn2c(CC3CC3)nnc12 10.1021/jm3010724
11545979 165891 None 0 Human Functional pEC50 = 6.0 6.0 - 1
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 407 8 1 5 6.1 Cc1c(OCc2ccc(Sc3ccncc3)cc2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
CHEMBL424795 165891 None 0 Human Functional pEC50 = 6.0 6.0 - 1
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 407 8 1 5 6.1 Cc1c(OCc2ccc(Sc3ccncc3)cc2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
44595851 3802 None 6 Human Functional pEC50 = 7.0 7.0 -3 2
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 475 8 2 6 4.5 Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C 10.1021/acs.jmedchem.7b00669
6259 3802 None 6 Human Functional pEC50 = 7.0 7.0 -3 2
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 475 8 2 6 4.5 Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C 10.1021/acs.jmedchem.7b00669
CHEMBL4092105 3802 None 6 Human Functional pEC50 = 7.0 7.0 -3 2
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 475 8 2 6 4.5 Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C 10.1021/acs.jmedchem.7b00669
11950926 67280 None 0 Human Functional pEC50 = 6.0 6.0 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 433 9 1 6 5.4 Cc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
CHEMBL188080 67280 None 0 Human Functional pEC50 = 6.0 6.0 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 433 9 1 6 5.4 Cc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
155514221 169942 None 0 Human Functional pEC50 = 6.0 6.0 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 191 2 0 3 2.0 Fc1cccc2c1nnn2CC1CC1 10.1021/acs.jmedchem.8b00161
CHEMBL4439927 169942 None 0 Human Functional pEC50 = 6.0 6.0 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 191 2 0 3 2.0 Fc1cccc2c1nnn2CC1CC1 10.1021/acs.jmedchem.8b00161
118714735 114621 None 0 Human Functional pEC50 = 5.0 5.0 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 309 6 0 4 3.4 CC(C)CCn1ccc(N(C)Cc2ccccc2)c(C#N)c1=O 10.1021/jm500496m
CHEMBL3337500 114621 None 0 Human Functional pEC50 = 5.0 5.0 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 309 6 0 4 3.4 CC(C)CCn1ccc(N(C)Cc2ccccc2)c(C#N)c1=O 10.1021/jm500496m
70681520 74632 None 0 Human Functional pEC50 = 6.0 6.0 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 357 5 0 5 4.3 Cc1ncccc1Oc1ccc(-c2ccn(CC3CC3)c(=O)c2C#N)cc1 10.1021/jm2016864
CHEMBL2029811 74632 None 0 Human Functional pEC50 = 6.0 6.0 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 357 5 0 5 4.3 Cc1ncccc1Oc1ccc(-c2ccn(CC3CC3)c(=O)c2C#N)cc1 10.1021/jm2016864
59599475 149246 None 0 Human Functional pEC50 = 6.0 6.0 1 2
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 421 7 2 8 3.7 CC(=O)c1ccc(OCc2cccc(Oc3ccc(-c4nn[nH]n4)cn3)c2)c(F)c1O 10.1016/j.bmcl.2016.11.049
CHEMBL3943547 149246 None 0 Human Functional pEC50 = 6.0 6.0 1 2
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 421 7 2 8 3.7 CC(=O)c1ccc(OCc2cccc(Oc3ccc(-c4nn[nH]n4)cn3)c2)c(F)c1O 10.1016/j.bmcl.2016.11.049
46225569 203819 None 0 Rat Functional pEC50 = 7.0 7.0 12 2
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 373 3 0 3 5.0 Cn1c(CN2CCC(c3ccccc3C(F)(F)F)CC2)nc2ccccc21 10.1021/jm101414h
CHEMBL604467 203819 None 0 Rat Functional pEC50 = 7.0 7.0 12 2
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 373 3 0 3 5.0 Cn1c(CN2CCC(c3ccccc3C(F)(F)F)CC2)nc2ccccc21 10.1021/jm101414h
59599577 144973 None 0 Human Functional pEC50 = 7.0 7.0 -1 2
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 445 9 2 8 4.5 CCCc1c(OCc2cccc(Oc3cc(-c4nn[nH]n4)ccn3)c2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2016.11.049
CHEMBL3909995 144973 None 0 Human Functional pEC50 = 7.0 7.0 -1 2
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 445 9 2 8 4.5 CCCc1c(OCc2cccc(Oc3cc(-c4nn[nH]n4)ccn3)c2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2016.11.049
11646457 66335 None 0 Human Functional pEC50 = 6.0 6.0 - 1
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 373 10 1 5 5.3 Cc1c(OCCCCSc2cccnc2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
CHEMBL184917 66335 None 0 Human Functional pEC50 = 6.0 6.0 - 1
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 373 10 1 5 5.3 Cc1c(OCCCCSc2cccnc2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
46226934 202501 None 0 Human Functional pEC50 = 6.0 6.0 - 1
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 373 5 0 7 2.7 N#Cc1c(N2CCN(c3ncccn3)CC2)ccn2c(CCC3CC3)cnc12 10.1016/j.bmcl.2009.11.008
CHEMBL595587 202501 None 0 Human Functional pEC50 = 6.0 6.0 - 1
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 373 5 0 7 2.7 N#Cc1c(N2CCN(c3ncccn3)CC2)ccn2c(CCC3CC3)cnc12 10.1016/j.bmcl.2009.11.008
69093509 83944 None 0 Human Functional pEC50 = 8.0 8.0 - 1
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 448 5 0 5 5.2 COc1c(F)cccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1 10.1021/jm300912k
CHEMBL2206448 83944 None 0 Human Functional pEC50 = 8.0 8.0 - 1
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 448 5 0 5 5.2 COc1c(F)cccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1 10.1021/jm300912k
117972256 142285 None 0 Human Functional pEC50 = 8.0 8.0 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 347 5 0 4 4.6 Clc1ccccc1COc1ccn2c(CC3CC3)nnc2c1Cl 10.1016/j.bmc.2016.11.018
CHEMBL3884075 142285 None 0 Human Functional pEC50 = 8.0 8.0 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 347 5 0 4 4.6 Clc1ccccc1COc1ccn2c(CC3CC3)nnc2c1Cl 10.1016/j.bmc.2016.11.018
117972015 142309 None 0 Human Functional pEC50 = 8.0 8.0 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 407 6 0 4 5.2 CC(C)(COc1ccn2c(CC3CC3)nnc2c1C(F)(F)F)c1ccc(F)cc1 10.1016/j.bmc.2016.11.018
CHEMBL3884332 142309 None 0 Human Functional pEC50 = 8.0 8.0 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 407 6 0 4 5.2 CC(C)(COc1ccn2c(CC3CC3)nnc2c1C(F)(F)F)c1ccc(F)cc1 10.1016/j.bmc.2016.11.018
68107863 192481 None 0 Human Functional pEC50 = 8.0 8.0 - 1
Positive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP AssayPositive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP Assay
ChEMBL 467 5 0 5 4.8 Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(Cl)c1 10.1021/acs.jmedchem.2c00593
CHEMBL5207431 192481 None 0 Human Functional pEC50 = 8.0 8.0 - 1
Positive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP AssayPositive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP Assay
ChEMBL 467 5 0 5 4.8 Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(Cl)c1 10.1021/acs.jmedchem.2c00593
1393 1539 None 42 Human Functional pEC50 = 8.0 8.0 2 6
Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm060917u
1396 1539 None 42 Human Functional pEC50 = 8.0 8.0 2 6
Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm060917u
213056 1539 None 42 Human Functional pEC50 = 8.0 8.0 2 6
Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm060917u
CHEMBL8759 1539 None 42 Human Functional pEC50 = 8.0 8.0 2 6
Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm060917u
1393 1539 None 42 Rat Functional pEC50 = 8.0 8.0 -2 6
Agonist activity at mGLUR2 in rat cerebral cortex assessed as inhibition of forskolin-stimulated cAMP productionAgonist activity at mGLUR2 in rat cerebral cortex assessed as inhibition of forskolin-stimulated cAMP production
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1016/j.bmcl.2012.01.039
1396 1539 None 42 Rat Functional pEC50 = 8.0 8.0 -2 6
Agonist activity at mGLUR2 in rat cerebral cortex assessed as inhibition of forskolin-stimulated cAMP productionAgonist activity at mGLUR2 in rat cerebral cortex assessed as inhibition of forskolin-stimulated cAMP production
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1016/j.bmcl.2012.01.039
213056 1539 None 42 Rat Functional pEC50 = 8.0 8.0 -2 6
Agonist activity at mGLUR2 in rat cerebral cortex assessed as inhibition of forskolin-stimulated cAMP productionAgonist activity at mGLUR2 in rat cerebral cortex assessed as inhibition of forskolin-stimulated cAMP production
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1016/j.bmcl.2012.01.039
CHEMBL8759 1539 None 42 Rat Functional pEC50 = 8.0 8.0 -2 6
Agonist activity at mGLUR2 in rat cerebral cortex assessed as inhibition of forskolin-stimulated cAMP productionAgonist activity at mGLUR2 in rat cerebral cortex assessed as inhibition of forskolin-stimulated cAMP production
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1016/j.bmcl.2012.01.039
1393 1539 None 42 Human Functional pEC50 = 8.0 8.0 2 6
Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm980616n
1396 1539 None 42 Human Functional pEC50 = 8.0 8.0 2 6
Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm980616n
213056 1539 None 42 Human Functional pEC50 = 8.0 8.0 2 6
Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm980616n
CHEMBL8759 1539 None 42 Human Functional pEC50 = 8.0 8.0 2 6
Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm980616n
71136653 123470 None 0 Human Functional pEC50 = 8.0 8.0 51 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616854 123470 None 0 Human Functional pEC50 = 8.0 8.0 51 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
156013901 177343 None 0 Human Functional pEC50 = 7.9 7.9 114 2
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 440 8 0 6 4.7 COCCOc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1 10.1021/acs.jmedchem.0c01058
CHEMBL4635729 177343 None 0 Human Functional pEC50 = 7.9 7.9 114 2
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 440 8 0 6 4.7 COCCOc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1 10.1021/acs.jmedchem.0c01058
71137034 123466 None 0 Human Functional pEC50 = 7.9 7.9 7 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 334 5 4 6 0.3 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc(C(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616850 123466 None 0 Human Functional pEC50 = 7.9 7.9 7 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 334 5 4 6 0.3 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc(C(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
71454787 80840 None 0 Human Functional pEC50 = 7.0 7.0 - 1
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 428 4 0 4 6.0 N#Cc1c(-c2cc(Cl)c3c(ccn3CC3CC3)c2)ccn2c(CC(F)(F)F)cnc12 10.1021/jm201561r
CHEMBL2152118 80840 None 0 Human Functional pEC50 = 7.0 7.0 - 1
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 428 4 0 4 6.0 N#Cc1c(-c2cc(Cl)c3c(ccn3CC3CC3)c2)ccn2c(CC(F)(F)F)cnc12 10.1021/jm201561r
70685763 74613 None 0 Human Functional pEC50 = 7.0 7.0 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 370 7 0 4 4.9 CC(C)CCn1ccc(-c2ccc(OCC3CC3)c(Cl)c2)c(C#N)c1=O 10.1021/jm2016864
CHEMBL2029794 74613 None 0 Human Functional pEC50 = 7.0 7.0 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 370 7 0 4 4.9 CC(C)CCn1ccc(-c2ccc(OCC3CC3)c(Cl)c2)c(C#N)c1=O 10.1021/jm2016864
51357934 61995 None 0 Rat Functional pEC50 = 7.0 7.0 - 1
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 388 3 0 4 4.6 C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(C(F)(F)F)cc1 10.1021/jm101414h
CHEMBL1774227 61995 None 0 Rat Functional pEC50 = 7.0 7.0 - 1
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 388 3 0 4 4.6 C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(C(F)(F)F)cc1 10.1021/jm101414h
9815617 114563 None 3 Rat Functional pEC50 = 6.0 6.0 -1 2
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 203 2 3 3 -0.4 N[C@@]1(C(=O)O)CC[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm000346k
CHEMBL333519 114563 None 3 Rat Functional pEC50 = 6.0 6.0 -1 2
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 203 2 3 3 -0.4 N[C@@]1(C(=O)O)CC[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm000346k
57459485 82667 None 0 Human Functional pEC50 = 6.0 6.0 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 386 4 0 6 3.6 N#Cc1c(N2CCC(c3ccccc3)CC2)ccn2c(CN3CCCC3)nnc12 10.1021/jm3010724
CHEMBL2179312 82667 None 0 Human Functional pEC50 = 6.0 6.0 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 386 4 0 6 3.6 N#Cc1c(N2CCC(c3ccccc3)CC2)ccn2c(CN3CCCC3)nnc12 10.1021/jm3010724
11951989 68049 None 0 Human Functional pEC50 = 6.0 6.0 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 433 11 1 6 5.6 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2C(C)C 10.1016/j.bmcl.2005.06.017
CHEMBL191391 68049 None 0 Human Functional pEC50 = 6.0 6.0 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 433 11 1 6 5.6 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2C(C)C 10.1016/j.bmcl.2005.06.017
70685761 74607 None 0 Human Functional pEC50 = 5.9 5.9 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 296 5 0 4 3.4 COc1ccc(-c2ccn(CCC(C)C)c(=O)c2C#N)cc1 10.1021/jm2016864
CHEMBL2029787 74607 None 0 Human Functional pEC50 = 5.9 5.9 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 296 5 0 4 3.4 COc1ccc(-c2ccn(CCC(C)C)c(=O)c2C#N)cc1 10.1021/jm2016864
49822037 82671 None 0 Human Functional pEC50 = 6.9 6.9 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 412 3 0 4 5.0 FC(F)(F)Cc1nnc2c(Cl)c(N3CCC(F)(c4ccccc4)CC3)ccn12 10.1021/jm3010724
CHEMBL2179316 82671 None 0 Human Functional pEC50 = 6.9 6.9 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 412 3 0 4 5.0 FC(F)(F)Cc1nnc2c(Cl)c(N3CCC(F)(c4ccccc4)CC3)ccn12 10.1021/jm3010724
57459500 82674 None 0 Human Functional pEC50 = 6.9 6.9 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 374 3 0 4 4.7 CCc1nnc2c(C(F)(F)F)c(N3CCC(c4ccccc4)CC3)ccn12 10.1021/jm3010724
CHEMBL2179320 82674 None 0 Human Functional pEC50 = 6.9 6.9 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 374 3 0 4 4.7 CCc1nnc2c(C(F)(F)F)c(N3CCC(c4ccccc4)CC3)ccn12 10.1021/jm3010724
71117470 145770 None 0 Human Functional pEC50 = 6.9 6.9 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 498 5 1 6 4.7 Cc1cccc(S(=O)(=O)NC2CC(c3ccc4c(n3)n(C)c(=O)n4CC(C)(C)C)CCC2(C)C)c1 nan
CHEMBL3916091 145770 None 0 Human Functional pEC50 = 6.9 6.9 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 498 5 1 6 4.7 Cc1cccc(S(=O)(=O)NC2CC(c3ccc4c(n3)n(C)c(=O)n4CC(C)(C)C)CCC2(C)C)c1 nan
25173448 184368 None 0 Human Functional pEC50 = 6.9 6.9 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 303 5 0 3 4.0 O=C1OCCCN1Cc1ccc(OCC2CCCCC2)cc1 10.1016/j.bmcl.2009.03.032
CHEMBL483754 184368 None 0 Human Functional pEC50 = 6.9 6.9 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 303 5 0 3 4.0 O=C1OCCCN1Cc1ccc(OCC2CCCCC2)cc1 10.1016/j.bmcl.2009.03.032
71681826 90095 None 0 Human Functional pEC50 = 5.9 5.9 -1 3
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 293 4 3 4 1.3 N[C@@]1(C(=O)O)C[C@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL2381651 90095 None 0 Human Functional pEC50 = 5.9 5.9 -1 3
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 293 4 3 4 1.3 N[C@@]1(C(=O)O)C[C@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
44155423 8701 None 0 Human Functional pEC50 = 5.9 5.9 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 277 7 0 3 4.0 CCCCCCC1CN(c2ccc(OC)cc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1095750 8701 None 0 Human Functional pEC50 = 5.9 5.9 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 277 7 0 3 4.0 CCCCCCC1CN(c2ccc(OC)cc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
24809653 74609 None 0 Human Functional pEC50 = 5.9 5.9 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 314 5 0 4 3.6 COc1ccc(-c2ccn(CCC(C)C)c(=O)c2C#N)cc1F 10.1021/jm2016864
CHEMBL2029790 74609 None 0 Human Functional pEC50 = 5.9 5.9 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 314 5 0 4 3.6 COc1ccc(-c2ccn(CCC(C)C)c(=O)c2C#N)cc1F 10.1021/jm2016864
11950744 126876 None 0 Human Functional pEC50 = 5.9 5.9 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 463 11 1 6 5.5 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1CCN2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
CHEMBL365440 126876 None 0 Human Functional pEC50 = 5.9 5.9 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 463 11 1 6 5.5 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1CCN2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
71117232 153980 None 0 Human Functional pEC50 = 5.9 5.9 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 398 7 1 7 2.3 Cn1cnc(C(=O)NCCCCc2ccc3c(n2)n(C)c(=O)n3CC(C)(C)C)c1 nan
CHEMBL3983091 153980 None 0 Human Functional pEC50 = 5.9 5.9 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 398 7 1 7 2.3 Cn1cnc(C(=O)NCCCCc2ccc3c(n2)n(C)c(=O)n3CC(C)(C)C)c1 nan
155523303 170938 None 0 Human Functional pEC50 = 6.9 6.9 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 337 3 0 3 4.9 Fc1ccc(-c2ccc(Cn3nnc4ccccc43)cc2)c(Cl)c1 10.1021/acs.jmedchem.8b00161
CHEMBL4453680 170938 None 0 Human Functional pEC50 = 6.9 6.9 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 337 3 0 3 4.9 Fc1ccc(-c2ccc(Cn3nnc4ccccc43)cc2)c(Cl)c1 10.1021/acs.jmedchem.8b00161
46887460 8848 None 0 Human Functional pEC50 = 5.9 5.9 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 337 4 0 3 4.1 O=C1OC(COc2cccc(C(F)(F)F)c2)CN1c1ccccc1 10.1016/j.bmcl.2010.03.089
CHEMBL1097044 8848 None 0 Human Functional pEC50 = 5.9 5.9 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 337 4 0 3 4.1 O=C1OC(COc2cccc(C(F)(F)F)c2)CN1c1ccccc1 10.1016/j.bmcl.2010.03.089
90643858 111929 None 0 Rat Functional pEC50 = 7.9 7.9 25 2
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293A cells by calcium mobilization assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293A cells by calcium mobilization assay
ChEMBL 430 12 2 6 4.9 COc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)CC(C)C)c(O)c1C 10.1021/jm5000563
CHEMBL3287695 111929 None 0 Rat Functional pEC50 = 7.9 7.9 25 2
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293A cells by calcium mobilization assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293A cells by calcium mobilization assay
ChEMBL 430 12 2 6 4.9 COc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)CC(C)C)c(O)c1C 10.1021/jm5000563
156013901 177343 None 0 Human Functional pEC50 = 7.9 7.9 114 2
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 440 8 0 6 4.7 COCCOc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1 10.1021/acs.jmedchem.0c01058
CHEMBL4635729 177343 None 0 Human Functional pEC50 = 7.9 7.9 114 2
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 440 8 0 6 4.7 COCCOc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1 10.1021/acs.jmedchem.0c01058
68109335 157203 None 0 Human Functional pEC50 = 7.9 7.9 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 438 5 0 5 6.5 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2Cl)c(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4074664 157203 None 0 Human Functional pEC50 = 7.9 7.9 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 438 5 0 5 6.5 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2Cl)c(C)n1 10.1021/acs.jmedchem.7b00669
71136640 123469 None 0 Human Functional pEC50 = 7.9 7.9 60 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@@H](Sc2c[nH]nn2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616853 123469 None 0 Human Functional pEC50 = 7.9 7.9 60 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@@H](Sc2c[nH]nn2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
46215878 80839 None 0 Human Functional pEC50 = 6.9 6.9 - 1
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 388 2 0 4 5.1 Cn1ccc2cc(-c3ccn4c(CC(F)(F)F)cnc4c3C#N)cc(Cl)c21 10.1021/jm201561r
CHEMBL2152117 80839 None 0 Human Functional pEC50 = 6.9 6.9 - 1
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 388 2 0 4 5.1 Cn1ccc2cc(-c3ccn4c(CC(F)(F)F)cnc4c3C#N)cc(Cl)c21 10.1021/jm201561r
156012835 177539 None 0 Human Functional pEC50 = 5.9 5.9 -2 2
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 985 30 0 14 8.5 COc1c(OCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4638687 177539 None 0 Human Functional pEC50 = 5.9 5.9 -2 2
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 985 30 0 14 8.5 COc1c(OCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
156016100 177792 None 0 Human Functional pEC50 = 5.9 5.9 -1 2
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 1162 42 0 18 8.6 COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4641860 177792 None 0 Human Functional pEC50 = 5.9 5.9 -1 2
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 1162 42 0 18 8.6 COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
46887271 8692 None 0 Human Functional pEC50 = 5.9 5.9 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 275 8 0 2 4.8 CCCCCCCCC1CN(c2ccccc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1095701 8692 None 0 Human Functional pEC50 = 5.9 5.9 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 275 8 0 2 4.8 CCCCCCCCC1CN(c2ccccc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
156016100 177792 None 0 Human Functional pEC50 = 5.9 5.9 -1 2
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 1162 42 0 18 8.6 COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4641860 177792 None 0 Human Functional pEC50 = 5.9 5.9 -1 2
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 1162 42 0 18 8.6 COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
162669954 182775 None 0 Human Functional pEC50 = 5.9 5.9 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 353 6 0 4 4.0 COc1ccc(CCCCN2CCn3c(nc4ccccc43)C2)c(F)c1 10.1016/j.ejmech.2019.111881
CHEMBL4789052 182775 None 0 Human Functional pEC50 = 5.9 5.9 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 353 6 0 4 4.0 COc1ccc(CCCCN2CCn3c(nc4ccccc43)C2)c(F)c1 10.1016/j.ejmech.2019.111881
44155986 8550 None 0 Human Functional pEC50 = 5.9 5.9 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 305 7 0 4 3.8 CCCCCCC1CN(c2ccc(C(=O)OC)cc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1094462 8550 None 0 Human Functional pEC50 = 5.9 5.9 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 305 7 0 4 3.8 CCCCCCC1CN(c2ccc(C(=O)OC)cc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
71117222 146173 None 0 Human Functional pEC50 = 6.9 6.9 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 441 4 0 7 2.6 Cn1c(=O)n(CC2CC2(F)F)c2ccc(C3=CC4CN(C(=O)c5ncco5)CC4C3)nc21 nan
CHEMBL3919237 146173 None 0 Human Functional pEC50 = 6.9 6.9 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 441 4 0 7 2.6 Cn1c(=O)n(CC2CC2(F)F)c2ccc(C3=CC4CN(C(=O)c5ncco5)CC4C3)nc21 nan
57459655 82665 None 0 Human Functional pEC50 = 5.9 5.9 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 359 2 0 5 4.3 CC(C)(C)c1nnc2c(C#N)c(N3CCC(c4ccccc4)CC3)ccn12 10.1021/jm3010724
CHEMBL2179310 82665 None 0 Human Functional pEC50 = 5.9 5.9 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 359 2 0 5 4.3 CC(C)(C)c1nnc2c(C#N)c(N3CCC(c4ccccc4)CC3)ccn12 10.1021/jm3010724
68107697 82679 None 0 Human Functional pEC50 = 5.9 5.9 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 386 4 0 4 4.7 FC(F)(F)c1c(N2CCC(c3ccccc3)C2)ccn2c(CC3CC3)nnc12 10.1021/jm3010724
CHEMBL2179325 82679 None 0 Human Functional pEC50 = 5.9 5.9 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 386 4 0 4 4.7 FC(F)(F)c1c(N2CCC(c3ccccc3)C2)ccn2c(CC3CC3)nnc12 10.1021/jm3010724
156012835 177539 None 0 Human Functional pEC50 = 5.9 5.9 -2 2
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 985 30 0 14 8.5 COc1c(OCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4638687 177539 None 0 Human Functional pEC50 = 5.9 5.9 -2 2
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 985 30 0 14 8.5 COc1c(OCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
58103861 82686 None 0 Human Functional pEC50 = 6.9 6.9 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 384 3 0 4 4.7 N#Cc1c(N2CCC(c3ccccc3)CC2)ccn2c(CC(F)(F)F)cnc12 10.1021/jm3010724
CHEMBL2179332 82686 None 0 Human Functional pEC50 = 6.9 6.9 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 384 3 0 4 4.7 N#Cc1c(N2CCC(c3ccccc3)CC2)ccn2c(CC(F)(F)F)cnc12 10.1021/jm3010724
90668093 109594 None 0 Human Functional pEC50 = 6.9 6.9 - 1
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 336 7 1 4 4.1 CCCn1ccc2c(NCCc3ccccc3OC)cccc2c1=O 10.1039/C0MD00200C
CHEMBL3221832 109594 None 0 Human Functional pEC50 = 6.9 6.9 - 1
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 336 7 1 4 4.1 CCCn1ccc2c(NCCc3ccccc3OC)cccc2c1=O 10.1039/C0MD00200C
53322147 57741 None 0 Human Functional pEC50 = 5.9 5.9 - 1
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 298 3 0 3 4.1 CCCn1ccc2cc(-c3ccncc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669380 57741 None 0 Human Functional pEC50 = 5.9 5.9 - 1
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 298 3 0 3 4.1 CCCn1ccc2cc(-c3ccncc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
53325451 57760 None 0 Human Functional pEC50 = 5.9 5.9 - 1
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 404 6 0 4 5.7 CCCn1ccc2cc(-c3ccc(OCc4cccnc4)cc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669398 57760 None 0 Human Functional pEC50 = 5.9 5.9 - 1
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 404 6 0 4 5.7 CCCn1ccc2cc(-c3ccc(OCc4cccnc4)cc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
46190878 1872 None 8 Human Functional pEC50 = 5.9 5.9 - 1
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 342 3 0 6 2.3 Clc1cnc(nc1)N1CCN(CC1)Cc1nc2c(n1C)cccc2 10.1016/j.bmcl.2009.11.032
6253 1872 None 8 Human Functional pEC50 = 5.9 5.9 - 1
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 342 3 0 6 2.3 Clc1cnc(nc1)N1CCN(CC1)Cc1nc2c(n1C)cccc2 10.1016/j.bmcl.2009.11.032
CHEMBL595759 1872 None 8 Human Functional pEC50 = 5.9 5.9 - 1
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 342 3 0 6 2.3 Clc1cnc(nc1)N1CCN(CC1)Cc1nc2c(n1C)cccc2 10.1016/j.bmcl.2009.11.032
155548817 173944 None 0 Human Functional pEC50 = 5.9 5.9 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding measured after 1 hr by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding measured after 1 hr by scintillation spectrometry method
ChEMBL 518 6 1 6 5.3 O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
CHEMBL4538850 173944 None 0 Human Functional pEC50 = 5.9 5.9 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding measured after 1 hr by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding measured after 1 hr by scintillation spectrometry method
ChEMBL 518 6 1 6 5.3 O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
90668101 109605 None 0 Human Functional pEC50 = 5.9 5.9 - 1
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 384 7 1 4 5.8 CCCn1ccc2c(NCc3cccc(Oc4ccccc4)c3)cccc2c1=O 10.1039/C0MD00200C
CHEMBL3221842 109605 None 0 Human Functional pEC50 = 5.9 5.9 - 1
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 384 7 1 4 5.8 CCCn1ccc2c(NCc3cccc(Oc4ccccc4)c3)cccc2c1=O 10.1039/C0MD00200C
1310 2315 None 61 Human Functional pEC50 = 4.9 4.9 -389 17
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmcl.2010.12.048
1369 2315 None 61 Human Functional pEC50 = 4.9 4.9 -389 17
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmcl.2010.12.048
33032 2315 None 61 Human Functional pEC50 = 4.9 4.9 -389 17
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmcl.2010.12.048
44272391 2315 None 61 Human Functional pEC50 = 4.9 4.9 -389 17
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmcl.2010.12.048
88747398 2315 None 61 Human Functional pEC50 = 4.9 4.9 -389 17
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmcl.2010.12.048
CHEMBL575060 2315 None 61 Human Functional pEC50 = 4.9 4.9 -389 17
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmcl.2010.12.048
DB00142 2315 None 61 Human Functional pEC50 = 4.9 4.9 -389 17
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmcl.2010.12.048
70694131 74627 None 0 Human Functional pEC50 = 6.9 6.9 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 371 5 0 5 4.7 Cc1cc(Oc2ccc(-c3ccn(CC4CCC4)c(=O)c3C#N)cc2)ccn1 10.1021/jm2016864
CHEMBL2029806 74627 None 0 Human Functional pEC50 = 6.9 6.9 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 371 5 0 5 4.7 Cc1cc(Oc2ccc(-c3ccn(CC4CCC4)c(=O)c3C#N)cc2)ccn1 10.1021/jm2016864
71137012 123467 None 0 Human Functional pEC50 = 7.9 7.9 11 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 299 4 5 7 -1.0 Nc1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
CHEMBL3616851 123467 None 0 Human Functional pEC50 = 7.9 7.9 11 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 299 4 5 7 -1.0 Nc1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
117971683 142393 None 0 Human Functional pEC50 = 7.9 7.9 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 421 6 0 4 5.5 FC(F)(F)c1c(OCC2(c3ccc(Cl)cc3)CC2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
CHEMBL3885312 142393 None 0 Human Functional pEC50 = 7.9 7.9 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 421 6 0 4 5.5 FC(F)(F)c1c(OCC2(c3ccc(Cl)cc3)CC2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
134131394 142401 None 0 Human Functional pEC50 = 7.9 7.9 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 389 6 0 4 5.6 Clc1c(OCc2cccc(-c3ccccc3)c2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
CHEMBL3885396 142401 None 0 Human Functional pEC50 = 7.9 7.9 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 389 6 0 4 5.6 Clc1c(OCc2cccc(-c3ccccc3)c2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
155536450 172282 None 0 Human Functional pEC50 = 7.9 7.9 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 406 3 0 4 5.4 Fc1cc(Cl)ccc1-c1ccc(Cn2nnc3c(C(F)(F)F)cccc32)cn1 10.1021/acs.jmedchem.8b00161
CHEMBL4473537 172282 None 0 Human Functional pEC50 = 7.9 7.9 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 406 3 0 4 5.4 Fc1cc(Cl)ccc1-c1ccc(Cn2nnc3c(C(F)(F)F)cccc32)cn1 10.1021/acs.jmedchem.8b00161
25008958 61984 None 1 Rat Functional pEC50 = 7.9 7.9 - 1
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 404 4 0 5 4.4 COc1cc(C(F)(F)F)ccc1C1CCN(Cc2nc3ncccc3n2C)CC1 10.1021/jm101414h
CHEMBL1774112 61984 None 1 Rat Functional pEC50 = 7.9 7.9 - 1
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 404 4 0 5 4.4 COc1cc(C(F)(F)F)ccc1C1CCN(Cc2nc3ncccc3n2C)CC1 10.1021/jm101414h
50992248 166637 None 0 Human Functional pEC50 = 7.9 7.9 1 2
Positive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis
ChEMBL 376 5 0 5 3.9 CCc1cn2c(nc1=O)O[C@H](COc1ccc(-c3cccc(C)c3C)cc1)C2 10.1016/j.bmcl.2018.08.022
CHEMBL4279401 166637 None 0 Human Functional pEC50 = 7.9 7.9 1 2
Positive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis
ChEMBL 376 5 0 5 3.9 CCc1cn2c(nc1=O)O[C@H](COc1ccc(-c3cccc(C)c3C)cc1)C2 10.1016/j.bmcl.2018.08.022
71137010 123465 None 0 Human Functional pEC50 = 7.9 7.9 5 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 352 4 4 6 0.4 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc(C(F)(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616849 123465 None 0 Human Functional pEC50 = 7.9 7.9 5 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 352 4 4 6 0.4 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc(C(F)(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
162651557 180291 None 0 Human Functional pEC50 = 6.9 6.9 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 319 6 0 3 4.3 c1ccc(CCCCCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
CHEMBL4749289 180291 None 0 Human Functional pEC50 = 6.9 6.9 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 319 6 0 3 4.3 c1ccc(CCCCCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
24815439 204392 None 1 Human Functional pEC50 = 6.9 6.9 -18 2
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 323 3 0 3 4.1 Cn1c(CN2CCC(c3ccccc3F)CC2)nc2ccccc21 10.1016/j.ejmech.2019.111881
CHEMBL607689 204392 None 1 Human Functional pEC50 = 6.9 6.9 -18 2
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 323 3 0 3 4.1 Cn1c(CN2CCC(c3ccccc3F)CC2)nc2ccccc21 10.1016/j.ejmech.2019.111881
46887273 8694 None 3 Human Functional pEC50 = 5.9 5.9 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 219 4 0 2 3.2 CCCCC1CN(c2ccccc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1095703 8694 None 3 Human Functional pEC50 = 5.9 5.9 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 219 4 0 2 3.2 CCCCC1CN(c2ccccc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
6604704 101455 None 23 Human Functional pEC50 = 4.9 4.9 2 3
Agonist activity against Metabotropic glutamate receptor 2 expressed in HEK 293 cells was evaluated by measuring total inositol phosphate accumulationAgonist activity against Metabotropic glutamate receptor 2 expressed in HEK 293 cells was evaluated by measuring total inositol phosphate accumulation
ChEMBL 173 2 3 3 -0.3 N[C@@]1(C(=O)O)CC[C@H](C(=O)O)C1 10.1021/jm970207b
CHEMBL29726 101455 None 23 Human Functional pEC50 = 4.9 4.9 2 3
Agonist activity against Metabotropic glutamate receptor 2 expressed in HEK 293 cells was evaluated by measuring total inositol phosphate accumulationAgonist activity against Metabotropic glutamate receptor 2 expressed in HEK 293 cells was evaluated by measuring total inositol phosphate accumulation
ChEMBL 173 2 3 3 -0.3 N[C@@]1(C(=O)O)CC[C@H](C(=O)O)C1 10.1021/jm970207b
1310 2315 None 61 Rat Functional pEC50 = 4.9 4.9 -457 17
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
1369 2315 None 61 Rat Functional pEC50 = 4.9 4.9 -457 17
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
33032 2315 None 61 Rat Functional pEC50 = 4.9 4.9 -457 17
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
44272391 2315 None 61 Rat Functional pEC50 = 4.9 4.9 -457 17
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
88747398 2315 None 61 Rat Functional pEC50 = 4.9 4.9 -457 17
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
CHEMBL575060 2315 None 61 Rat Functional pEC50 = 4.9 4.9 -457 17
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
DB00142 2315 None 61 Rat Functional pEC50 = 4.9 4.9 -457 17
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
44397878 124468 None 0 Human Functional pEC50 = 6.9 6.9 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 389 6 1 5 5.6 CCCc1c(Oc2cccc(-c3nnn[nH]3)c2)ccc2c1ccn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
CHEMBL363945 124468 None 0 Human Functional pEC50 = 6.9 6.9 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 389 6 1 5 5.6 CCCc1c(Oc2cccc(-c3nnn[nH]3)c2)ccc2c1ccn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
71116730 149150 None 0 Human Functional pEC50 = 6.9 6.9 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 424 3 1 6 2.6 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)C5(O)CCC5)CC4C3)nc21 nan
CHEMBL3942904 149150 None 0 Human Functional pEC50 = 6.9 6.9 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 424 3 1 6 2.6 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)C5(O)CCC5)CC4C3)nc21 nan
44155989 8549 None 0 Human Functional pEC50 = 5.9 5.9 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 305 7 0 4 3.8 CCCCCCC1CN(c2cccc(C(=O)OC)c2)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1094461 8549 None 0 Human Functional pEC50 = 5.9 5.9 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 305 7 0 4 3.8 CCCCCCC1CN(c2cccc(C(=O)OC)c2)C(=O)O1 10.1016/j.bmcl.2010.03.089
25073615 166559 None 0 Human Functional pEC50 = 5.9 5.9 -4 2
Positive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis
ChEMBL 300 3 0 5 2.4 CC(C)(C)c1ccc(OC[C@@H]2Cn3ccc(=O)nc3O2)cc1 10.1016/j.bmcl.2018.08.022
CHEMBL4278070 166559 None 0 Human Functional pEC50 = 5.9 5.9 -4 2
Positive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis
ChEMBL 300 3 0 5 2.4 CC(C)(C)c1ccc(OC[C@@H]2Cn3ccc(=O)nc3O2)cc1 10.1016/j.bmcl.2018.08.022
11951270 67347 None 0 Human Functional pEC50 = 5.9 5.9 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 433 9 1 6 5.3 CCCc1c(OCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
CHEMBL188455 67347 None 0 Human Functional pEC50 = 5.9 5.9 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 433 9 1 6 5.3 CCCc1c(OCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
156817945 190593 None 0 Human Functional pEC50 = 6.9 6.9 - 1
Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay
ChEMBL 451 5 0 5 4.3 Fc1ccc(N2CCN(Cc3cc(C(F)(F)F)cn4c(CC5CC5)nnc34)CC2)c(F)c1 10.1021/acs.jmedchem.2c00593
CHEMBL5179002 190593 None 0 Human Functional pEC50 = 6.9 6.9 - 1
Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay
ChEMBL 451 5 0 5 4.3 Fc1ccc(N2CCN(Cc3cc(C(F)(F)F)cn4c(CC5CC5)nnc34)CC2)c(F)c1 10.1021/acs.jmedchem.2c00593
162676513 183619 None 0 Human Functional pEC50 = 5.9 5.9 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 291 4 0 3 3.5 c1ccc(CCCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
CHEMBL4799794 183619 None 0 Human Functional pEC50 = 5.9 5.9 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 291 4 0 3 3.5 c1ccc(CCCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
70689928 74633 None 0 Human Functional pEC50 = 6.9 6.9 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 373 6 0 5 5.0 CCCCn1ccc(-c2ccc(Oc3ccc(C)nc3C)cc2)c(C#N)c1=O 10.1021/jm2016864
CHEMBL2029812 74633 None 0 Human Functional pEC50 = 6.9 6.9 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 373 6 0 5 5.0 CCCCn1ccc(-c2ccc(Oc3ccc(C)nc3C)cc2)c(C#N)c1=O 10.1021/jm2016864
46887493 8586 None 0 Human Functional pEC50 = 4.9 4.9 - 1
Agonist activity at human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by LIPR assayAgonist activity at human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by LIPR assay
ChEMBL 247 6 0 2 4.0 CCCCCC[C@@H]1CN(c2ccccc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1094762 8586 None 0 Human Functional pEC50 = 4.9 4.9 - 1
Agonist activity at human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by LIPR assayAgonist activity at human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by LIPR assay
ChEMBL 247 6 0 2 4.0 CCCCCC[C@@H]1CN(c2ccccc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
162674797 183574 None 0 Human Functional pEC50 = 5.9 5.9 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 295 3 0 3 3.2 Fc1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
CHEMBL4799164 183574 None 0 Human Functional pEC50 = 5.9 5.9 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 295 3 0 3 3.2 Fc1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
155562956 175281 None 0 Human Functional pEC50 = 7.9 7.9 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 365 2 0 3 4.0 Brc1ccc(Cn2nnc3c(Br)cccc32)cc1 10.1021/acs.jmedchem.8b00161
CHEMBL4570470 175281 None 0 Human Functional pEC50 = 7.9 7.9 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 365 2 0 3 4.0 Brc1ccc(Cn2nnc3c(Br)cccc32)cc1 10.1021/acs.jmedchem.8b00161
67060162 167059 None 0 Human Functional pEC50 = 7.9 7.9 - 1
Positive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis
ChEMBL 362 4 0 5 3.7 Cc1cccc(-c2ccc(OC[C@@H]3Cn4cc(C)c(=O)nc4O3)cc2)c1C 10.1016/j.bmcl.2018.08.022
CHEMBL4287326 167059 None 0 Human Functional pEC50 = 7.9 7.9 - 1
Positive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis
ChEMBL 362 4 0 5 3.7 Cc1cccc(-c2ccc(OC[C@@H]3Cn4cc(C)c(=O)nc4O3)cc2)c1C 10.1016/j.bmcl.2018.08.022
71116701 144947 None 0 Human Functional pEC50 = 7.8 7.8 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 387 4 1 4 2.4 CC1C(c2ccc3c(n2)N(C)S(=O)(=O)N3CC2CC2(F)F)C1C(C)(C)O nan
CHEMBL3909811 144947 None 0 Human Functional pEC50 = 7.8 7.8 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 387 4 1 4 2.4 CC1C(c2ccc3c(n2)N(C)S(=O)(=O)N3CC2CC2(F)F)C1C(C)(C)O nan
146036860 173382 None 6 Human Functional pEC50 = 6.9 6.9 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 253 2 0 3 2.9 CC(C)Cn1nnc2c(Br)cccc21 10.1021/acs.jmedchem.8b00161
CHEMBL4525401 173382 None 6 Human Functional pEC50 = 6.9 6.9 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 253 2 0 3 2.9 CC(C)Cn1nnc2c(Br)cccc21 10.1021/acs.jmedchem.8b00161
155552571 174260 None 0 Human Functional pEC50 = 6.9 6.9 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 319 2 0 3 3.6 FC(F)(F)c1cc(Br)c2nnn(CC3CC3)c2c1 10.1021/acs.jmedchem.8b00161
CHEMBL4546739 174260 None 0 Human Functional pEC50 = 6.9 6.9 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 319 2 0 3 3.6 FC(F)(F)c1cc(Br)c2nnn(CC3CC3)c2c1 10.1021/acs.jmedchem.8b00161
118714748 114634 None 0 Human Functional pEC50 = 6.9 6.9 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 351 4 0 4 3.7 N#Cc1c(N2CCC(c3cccc(F)c3)CC2)ccn(CC2CC2)c1=O 10.1021/jm500496m
CHEMBL3337514 114634 None 0 Human Functional pEC50 = 6.9 6.9 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 351 4 0 4 3.7 N#Cc1c(N2CCC(c3cccc(F)c3)CC2)ccn(CC2CC2)c1=O 10.1021/jm500496m
155519836 170473 None 0 Human Functional pEC50 = 6.9 6.9 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 338 3 0 4 4.3 Fc1cc(Cl)ccc1-c1ccc(Cn2nnc3ccccc32)nc1 10.1021/acs.jmedchem.8b00161
CHEMBL4447702 170473 None 0 Human Functional pEC50 = 6.9 6.9 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 338 3 0 4 4.3 Fc1cc(Cl)ccc1-c1ccc(Cn2nnc3ccccc32)nc1 10.1021/acs.jmedchem.8b00161
46227787 202149 None 0 Human Functional pEC50 = 6.9 6.9 - 1
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 390 4 1 4 5.2 N#Cc1c(-c2ccc(NC3CC3)c(Cl)c2)ccn2c(CC(F)(F)F)cnc12 10.1016/j.bmcl.2009.11.008
CHEMBL593168 202149 None 0 Human Functional pEC50 = 6.9 6.9 - 1
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 390 4 1 4 5.2 N#Cc1c(-c2ccc(NC3CC3)c(Cl)c2)ccn2c(CC(F)(F)F)cnc12 10.1016/j.bmcl.2009.11.008
25173776 184408 None 0 Human Functional pEC50 = 6.9 6.9 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 267 3 0 2 3.7 C[C@@H]1CN(Cc2ccc(-c3ccccc3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL484128 184408 None 0 Human Functional pEC50 = 6.9 6.9 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 267 3 0 2 3.7 C[C@@H]1CN(Cc2ccc(-c3ccccc3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
59599515 148235 None 0 Human Functional pEC50 = 5.8 5.8 -10 2
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 421 9 2 6 5.0 CCCc1c(OCc2ccc(Oc3ccc(C(=O)O)cn3)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2016.11.049
CHEMBL3935529 148235 None 0 Human Functional pEC50 = 5.8 5.8 -10 2
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 421 9 2 6 5.0 CCCc1c(OCc2ccc(Oc3ccc(C(=O)O)cn3)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2016.11.049
24815882 61977 None 0 Rat Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 339 3 0 3 4.6 Cn1c(CN2CCC(c3ccccc3Cl)CC2)nc2ccccc21 10.1021/jm101414h
CHEMBL1774104 61977 None 0 Rat Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 339 3 0 3 4.6 Cn1c(CN2CCC(c3ccccc3Cl)CC2)nc2ccccc21 10.1021/jm101414h
71137008 123471 None 0 Human Functional pEC50 = 6.8 6.8 7 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 298 4 4 6 -0.3 Cc1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
CHEMBL3616855 123471 None 0 Human Functional pEC50 = 6.8 6.8 7 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 298 4 4 6 -0.3 Cc1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
25195461 2144 None 42 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/jm500496m
8946 2144 None 42 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/jm500496m
CHEMBL3337527 2144 None 42 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/jm500496m
DB12059 2144 None 42 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/jm500496m
68109272 158710 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 416 5 1 5 5.2 Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CCOCC1 10.1021/acs.jmedchem.7b00669
CHEMBL4092275 158710 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 416 5 1 5 5.2 Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CCOCC1 10.1021/acs.jmedchem.7b00669
70689926 74625 None 0 Human Functional pEC50 = 5.8 5.8 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 358 6 1 5 4.6 CC(C)CCn1ccc(-c2ccc(Nc3ccncc3)cc2)c(C#N)c1=O 10.1021/jm2016864
CHEMBL2029804 74625 None 0 Human Functional pEC50 = 5.8 5.8 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 358 6 1 5 4.6 CC(C)CCn1ccc(-c2ccc(Nc3ccncc3)cc2)c(C#N)c1=O 10.1021/jm2016864
70977933 171407 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 241 2 0 3 2.9 FC(F)(F)c1cccc2c1nnn2CC1CC1 10.1021/acs.jmedchem.8b00161
CHEMBL4460927 171407 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 241 2 0 3 2.9 FC(F)(F)c1cccc2c1nnn2CC1CC1 10.1021/acs.jmedchem.8b00161
57459517 82677 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 372 3 0 4 4.3 FC(F)(F)c1c(N2CCc3ccccc3C2)ccn2c(CC3CC3)nnc12 10.1021/jm3010724
CHEMBL2179323 82677 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 372 3 0 4 4.3 FC(F)(F)c1c(N2CCc3ccccc3C2)ccn2c(CC3CC3)nnc12 10.1021/jm3010724
25173286 172797 None 0 Human Functional pEC50 = 7.8 7.8 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 303 5 0 3 4.0 CC1CN(Cc2ccc(OCC3CCCCC3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL450207 172797 None 0 Human Functional pEC50 = 7.8 7.8 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 303 5 0 3 4.0 CC1CN(Cc2ccc(OCC3CCCCC3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
155534303 172047 None 0 Human Functional pEC50 = 7.8 7.8 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 305 2 0 3 3.4 Fc1ccc(Cn2nnc3c(Br)cccc32)cc1 10.1021/acs.jmedchem.8b00161
CHEMBL4470447 172047 None 0 Human Functional pEC50 = 7.8 7.8 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 305 2 0 3 3.4 Fc1ccc(Cn2nnc3c(Br)cccc32)cc1 10.1021/acs.jmedchem.8b00161
155567633 176104 None 0 Human Functional pEC50 = 7.8 7.8 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry method
ChEMBL 532 7 1 6 5.0 O=C(NCc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
CHEMBL4589377 176104 None 0 Human Functional pEC50 = 7.8 7.8 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry method
ChEMBL 532 7 1 6 5.0 O=C(NCc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
66785780 158836 None 0 Human Functional pEC50 = 7.8 7.8 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 453 7 1 6 5.4 COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2)cn1 10.1021/acs.jmedchem.7b00669
CHEMBL4093657 158836 None 0 Human Functional pEC50 = 7.8 7.8 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 453 7 1 6 5.4 COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2)cn1 10.1021/acs.jmedchem.7b00669
58103890 80842 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 457 4 2 4 6.1 O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC(F)(F)F)cnc4c3Cl)cc2Cl)CC1 10.1021/jm201561r
CHEMBL2152120 80842 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 457 4 2 4 6.1 O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC(F)(F)F)cnc4c3Cl)cc2Cl)CC1 10.1021/jm201561r
11531870 64334 None 0 Human Functional pEC50 = 5.8 5.8 - 1
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 420 10 1 4 5.6 CC(C)CC(=O)c1ccc(OCCCCOc2ccccc2)c(Br)c1O 10.1016/j.bmcl.2004.09.028
CHEMBL181089 64334 None 0 Human Functional pEC50 = 5.8 5.8 - 1
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 420 10 1 4 5.6 CC(C)CC(=O)c1ccc(OCCCCOc2ccccc2)c(Br)c1O 10.1016/j.bmcl.2004.09.028
59234231 2143 None 4 Human Functional pEC50 = 6.8 6.8 -1 2
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 10.1021/jm500496m
6330 2143 None 4 Human Functional pEC50 = 6.8 6.8 -1 2
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 10.1021/jm500496m
6331 2143 None 4 Human Functional pEC50 = 6.8 6.8 -1 2
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 10.1021/jm500496m
CHEMBL3337510 2143 None 4 Human Functional pEC50 = 6.8 6.8 -1 2
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 10.1021/jm500496m
118714757 114643 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 369 4 0 4 3.8 N#Cc1c(N2CCC(c3cc(F)cc(F)c3)CC2)ccn(CC2CC2)c1=O 10.1021/jm500496m
CHEMBL3337523 114643 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 369 4 0 4 3.8 N#Cc1c(N2CCC(c3cc(F)cc(F)c3)CC2)ccn(CC2CC2)c1=O 10.1021/jm500496m
66785393 156986 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 419 7 1 6 5.0 COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2)cn1 10.1021/acs.jmedchem.7b00669
CHEMBL4072134 156986 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 419 7 1 6 5.0 COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2)cn1 10.1021/acs.jmedchem.7b00669
9815616 114864 None 4 Human Functional pEC50 = 6.8 6.8 -2 4
Agonist activity at human mGlu2 receptor expressed in CHO cell membranes by GTPgammaS binding assayAgonist activity at human mGlu2 receptor expressed in CHO cell membranes by GTPgammaS binding assay
ChEMBL 203 2 3 3 -0.5 N[C@@]1(C(=O)O)[C@@H](F)C[C@H]2[C@H](C(=O)O)[C@H]21 10.1016/j.ejmech.2020.112521
CHEMBL334014 114864 None 4 Human Functional pEC50 = 6.8 6.8 -2 4
Agonist activity at human mGlu2 receptor expressed in CHO cell membranes by GTPgammaS binding assayAgonist activity at human mGlu2 receptor expressed in CHO cell membranes by GTPgammaS binding assay
ChEMBL 203 2 3 3 -0.5 N[C@@]1(C(=O)O)[C@@H](F)C[C@H]2[C@H](C(=O)O)[C@H]21 10.1016/j.ejmech.2020.112521
11530877 64899 None 0 Human Functional pEC50 = 5.8 5.8 - 1
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 373 10 1 5 5.3 Cc1c(OCCCCSc2ccccn2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
CHEMBL182166 64899 None 0 Human Functional pEC50 = 5.8 5.8 - 1
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 373 10 1 5 5.3 Cc1c(OCCCCSc2ccccn2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
9815616 114864 None 4 Rat Functional pEC50 = 6.8 6.8 -2 4
Agonist activity at rat mGlu2 receptor expressed in CHO cell membranes by GTPgammaS binding assayAgonist activity at rat mGlu2 receptor expressed in CHO cell membranes by GTPgammaS binding assay
ChEMBL 203 2 3 3 -0.5 N[C@@]1(C(=O)O)[C@@H](F)C[C@H]2[C@H](C(=O)O)[C@H]21 10.1016/j.ejmech.2020.112521
CHEMBL334014 114864 None 4 Rat Functional pEC50 = 6.8 6.8 -2 4
Agonist activity at rat mGlu2 receptor expressed in CHO cell membranes by GTPgammaS binding assayAgonist activity at rat mGlu2 receptor expressed in CHO cell membranes by GTPgammaS binding assay
ChEMBL 203 2 3 3 -0.5 N[C@@]1(C(=O)O)[C@@H](F)C[C@H]2[C@H](C(=O)O)[C@H]21 10.1016/j.ejmech.2020.112521
156014194 177315 None 0 Human Functional pEC50 = 5.8 5.8 -2 2
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 941 27 0 13 8.5 COc1c(OCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4635373 177315 None 0 Human Functional pEC50 = 5.8 5.8 -2 2
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 941 27 0 13 8.5 COc1c(OCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
156018860 178019 None 0 Human Functional pEC50 = 5.8 5.8 -2 2
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 1074 36 0 16 8.6 COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4645193 178019 None 0 Human Functional pEC50 = 5.8 5.8 -2 2
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 1074 36 0 16 8.6 COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
7504549 171614 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 285 3 0 3 4.1 c1ccc(-c2ccc(Cn3nnc4ccccc43)cc2)cc1 10.1021/acs.jmedchem.8b00161
CHEMBL4464043 171614 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 285 3 0 3 4.1 c1ccc(-c2ccc(Cn3nnc4ccccc43)cc2)cc1 10.1021/acs.jmedchem.8b00161
71462632 82684 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 344 4 0 4 4.5 CCCc1cnc2c(C#N)c(N3CCC(c4ccccc4)CC3)ccn12 10.1021/jm3010724
CHEMBL2179330 82684 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 344 4 0 4 4.5 CCCc1cnc2c(C#N)c(N3CCC(c4ccccc4)CC3)ccn12 10.1021/jm3010724
168299101 192859 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding
ChEMBL 372 7 0 6 3.8 CCCCn1ccn2c(-c3ccc(OCC4CC4)c(Cl)c3)nnc2c1=O 10.1021/acs.jmedchem.2c00969
CHEMBL5220917 192859 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding
ChEMBL 372 7 0 6 3.8 CCCCn1ccn2c(-c3ccc(OCC4CC4)c(Cl)c3)nnc2c1=O 10.1021/acs.jmedchem.2c00969
44591744 188772 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 301 3 0 2 4.3 C[C@@H]1CN(Cc2ccc(-c3cccc(Cl)c3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL503697 188772 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 301 3 0 2 4.3 C[C@@H]1CN(Cc2ccc(-c3cccc(Cl)c3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
156020355 178133 None 0 Human Functional pEC50 = 6.8 6.8 104 2
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 396 5 0 5 4.7 COc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1 10.1021/acs.jmedchem.0c01058
CHEMBL4646835 178133 None 0 Human Functional pEC50 = 6.8 6.8 104 2
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 396 5 0 5 4.7 COc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1 10.1021/acs.jmedchem.0c01058
53321493 57759 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 390 5 0 4 5.9 CCCn1ccc2cc(-c3ccc(Oc4ccncc4)cc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669397 57759 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 390 5 0 4 5.9 CCCn1ccc2cc(-c3ccc(Oc4ccncc4)cc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
46227786 202301 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 407 5 0 4 5.6 N#Cc1c(-c2ccc(OCc3ccccc3)cc2)ccn2c(CC(F)(F)F)cnc12 10.1016/j.bmcl.2009.11.008
CHEMBL594334 202301 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 407 5 0 4 5.6 N#Cc1c(-c2ccc(OCc3ccccc3)cc2)ccn2c(CC(F)(F)F)cnc12 10.1016/j.bmcl.2009.11.008
155533313 171955 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry method
ChEMBL 518 6 1 6 5.3 O=C(Nc1cccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)c1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
CHEMBL4468977 171955 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry method
ChEMBL 518 6 1 6 5.3 O=C(Nc1cccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)c1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
155548817 173944 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry method
ChEMBL 518 6 1 6 5.3 O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
CHEMBL4538850 173944 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry method
ChEMBL 518 6 1 6 5.3 O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
90668097 109600 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 320 7 1 3 4.5 CCCn1ccc2c(NCCCc3ccccc3)cccc2c1=O 10.1039/C0MD00200C
CHEMBL3221838 109600 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 320 7 1 3 4.5 CCCn1ccc2c(NCCCc3ccccc3)cccc2c1=O 10.1039/C0MD00200C
68109333 157721 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 459 4 1 5 5.5 O[C@H]1CC[C@H](Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4081244 157721 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 459 4 1 5 5.5 O[C@H]1CC[C@H](Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
53323491 57744 None 0 Human Functional pEC50 = 5.8 5.8 - 1
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 287 3 1 3 3.5 CCCn1ccc2cc(-c3cn[nH]c3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669383 57744 None 0 Human Functional pEC50 = 5.8 5.8 - 1
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 287 3 1 3 3.5 CCCn1ccc2cc(-c3cn[nH]c3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
24815355 61976 None 0 Rat Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 323 3 0 3 4.1 Cn1c(CN2CCC(c3ccc(F)cc3)CC2)nc2ccccc21 10.1021/jm101414h
CHEMBL1774103 61976 None 0 Rat Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 323 3 0 3 4.1 Cn1c(CN2CCC(c3ccc(F)cc3)CC2)nc2ccccc21 10.1021/jm101414h
51030965 167246 None 0 Human Functional pEC50 = 6.8 6.8 1 2
Positive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis
ChEMBL 312 3 0 5 2.3 CC1(C)CCc2cc(OC[C@@H]3Cn4ccc(=O)nc4O3)ccc21 10.1016/j.bmcl.2018.08.022
CHEMBL4290744 167246 None 0 Human Functional pEC50 = 6.8 6.8 1 2
Positive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis
ChEMBL 312 3 0 5 2.3 CC1(C)CCc2cc(OC[C@@H]3Cn4ccc(=O)nc4O3)ccc21 10.1016/j.bmcl.2018.08.022
60096246 156037 None 0 Human Functional pEC50 = 7.8 7.8 -6 2
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 334 5 4 5 -0.1 COc1ccc(C(=O)N[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)cc1 10.1021/acs.jmedchem.7b01481
CHEMBL4061162 156037 None 0 Human Functional pEC50 = 7.8 7.8 -6 2
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 334 5 4 5 -0.1 COc1ccc(C(=O)N[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)cc1 10.1021/acs.jmedchem.7b01481
117972153 142389 None 0 Human Functional pEC50 = 7.8 7.8 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 405 6 0 4 5.0 Fc1ccc(C2(COc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)cc1 10.1016/j.bmc.2016.11.018
CHEMBL3885265 142389 None 0 Human Functional pEC50 = 7.8 7.8 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 405 6 0 4 5.0 Fc1ccc(C2(COc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)cc1 10.1016/j.bmc.2016.11.018
49822115 2146 None 24 Human Functional pEC50 = 7.8 7.8 - 1
Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding
ChEMBL 414 5 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.2c00969
8947 2146 None 24 Human Functional pEC50 = 7.8 7.8 - 1
Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding
ChEMBL 414 5 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.2c00969
CHEMBL3947764 2146 None 24 Human Functional pEC50 = 7.8 7.8 - 1
Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding
ChEMBL 414 5 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.2c00969
71136746 148688 None 0 Human Functional pEC50 = 7.8 7.8 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 421 3 0 7 3.1 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3ccon3)nc21 nan
CHEMBL3939174 148688 None 0 Human Functional pEC50 = 7.8 7.8 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 421 3 0 7 3.1 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3ccon3)nc21 nan
71136655 123468 None 0 Human Functional pEC50 = 7.8 7.8 12 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 326 5 4 6 0.5 CC(C)c1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
CHEMBL3616852 123468 None 0 Human Functional pEC50 = 7.8 7.8 12 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 326 5 4 6 0.5 CC(C)c1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
9815617 114563 None 3 Rat Functional pEC50 = 7.8 7.8 -1 2
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 203 2 3 3 -0.4 N[C@@]1(C(=O)O)CC[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm000346k
CHEMBL333519 114563 None 3 Rat Functional pEC50 = 7.8 7.8 -1 2
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 203 2 3 3 -0.4 N[C@@]1(C(=O)O)CC[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm000346k
46215704 80841 None 0 Human Functional pEC50 = 6.8 6.8 33 2
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 447 3 1 4 6.2 O[C@H]1CC[C@H](n2ccc3cc(-c4ccn5c(CC(F)(F)F)cnc5c4Cl)ccc32)CC1 10.1021/jm201561r
CHEMBL2152119 80841 None 0 Human Functional pEC50 = 6.8 6.8 33 2
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 447 3 1 4 6.2 O[C@H]1CC[C@H](n2ccc3cc(-c4ccn5c(CC(F)(F)F)cnc5c4Cl)ccc32)CC1 10.1021/jm201561r
156020355 178133 None 0 Human Functional pEC50 = 6.8 6.8 104 2
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 396 5 0 5 4.7 COc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1 10.1021/acs.jmedchem.0c01058
CHEMBL4646835 178133 None 0 Human Functional pEC50 = 6.8 6.8 104 2
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 396 5 0 5 4.7 COc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1 10.1021/acs.jmedchem.0c01058
156014194 177315 None 0 Human Functional pEC50 = 5.8 5.8 -2 2
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 941 27 0 13 8.5 COc1c(OCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4635373 177315 None 0 Human Functional pEC50 = 5.8 5.8 -2 2
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 941 27 0 13 8.5 COc1c(OCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
156018860 178019 None 0 Human Functional pEC50 = 5.8 5.8 -2 2
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 1074 36 0 16 8.6 COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4645193 178019 None 0 Human Functional pEC50 = 5.8 5.8 -2 2
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 1074 36 0 16 8.6 COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
10976811 109769 None 0 Rat Functional pEC50 = 4.8 4.8 - 1
Activity tested at cloned rat mGluR2 receptor expressed in Chinese Hamster Ovary (CHO) cellsActivity tested at cloned rat mGluR2 receptor expressed in Chinese Hamster Ovary (CHO) cells
ChEMBL 214 2 3 5 -1.0 N[C@]1(C(=O)O)C[C@@H]2ON=C(C(=O)O)[C@@H]2C1 10.1021/jm0308085
CHEMBL322887 109769 None 0 Rat Functional pEC50 = 4.8 4.8 - 1
Activity tested at cloned rat mGluR2 receptor expressed in Chinese Hamster Ovary (CHO) cellsActivity tested at cloned rat mGluR2 receptor expressed in Chinese Hamster Ovary (CHO) cells
ChEMBL 214 2 3 5 -1.0 N[C@]1(C(=O)O)C[C@@H]2ON=C(C(=O)O)[C@@H]2C1 10.1021/jm0308085
1310 2315 None 61 Rat Functional pEC50 = 4.8 4.8 -457 17
Agonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cellsAgonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/s0960-894x(01)00158-5
1369 2315 None 61 Rat Functional pEC50 = 4.8 4.8 -457 17
Agonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cellsAgonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/s0960-894x(01)00158-5
33032 2315 None 61 Rat Functional pEC50 = 4.8 4.8 -457 17
Agonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cellsAgonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/s0960-894x(01)00158-5
44272391 2315 None 61 Rat Functional pEC50 = 4.8 4.8 -457 17
Agonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cellsAgonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/s0960-894x(01)00158-5
88747398 2315 None 61 Rat Functional pEC50 = 4.8 4.8 -457 17
Agonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cellsAgonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/s0960-894x(01)00158-5
CHEMBL575060 2315 None 61 Rat Functional pEC50 = 4.8 4.8 -457 17
Agonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cellsAgonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/s0960-894x(01)00158-5
DB00142 2315 None 61 Rat Functional pEC50 = 4.8 4.8 -457 17
Agonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cellsAgonist activity in rat at Metabotropic glutamate receptor 2 expressed in HEK293 cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/s0960-894x(01)00158-5
11310142 2422 None 14 Human Functional pEC50 = 6.8 6.8 13 3
Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor
ChEMBL 199 2 3 3 -0.2 C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O 10.1021/jm040222y
11614 2422 None 14 Human Functional pEC50 = 6.8 6.8 13 3
Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor
ChEMBL 199 2 3 3 -0.2 C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O 10.1021/jm040222y
CHEMBL192051 2422 None 14 Human Functional pEC50 = 6.8 6.8 13 3
Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor
ChEMBL 199 2 3 3 -0.2 C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O 10.1021/jm040222y
51357397 61978 None 0 Rat Functional pEC50 = 5.8 5.8 - 1
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 330 3 0 4 3.8 Cn1c(CN2CCC(c3cccc(C#N)c3)CC2)nc2ccccc21 10.1021/jm101414h
CHEMBL1774105 61978 None 0 Rat Functional pEC50 = 5.8 5.8 - 1
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 330 3 0 4 3.8 Cn1c(CN2CCC(c3cccc(C#N)c3)CC2)nc2ccccc21 10.1021/jm101414h
70696263 74636 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 393 6 0 5 5.3 CCCCn1ccc(-c2ccc(Oc3ccnc(C)c3)c(Cl)c2)c(C#N)c1=O 10.1021/jm2016864
CHEMBL2029815 74636 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 393 6 0 5 5.3 CCCCn1ccc(-c2ccc(Oc3ccnc(C)c3)c(Cl)c2)c(C#N)c1=O 10.1021/jm2016864
49822116 147080 None 14 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP AssayPositive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP Assay
ChEMBL 451 5 0 5 4.3 Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.2c00593
CHEMBL3926416 147080 None 14 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP AssayPositive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP Assay
ChEMBL 451 5 0 5 4.3 Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.2c00593
168299087 192851 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding
ChEMBL 320 4 1 4 3.8 CCCCn1ccn2c(-c3ccc4[nH]ccc4c3)c(C)nc2c1=O 10.1021/acs.jmedchem.2c00969
CHEMBL5220552 192851 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding
ChEMBL 320 4 1 4 3.8 CCCCn1ccn2c(-c3ccc4[nH]ccc4c3)c(C)nc2c1=O 10.1021/acs.jmedchem.2c00969
46216056 80833 None 0 Human Functional pEC50 = 5.8 5.8 - 1
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 358 2 1 5 3.8 N#Cc1c(-c2ccc3c(c2)OCCN3)ccn2c(CC(F)(F)F)cnc12 10.1021/jm201561r
CHEMBL2152110 80833 None 0 Human Functional pEC50 = 5.8 5.8 - 1
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 358 2 1 5 3.8 N#Cc1c(-c2ccc3c(c2)OCCN3)ccn2c(CC(F)(F)F)cnc12 10.1021/jm201561r
25008437 61981 None 0 Rat Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 374 3 0 4 4.4 Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2cnccc21 10.1021/jm101414h
CHEMBL1774109 61981 None 0 Rat Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 374 3 0 4 4.4 Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2cnccc21 10.1021/jm101414h
117972044 142370 None 0 Human Functional pEC50 = 7.8 7.8 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 347 5 0 4 4.6 Clc1cccc(COc2ccn3c(CC4CC4)nnc3c2Cl)c1 10.1016/j.bmc.2016.11.018
CHEMBL3885097 142370 None 0 Human Functional pEC50 = 7.8 7.8 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 347 5 0 4 4.6 Clc1cccc(COc2ccn3c(CC4CC4)nnc3c2Cl)c1 10.1016/j.bmc.2016.11.018
155566740 175989 None 0 Human Functional pEC50 = 7.8 7.8 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 321 2 0 3 3.9 Clc1ccc(Cn2nnc3c(Br)cccc32)cc1 10.1021/acs.jmedchem.8b00161
CHEMBL4586335 175989 None 0 Human Functional pEC50 = 7.8 7.8 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 321 2 0 3 3.9 Clc1ccc(Cn2nnc3c(Br)cccc32)cc1 10.1021/acs.jmedchem.8b00161
49765871 2145 None 41 Human Functional pEC50 = 7.8 7.8 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/jm3010724
6317 2145 None 41 Human Functional pEC50 = 7.8 7.8 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/jm3010724
CHEMBL2179319 2145 None 41 Human Functional pEC50 = 7.8 7.8 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/jm3010724
60096236 158514 None 0 Human Functional pEC50 = 7.8 7.8 -3 2
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 322 4 4 4 0.1 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2F)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4090293 158514 None 0 Human Functional pEC50 = 7.8 7.8 -3 2
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 322 4 4 4 0.1 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2F)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
66784246 156455 None 0 Human Functional pEC50 = 7.8 7.8 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 418 5 0 5 6.1 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C)cc2Cl)c(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4066051 156455 None 0 Human Functional pEC50 = 7.8 7.8 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 418 5 0 5 6.1 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C)cc2Cl)c(C)n1 10.1021/acs.jmedchem.7b00669
66785300 156563 None 0 Human Functional pEC50 = 7.8 7.8 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 408 5 1 4 5.8 CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1Cl 10.1021/acs.jmedchem.7b00669
CHEMBL4067421 156563 None 0 Human Functional pEC50 = 7.8 7.8 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 408 5 1 4 5.8 CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1Cl 10.1021/acs.jmedchem.7b00669
59599580 152805 None 0 Human Functional pEC50 = 7.8 7.8 8 2
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 471 7 2 8 4.6 CC(=O)c1ccc(OCc2cccc(Oc3ccc(-c4nn[nH]n4)cn3)c2)c(C(F)(F)F)c1O 10.1016/j.bmcl.2016.11.049
CHEMBL3973048 152805 None 0 Human Functional pEC50 = 7.8 7.8 8 2
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 471 7 2 8 4.6 CC(=O)c1ccc(OCc2cccc(Oc3ccc(-c4nn[nH]n4)cn3)c2)c(C(F)(F)F)c1O 10.1016/j.bmcl.2016.11.049
71116952 147402 None 0 Human Functional pEC50 = 7.8 7.8 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 421 3 0 7 2.9 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)c5ncco5)CC4C3)nc21 nan
CHEMBL3929070 147402 None 0 Human Functional pEC50 = 7.8 7.8 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 421 3 0 7 2.9 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)c5ncco5)CC4C3)nc21 nan
59497100 114644 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 342 4 0 3 4.3 O=c1c(Cl)c(N2CCC(c3ccccc3)CC2)ccn1CC1CC1 10.1021/jm500496m
CHEMBL3337524 114644 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 342 4 0 3 4.3 O=c1c(Cl)c(N2CCC(c3ccccc3)CC2)ccn1CC1CC1 10.1021/jm500496m
162659390 181298 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 359 5 0 4 4.1 Fc1ccc(OCCCN2CCn3c(nc4ccccc43)C2)cc1Cl 10.1016/j.ejmech.2019.111881
CHEMBL4761080 181298 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 359 5 0 4 4.1 Fc1ccc(OCCCN2CCn3c(nc4ccccc43)C2)cc1Cl 10.1016/j.ejmech.2019.111881
1402 122 None 35 Human Functional pEC50 = 5.8 5.8 - 1
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 452 8 0 5 4.8 COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 10.1016/j.bmcl.2004.09.028
9825084 122 None 35 Human Functional pEC50 = 5.8 5.8 - 1
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 452 8 0 5 4.8 COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 10.1016/j.bmcl.2004.09.028
CHEMBL108939 122 None 35 Human Functional pEC50 = 5.8 5.8 - 1
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 452 8 0 5 4.8 COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 10.1016/j.bmcl.2004.09.028
10608207 118828 None 3 Rat Functional pEC50 = 4.8 4.8 - 1
Antagonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated in presence of 30 uM glutamic acidAntagonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated in presence of 30 uM glutamic acid
ChEMBL 203 2 3 3 -0.5 N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2C[C@H]1F 10.1021/jm000346k
CHEMBL341888 118828 None 3 Rat Functional pEC50 = 4.8 4.8 - 1
Antagonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated in presence of 30 uM glutamic acidAntagonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated in presence of 30 uM glutamic acid
ChEMBL 203 2 3 3 -0.5 N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2C[C@H]1F 10.1021/jm000346k
11537726 66714 None 0 Human Functional pEC50 = 5.8 5.8 - 1
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 357 10 1 5 4.6 Cc1c(OCCCCOc2cccnc2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
CHEMBL185490 66714 None 0 Human Functional pEC50 = 5.8 5.8 - 1
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 357 10 1 5 4.6 Cc1c(OCCCCOc2cccnc2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
25004010 74623 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 399 6 1 5 4.7 CC(C)CCn1ccc(-c2ccc(NC3CCOCC3)c(Cl)c2)c(C#N)c1=O 10.1021/jm2016864
CHEMBL2029802 74623 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 399 6 1 5 4.7 CC(C)CCn1ccc(-c2ccc(NC3CCOCC3)c(Cl)c2)c(C#N)c1=O 10.1021/jm2016864
168298053 192856 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding
ChEMBL 356 3 1 3 4.8 FC(F)(F)c1c(-c2ccc3[nH]ccc3c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.2c00969
CHEMBL5220838 192856 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding
ChEMBL 356 3 1 3 4.8 FC(F)(F)c1c(-c2ccc3[nH]ccc3c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.2c00969
44155644 8852 None 0 Human Functional pEC50 = 5.8 5.8 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 272 6 0 3 3.9 CCCCCCC1CN(c2ccccc2C#N)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1097054 8852 None 0 Human Functional pEC50 = 5.8 5.8 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 272 6 0 3 3.9 CCCCCCC1CN(c2ccccc2C#N)C(=O)O1 10.1016/j.bmcl.2010.03.089
1310 2315 None 61 Human Functional pEC50 = 5.8 5.8 -389 17
Agonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
1369 2315 None 61 Human Functional pEC50 = 5.8 5.8 -389 17
Agonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
33032 2315 None 61 Human Functional pEC50 = 5.8 5.8 -389 17
Agonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
44272391 2315 None 61 Human Functional pEC50 = 5.8 5.8 -389 17
Agonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
88747398 2315 None 61 Human Functional pEC50 = 5.8 5.8 -389 17
Agonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
CHEMBL575060 2315 None 61 Human Functional pEC50 = 5.8 5.8 -389 17
Agonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
DB00142 2315 None 61 Human Functional pEC50 = 5.8 5.8 -389 17
Agonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
71117549 146932 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 437 4 0 6 1.8 CN1c2nc(C3=CCN(C(=O)c4ccon4)C3)ccc2N(CC2CC2(F)F)S1(=O)=O nan
CHEMBL3925103 146932 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 437 4 0 6 1.8 CN1c2nc(C3=CCN(C(=O)c4ccon4)C3)ccc2N(CC2CC2(F)F)S1(=O)=O nan
155548817 173944 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 3 hrs followed by [35S]GTPgammaS addition and measured after 1 hr by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 3 hrs followed by [35S]GTPgammaS addition and measured after 1 hr by scintillation spectrometry method
ChEMBL 518 6 1 6 5.3 O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
CHEMBL4538850 173944 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 3 hrs followed by [35S]GTPgammaS addition and measured after 1 hr by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 3 hrs followed by [35S]GTPgammaS addition and measured after 1 hr by scintillation spectrometry method
ChEMBL 518 6 1 6 5.3 O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
118714745 114631 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 347 5 0 4 3.9 N#Cc1c(N2CCC(c3ccccc3)CC2)ccn(CCC2CC2)c1=O 10.1021/jm500496m
CHEMBL3337511 114631 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 347 5 0 4 3.9 N#Cc1c(N2CCC(c3ccccc3)CC2)ccn(CCC2CC2)c1=O 10.1021/jm500496m
57459504 82672 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 434 4 0 4 5.4 FC(F)(F)C1(c2ccccc2)CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm3010724
CHEMBL2179317 82672 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 434 4 0 4 5.4 FC(F)(F)C1(c2ccccc2)CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm3010724
134131242 142366 None 0 Human Functional pEC50 = 7.8 7.8 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 353 4 0 4 4.3 Clc1c(OC2CCc3ccccc3C2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
CHEMBL3885072 142366 None 0 Human Functional pEC50 = 7.8 7.8 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 353 4 0 4 4.3 Clc1c(OC2CCc3ccccc3C2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
155519900 170503 None 0 Human Functional pEC50 = 7.8 7.8 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 339 2 0 3 4.0 Fc1cc(Cn2nnc3c(Br)cccc32)ccc1Cl 10.1021/acs.jmedchem.8b00161
CHEMBL4448031 170503 None 0 Human Functional pEC50 = 7.8 7.8 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 339 2 0 3 4.0 Fc1cc(Cn2nnc3c(Br)cccc32)ccc1Cl 10.1021/acs.jmedchem.8b00161
155565817 175725 None 0 Human Functional pEC50 = 7.8 7.8 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 305 2 0 3 3.4 Fc1cccc(Cn2nnc3c(Br)cccc32)c1 10.1021/acs.jmedchem.8b00161
CHEMBL4580527 175725 None 0 Human Functional pEC50 = 7.8 7.8 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 305 2 0 3 3.4 Fc1cccc(Cn2nnc3c(Br)cccc32)c1 10.1021/acs.jmedchem.8b00161
60096190 158605 None 0 Human Functional pEC50 = 7.7 7.7 -9 2
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 322 4 4 4 0.1 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2cccc(F)c2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4091203 158605 None 0 Human Functional pEC50 = 7.7 7.7 -9 2
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 322 4 4 4 0.1 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2cccc(F)c2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
10353365 83279 None 1 Human Functional pEC50 = 7.7 7.7 13 3
Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells
ChEMBL 219 2 3 4 -1.8 N[C@@]1(C(=O)O)C[S+]([O-])[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm060917u
CHEMBL218710 83279 None 1 Human Functional pEC50 = 7.7 7.7 13 3
Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells
ChEMBL 219 2 3 4 -1.8 N[C@@]1(C(=O)O)C[S+]([O-])[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm060917u
49822115 2146 None 24 Human Functional pEC50 = 7.7 7.7 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry method
ChEMBL 414 5 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.8b00051
8947 2146 None 24 Human Functional pEC50 = 7.7 7.7 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry method
ChEMBL 414 5 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.8b00051
CHEMBL3947764 2146 None 24 Human Functional pEC50 = 7.7 7.7 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry methodPositive allosteric modulation of human mGlu2 receptor expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition and measured after 90 mins by scintillation spectrometry method
ChEMBL 414 5 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.8b00051
1393 1539 None 42 Rat Functional pEC50 = 7.7 7.7 -2 6
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm000346k
1396 1539 None 42 Rat Functional pEC50 = 7.7 7.7 -2 6
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm000346k
213056 1539 None 42 Rat Functional pEC50 = 7.7 7.7 -2 6
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm000346k
CHEMBL8759 1539 None 42 Rat Functional pEC50 = 7.7 7.7 -2 6
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm000346k
66787355 156316 None 0 Human Functional pEC50 = 7.7 7.7 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 450 5 1 5 5.6 FC(F)(F)c1c(-c2ccc(NC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
CHEMBL4064589 156316 None 0 Human Functional pEC50 = 7.7 7.7 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 450 5 1 5 5.6 FC(F)(F)c1c(-c2ccc(NC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
66784572 157000 None 0 Human Functional pEC50 = 7.7 7.7 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 468 6 0 5 6.6 Fc1cc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)ccc1Oc1ccnc(C2CC2)c1 10.1021/acs.jmedchem.7b00669
CHEMBL4072262 157000 None 0 Human Functional pEC50 = 7.7 7.7 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 468 6 0 5 6.6 Fc1cc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)ccc1Oc1ccnc(C2CC2)c1 10.1021/acs.jmedchem.7b00669
134130477 142411 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 313 5 0 4 3.9 Clc1c(OCc2ccccc2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
CHEMBL3885492 142411 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 313 5 0 4 3.9 Clc1c(OCc2ccccc2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
162644700 179529 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 373 5 0 4 3.8 O=C1c2nc3ccccc3n2CCN1CCCOc1ccc(F)c(Cl)c1 10.1016/j.ejmech.2019.111881
CHEMBL4740255 179529 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 373 5 0 4 3.8 O=C1c2nc3ccccc3n2CCN1CCCOc1ccc(F)c(Cl)c1 10.1016/j.ejmech.2019.111881
155527610 171351 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 366 2 0 4 3.4 Brc1ccc(Cn2nnc3c(Br)cccc32)nc1 10.1021/acs.jmedchem.8b00161
CHEMBL4460043 171351 None 0 Human Functional pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 366 2 0 4 3.4 Brc1ccc(Cn2nnc3c(Br)cccc32)nc1 10.1021/acs.jmedchem.8b00161
44591797 184750 None 0 Human Functional pEC50 = 5.8 5.8 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 304 3 0 3 3.4 C[C@@H]1CN(Cc2ccc(-c3ccc(F)c(F)c3)cn2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL484958 184750 None 0 Human Functional pEC50 = 5.8 5.8 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 304 3 0 3 3.4 C[C@@H]1CN(Cc2ccc(-c3ccc(F)c(F)c3)cn2)C(=O)O1 10.1016/j.bmcl.2009.03.032
104766 33 None 30 Human Functional pEC50 = 4.8 4.8 -2 14
Agonist activity against Metabotropic glutamate receptor 2 expressed in HEK 293 cells was evaluated by measuring total inositol phosphate accumulationAgonist activity against Metabotropic glutamate receptor 2 expressed in HEK 293 cells was evaluated by measuring total inositol phosphate accumulation
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1021/jm970207b
1365 33 None 30 Human Functional pEC50 = 4.8 4.8 -2 14
Agonist activity against Metabotropic glutamate receptor 2 expressed in HEK 293 cells was evaluated by measuring total inositol phosphate accumulationAgonist activity against Metabotropic glutamate receptor 2 expressed in HEK 293 cells was evaluated by measuring total inositol phosphate accumulation
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1021/jm970207b
CHEMBL34453 33 None 30 Human Functional pEC50 = 4.8 4.8 -2 14
Agonist activity against Metabotropic glutamate receptor 2 expressed in HEK 293 cells was evaluated by measuring total inositol phosphate accumulationAgonist activity against Metabotropic glutamate receptor 2 expressed in HEK 293 cells was evaluated by measuring total inositol phosphate accumulation
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1021/jm970207b
1310 2315 None 61 Rat Functional pEC50 = 4.7 4.7 -457 17
Agonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assayAgonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmcl.2015.04.043
1369 2315 None 61 Rat Functional pEC50 = 4.7 4.7 -457 17
Agonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assayAgonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmcl.2015.04.043
33032 2315 None 61 Rat Functional pEC50 = 4.7 4.7 -457 17
Agonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assayAgonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmcl.2015.04.043
44272391 2315 None 61 Rat Functional pEC50 = 4.7 4.7 -457 17
Agonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assayAgonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmcl.2015.04.043
88747398 2315 None 61 Rat Functional pEC50 = 4.7 4.7 -457 17
Agonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assayAgonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmcl.2015.04.043
CHEMBL575060 2315 None 61 Rat Functional pEC50 = 4.7 4.7 -457 17
Agonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assayAgonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmcl.2015.04.043
DB00142 2315 None 61 Rat Functional pEC50 = 4.7 4.7 -457 17
Agonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assayAgonist activity at rat mGluR2 expressed in HEK293 cells assessed as induction of inositol phosphate production by HTRF assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmcl.2015.04.043
1310 2315 None 61 Human Functional pEC50 = 5.7 5.7 -389 17
Agonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
1369 2315 None 61 Human Functional pEC50 = 5.7 5.7 -389 17
Agonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
33032 2315 None 61 Human Functional pEC50 = 5.7 5.7 -389 17
Agonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
44272391 2315 None 61 Human Functional pEC50 = 5.7 5.7 -389 17
Agonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
88747398 2315 None 61 Human Functional pEC50 = 5.7 5.7 -389 17
Agonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
CHEMBL575060 2315 None 61 Human Functional pEC50 = 5.7 5.7 -389 17
Agonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
DB00142 2315 None 61 Human Functional pEC50 = 5.7 5.7 -389 17
Agonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
44591771 184346 None 0 Human Functional pEC50 = 6.7 6.7 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 351 4 0 3 4.6 C[C@@H]1CN(Cc2ccc(-c3ccc(OC(F)(F)F)cc3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL483561 184346 None 0 Human Functional pEC50 = 6.7 6.7 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 351 4 0 3 4.6 C[C@@H]1CN(Cc2ccc(-c3ccc(OC(F)(F)F)cc3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
162649571 180227 None 0 Human Functional pEC50 = 5.7 5.7 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 311 3 0 3 3.7 Clc1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
CHEMBL4748614 180227 None 0 Human Functional pEC50 = 5.7 5.7 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 311 3 0 3 3.7 Clc1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
51356833 61993 None 0 Rat Functional pEC50 = 6.7 6.7 - 1
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 400 3 0 4 4.9 Cn1c(CN2[C@H]3CC[C@@H]2CC(c2ccc(C(F)(F)F)cc2)C3)nc2ncccc21 10.1021/jm101414h
CHEMBL1774225 61993 None 0 Rat Functional pEC50 = 6.7 6.7 - 1
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 400 3 0 4 4.9 Cn1c(CN2[C@H]3CC[C@@H]2CC(c2ccc(C(F)(F)F)cc2)C3)nc2ncccc21 10.1021/jm101414h
46227797 204092 None 0 Human Functional pEC50 = 6.7 6.7 - 1
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 393 4 0 4 5.8 N#Cc1c(-c2ccc(Oc3ccccc3)cc2)ccn2c(CC(F)(F)F)cnc12 10.1021/jm201561r
CHEMBL605921 204092 None 0 Human Functional pEC50 = 6.7 6.7 - 1
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 393 4 0 4 5.8 N#Cc1c(-c2ccc(Oc3ccccc3)cc2)ccn2c(CC(F)(F)F)cnc12 10.1021/jm201561r
25004352 74615 None 0 Human Functional pEC50 = 6.7 6.7 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 400 6 0 5 4.6 CC(C)CCn1ccc(-c2ccc(OC3CCOCC3)c(Cl)c2)c(C#N)c1=O 10.1021/jm2016864
CHEMBL2029796 74615 None 0 Human Functional pEC50 = 6.7 6.7 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 400 6 0 5 4.6 CC(C)CCn1ccc(-c2ccc(OC3CCOCC3)c(Cl)c2)c(C#N)c1=O 10.1021/jm2016864
46227797 204092 None 0 Human Functional pEC50 = 6.7 6.7 - 1
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 393 4 0 4 5.8 N#Cc1c(-c2ccc(Oc3ccccc3)cc2)ccn2c(CC(F)(F)F)cnc12 10.1016/j.bmcl.2009.11.008
CHEMBL605921 204092 None 0 Human Functional pEC50 = 6.7 6.7 - 1
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 393 4 0 4 5.8 N#Cc1c(-c2ccc(Oc3ccccc3)cc2)ccn2c(CC(F)(F)F)cnc12 10.1016/j.bmcl.2009.11.008
11655609 165996 None 0 Human Functional pEC50 = 6.7 6.7 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 463 11 1 8 4.8 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1nnn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
CHEMBL424998 165996 None 0 Human Functional pEC50 = 6.7 6.7 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 463 11 1 8 4.8 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1nnn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
71476419 123476 None 0 Human Functional pEC50 = 7.7 7.7 51 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@H](Sc2c[nH]nn2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616860 123476 None 0 Human Functional pEC50 = 7.7 7.7 51 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@H](Sc2c[nH]nn2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
60096204 156215 None 0 Human Functional pEC50 = 7.7 7.7 -2 2
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 322 4 4 4 0.1 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccc(F)cc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4063336 156215 None 0 Human Functional pEC50 = 7.7 7.7 -2 2
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 322 4 4 4 0.1 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccc(F)cc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
11220424 159053 None 0 Human Functional pEC50 = 7.7 7.7 -3 2
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 304 4 4 4 -0.1 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4095995 159053 None 0 Human Functional pEC50 = 7.7 7.7 -3 2
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 304 4 4 4 -0.1 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
71456562 80835 None 0 Human Functional pEC50 = 6.7 6.7 - 1
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 394 4 0 4 5.3 N#Cc1c(-c2ccc3c(ccn3CC3CC3)c2)ccn2c(CC(F)(F)F)cnc12 10.1021/jm201561r
CHEMBL2152113 80835 None 0 Human Functional pEC50 = 6.7 6.7 - 1
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 394 4 0 4 5.3 N#Cc1c(-c2ccc3c(ccn3CC3CC3)c2)ccn2c(CC(F)(F)F)cnc12 10.1021/jm201561r
155519573 173372 None 0 Human Functional pEC50 = 6.7 6.7 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 339 2 0 3 4.0 Fc1ccc(Cn2nnc3c(Br)cccc32)c(Cl)c1 10.1021/acs.jmedchem.8b00161
CHEMBL4525207 173372 None 0 Human Functional pEC50 = 6.7 6.7 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 339 2 0 3 4.0 Fc1ccc(Cn2nnc3c(Br)cccc32)c(Cl)c1 10.1021/acs.jmedchem.8b00161
44155748 8506 None 0 Human Functional pEC50 = 5.7 5.7 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 263 6 1 3 3.7 CCCCCCC1CN(c2cccc(O)c2)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1094124 8506 None 0 Human Functional pEC50 = 5.7 5.7 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 263 6 1 3 3.7 CCCCCCC1CN(c2cccc(O)c2)C(=O)O1 10.1016/j.bmcl.2010.03.089
118263352 114646 None 0 Human Functional pEC50 = 6.7 6.7 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 344 4 0 3 4.5 CC(C)Cn1ccc(N2CCC(c3ccccc3)CC2)c(Cl)c1=O 10.1021/jm500496m
CHEMBL3337526 114646 None 0 Human Functional pEC50 = 6.7 6.7 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 344 4 0 3 4.5 CC(C)Cn1ccc(N2CCC(c3ccccc3)CC2)c(Cl)c1=O 10.1021/jm500496m
25009651 61982 None 0 Rat Functional pEC50 = 6.7 6.7 - 1
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 374 3 0 4 4.4 Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2ccncc21 10.1021/jm101414h
CHEMBL1774110 61982 None 0 Rat Functional pEC50 = 6.7 6.7 - 1
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 374 3 0 4 4.4 Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2ccncc21 10.1021/jm101414h
11559813 65029 None 0 Human Functional pEC50 = 5.7 5.7 - 1
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 374 10 1 4 5.3 Cc1c(OCCCCOc2ccccc2F)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
CHEMBL182316 65029 None 0 Human Functional pEC50 = 5.7 5.7 - 1
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 374 10 1 4 5.3 Cc1c(OCCCCOc2ccccc2F)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
90668095 109597 None 0 Human Functional pEC50 = 6.7 6.7 - 1
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 320 6 1 3 4.4 CCCn1ccc2c(NCCc3ccc(C)cc3)cccc2c1=O 10.1039/C0MD00200C
CHEMBL3221835 109597 None 0 Human Functional pEC50 = 6.7 6.7 - 1
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 320 6 1 3 4.4 CCCn1ccc2c(NCCc3ccc(C)cc3)cccc2c1=O 10.1039/C0MD00200C
90668102 109606 None 0 Human Functional pEC50 = 6.7 6.7 - 1
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 376 6 1 4 4.9 CCCn1ccc2c(NCc3cccc(OC(F)(F)F)c3)cccc2c1=O 10.1039/C0MD00200C
CHEMBL3221843 109606 None 0 Human Functional pEC50 = 6.7 6.7 - 1
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 376 6 1 4 4.9 CCCn1ccc2c(NCc3cccc(OC(F)(F)F)c3)cccc2c1=O 10.1039/C0MD00200C
46917716 109607 None 0 Human Functional pEC50 = 6.7 6.7 - 1
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 326 5 1 3 4.7 CCCn1ccc2c(NCc3ccccc3Cl)cccc2c1=O 10.1039/C0MD00200C
CHEMBL3221844 109607 None 0 Human Functional pEC50 = 6.7 6.7 - 1
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 326 5 1 3 4.7 CCCn1ccc2c(NCc3ccccc3Cl)cccc2c1=O 10.1039/C0MD00200C
53326710 57758 None 0 Human Functional pEC50 = 5.7 5.7 - 1
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 389 5 0 3 6.5 CCCn1ccc2cc(-c3ccc(Oc4ccccc4)cc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669396 57758 None 0 Human Functional pEC50 = 5.7 5.7 - 1
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 389 5 0 3 6.5 CCCn1ccc2cc(-c3ccc(Oc4ccccc4)cc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
46190877 1871 None 8 Human Functional pEC50 = 5.7 5.7 - 1
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 409 3 0 5 4.0 Clc1cc(cnc1N1CCN(CC1)Cc1nc2c(n1C)cccc2)C(F)(F)F 10.1016/j.bmcl.2009.11.032
6252 1871 None 8 Human Functional pEC50 = 5.7 5.7 - 1
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 409 3 0 5 4.0 Clc1cc(cnc1N1CCN(CC1)Cc1nc2c(n1C)cccc2)C(F)(F)F 10.1016/j.bmcl.2009.11.032
CHEMBL605836 1871 None 8 Human Functional pEC50 = 5.7 5.7 - 1
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 409 3 0 5 4.0 Clc1cc(cnc1N1CCN(CC1)Cc1nc2c(n1C)cccc2)C(F)(F)F 10.1016/j.bmcl.2009.11.032
24815976 202215 None 0 Human Functional pEC50 = 5.7 5.7 -5 2
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 373 3 0 3 5.0 Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL593745 202215 None 0 Human Functional pEC50 = 5.7 5.7 -5 2
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 373 3 0 3 5.0 Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
46225336 202504 None 0 Human Functional pEC50 = 5.7 5.7 - 1
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 363 3 0 6 3.5 Cn1c(CN2CCN(c3nc4ccccc4s3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL595609 202504 None 0 Human Functional pEC50 = 5.7 5.7 - 1
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 363 3 0 6 3.5 Cn1c(CN2CCN(c3nc4ccccc4s3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
90668098 109601 None 0 Human Functional pEC50 = 5.7 5.7 - 1
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 292 5 1 3 4.0 CCCn1ccc2c(NCc3ccccc3)cccc2c1=O 10.1039/C0MD00200C
CHEMBL3221839 109601 None 0 Human Functional pEC50 = 5.7 5.7 - 1
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 292 5 1 3 4.0 CCCn1ccc2c(NCc3ccccc3)cccc2c1=O 10.1039/C0MD00200C
10197984 2421 None 36 Human Functional pEC50 = 8.6 8.6 1 5
Agonist activity at human mGLUR2 assessed as inhibition of forskolin-stimulated cAMP production by cell-based assayAgonist activity at human mGLUR2 assessed as inhibition of forskolin-stimulated cAMP production by cell-based assay
ChEMBL 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10.1016/j.bmcl.2012.01.039
1394 2421 None 36 Human Functional pEC50 = 8.6 8.6 1 5
Agonist activity at human mGLUR2 assessed as inhibition of forskolin-stimulated cAMP production by cell-based assayAgonist activity at human mGLUR2 assessed as inhibition of forskolin-stimulated cAMP production by cell-based assay
ChEMBL 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10.1016/j.bmcl.2012.01.039
CHEMBL275079 2421 None 36 Human Functional pEC50 = 8.6 8.6 1 5
Agonist activity at human mGLUR2 assessed as inhibition of forskolin-stimulated cAMP production by cell-based assayAgonist activity at human mGLUR2 assessed as inhibition of forskolin-stimulated cAMP production by cell-based assay
ChEMBL 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10.1016/j.bmcl.2012.01.039
10197984 2421 None 36 Human Functional pEC50 = 8.6 8.6 1 5
Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2
ChEMBL 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10.1021/jm980616n
1394 2421 None 36 Human Functional pEC50 = 8.6 8.6 1 5
Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2
ChEMBL 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10.1021/jm980616n
CHEMBL275079 2421 None 36 Human Functional pEC50 = 8.6 8.6 1 5
Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2
ChEMBL 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10.1021/jm980616n
10197984 2421 None 36 Human Functional pEC50 = 8.6 8.6 1 5
Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells
ChEMBL 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10.1021/jm060917u
1394 2421 None 36 Human Functional pEC50 = 8.6 8.6 1 5
Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells
ChEMBL 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10.1021/jm060917u
CHEMBL275079 2421 None 36 Human Functional pEC50 = 8.6 8.6 1 5
Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells
ChEMBL 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10.1021/jm060917u
66786902 159555 None 0 Human Functional pEC50 = 8.5 8.5 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 472 5 0 5 6.8 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)c(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4101354 159555 None 0 Human Functional pEC50 = 8.5 8.5 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 472 5 0 5 6.8 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)c(C)n1 10.1021/acs.jmedchem.7b00669
71457756 83936 None 0 Human Functional pEC50 = 7.7 7.7 66 2
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 396 5 0 5 4.7 COc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm300912k
CHEMBL2206440 83936 None 0 Human Functional pEC50 = 7.7 7.7 66 2
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 396 5 0 5 4.7 COc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm300912k
134130276 142391 None 0 Human Functional pEC50 = 7.7 7.7 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 389 6 0 4 5.6 Clc1c(OCc2ccccc2-c2ccccc2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
CHEMBL3885277 142391 None 0 Human Functional pEC50 = 7.7 7.7 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 389 6 0 4 5.6 Clc1c(OCc2ccccc2-c2ccccc2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
155536501 172297 None 1 Human Functional pEC50 = 7.7 7.7 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 265 2 0 3 3.0 Brc1cccc2c1nnn2CC1CCC1 10.1021/acs.jmedchem.8b00161
CHEMBL4473685 172297 None 1 Human Functional pEC50 = 7.7 7.7 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 265 2 0 3 3.0 Brc1cccc2c1nnn2CC1CCC1 10.1021/acs.jmedchem.8b00161
68108457 148644 None 0 Human Functional pEC50 = 7.7 7.7 - 1
Positive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP AssayPositive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP Assay
ChEMBL 450 5 0 4 5.4 Fc1ccc(C2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.2c00593
CHEMBL3938796 148644 None 0 Human Functional pEC50 = 7.7 7.7 - 1
Positive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP AssayPositive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP Assay
ChEMBL 450 5 0 4 5.4 Fc1ccc(C2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.2c00593
CHEMBL5074658 216811 None 0 Human Functional pEC50 = 7.7 7.7 - 1
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL None None None O=C1c2nc3cccc(Br)c3n2CCN1Cc1ccc(Br)cc1 10.1021/acs.jmedchem.1c00563
71137011 123474 None 0 Human Functional pEC50 = 7.7 7.7 58 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 299 4 5 7 -1.0 Nc1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
CHEMBL3616858 123474 None 0 Human Functional pEC50 = 7.7 7.7 58 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 299 4 5 7 -1.0 Nc1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
53240406 123463 None 21 Human Functional pEC50 = 7.7 7.7 107 4
Agonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616847 123463 None 21 Human Functional pEC50 = 7.7 7.7 107 4
Agonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at wild type human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
50992248 166637 None 0 Rat Functional pEC50 = 7.7 7.7 -1 2
Positive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis
ChEMBL 376 5 0 5 3.9 CCc1cn2c(nc1=O)O[C@H](COc1ccc(-c3cccc(C)c3C)cc1)C2 10.1016/j.bmcl.2018.08.022
CHEMBL4279401 166637 None 0 Rat Functional pEC50 = 7.7 7.7 -1 2
Positive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis
ChEMBL 376 5 0 5 3.9 CCc1cn2c(nc1=O)O[C@H](COc1ccc(-c3cccc(C)c3C)cc1)C2 10.1016/j.bmcl.2018.08.022
1392 73 None 32 Rat Functional pEC50 = 6.7 6.7 5 4
Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor
ChEMBL 174 2 4 4 -1.8 OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O 10.1016/s0960-894x(99)00266-8
5310984 73 None 32 Rat Functional pEC50 = 6.7 6.7 5 4
Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor
ChEMBL 174 2 4 4 -1.8 OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O 10.1016/s0960-894x(99)00266-8
CHEMBL40086 73 None 32 Rat Functional pEC50 = 6.7 6.7 5 4
Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor
ChEMBL 174 2 4 4 -1.8 OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O 10.1016/s0960-894x(99)00266-8
104766 33 None 30 Rat Functional pEC50 = 5.7 5.7 2 14
Activity tested at cloned rat mGluR2 receptor expressed in Chinese Hamster Ovary (CHO) cellsActivity tested at cloned rat mGluR2 receptor expressed in Chinese Hamster Ovary (CHO) cells
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1021/jm0308085
1365 33 None 30 Rat Functional pEC50 = 5.7 5.7 2 14
Activity tested at cloned rat mGluR2 receptor expressed in Chinese Hamster Ovary (CHO) cellsActivity tested at cloned rat mGluR2 receptor expressed in Chinese Hamster Ovary (CHO) cells
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1021/jm0308085
CHEMBL34453 33 None 30 Rat Functional pEC50 = 5.7 5.7 2 14
Activity tested at cloned rat mGluR2 receptor expressed in Chinese Hamster Ovary (CHO) cellsActivity tested at cloned rat mGluR2 receptor expressed in Chinese Hamster Ovary (CHO) cells
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1021/jm0308085
11596869 143724 None 0 Human Functional pEC50 = 6.7 6.7 -8 2
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 417 7 2 8 3.9 CC(=O)c1ccc(OCc2ccc(Oc3cc(-c4nn[nH]n4)ccn3)cc2)c(C)c1O 10.1016/j.bmcl.2016.11.049
CHEMBL3899832 143724 None 0 Human Functional pEC50 = 6.7 6.7 -8 2
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 417 7 2 8 3.9 CC(=O)c1ccc(OCc2ccc(Oc3cc(-c4nn[nH]n4)ccn3)cc2)c(C)c1O 10.1016/j.bmcl.2016.11.049
25173287 170477 None 0 Human Functional pEC50 = 6.7 6.7 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 317 6 0 3 4.4 CC1CN(Cc2ccc(OCCC3CCCCC3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL444778 170477 None 0 Human Functional pEC50 = 6.7 6.7 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 317 6 0 3 4.4 CC1CN(Cc2ccc(OCCC3CCCCC3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
24809687 74624 None 0 Human Functional pEC50 = 5.7 5.7 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 351 5 0 5 3.3 CC(C)CCn1ccc(-c2ccc(N3CCOCC3)cc2)c(C#N)c1=O 10.1021/jm2016864
CHEMBL2029803 74624 None 0 Human Functional pEC50 = 5.7 5.7 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 351 5 0 5 3.3 CC(C)CCn1ccc(-c2ccc(N3CCOCC3)cc2)c(C#N)c1=O 10.1021/jm2016864
156817927 191715 None 0 Human Functional pEC50 = 5.7 5.7 - 1
Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay
ChEMBL 433 5 0 5 4.2 Fc1ccccc1N1CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1 10.1021/acs.jmedchem.2c00593
CHEMBL5195400 191715 None 0 Human Functional pEC50 = 5.7 5.7 - 1
Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay
ChEMBL 433 5 0 5 4.2 Fc1ccccc1N1CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1 10.1021/acs.jmedchem.2c00593
44363330 36483 None 0 Rat Functional pEC50 = 7.7 7.7 - 1
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 219 2 4 4 -1.4 N[C@@]1(C(=O)O)CC(O)[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm000346k
CHEMBL144747 36483 None 0 Rat Functional pEC50 = 7.7 7.7 - 1
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 219 2 4 4 -1.4 N[C@@]1(C(=O)O)CC(O)[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm000346k
53240406 123463 None 21 Human Functional pEC50 = 7.7 7.7 107 4
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616847 123463 None 21 Human Functional pEC50 = 7.7 7.7 107 4
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
11275666 90091 None 1 Human Functional pEC50 = 7.7 7.7 1 3
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 200 2 4 4 -1.6 N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/acs.jmedchem.7b01481
CHEMBL2381647 90091 None 1 Human Functional pEC50 = 7.7 7.7 1 3
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 200 2 4 4 -1.6 N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/acs.jmedchem.7b01481
156018305 177939 None 0 Human Functional pEC50 = 6.7 6.7 89 2
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 440 8 0 6 4.7 COCCOc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4643961 177939 None 0 Human Functional pEC50 = 6.7 6.7 89 2
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 440 8 0 6 4.7 COCCOc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/acs.jmedchem.0c01058
155539343 172932 None 0 Human Functional pEC50 = 6.7 6.7 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 366 2 0 4 3.4 Brc1ccc(Cn2nnc3c(Br)cccc32)cn1 10.1021/acs.jmedchem.8b00161
CHEMBL4514174 172932 None 0 Human Functional pEC50 = 6.7 6.7 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 366 2 0 4 3.4 Brc1ccc(Cn2nnc3c(Br)cccc32)cn1 10.1021/acs.jmedchem.8b00161
104766 33 None 30 Rat Functional pEC50 = 5.7 5.7 2 14
Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1016/s0960-894x(99)00266-8
1365 33 None 30 Rat Functional pEC50 = 5.7 5.7 2 14
Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1016/s0960-894x(99)00266-8
CHEMBL34453 33 None 30 Rat Functional pEC50 = 5.7 5.7 2 14
Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1016/s0960-894x(99)00266-8
24815434 202152 None 0 Rat Functional pEC50 = 6.7 6.7 5 2
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 305 3 0 3 4.0 Cn1c(CN2CCC(c3ccccc3)CC2)nc2ccccc21 10.1021/jm101414h
CHEMBL593196 202152 None 0 Rat Functional pEC50 = 6.7 6.7 5 2
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 305 3 0 3 4.0 Cn1c(CN2CCC(c3ccccc3)CC2)nc2ccccc21 10.1021/jm101414h
156018305 177939 None 0 Human Functional pEC50 = 6.7 6.7 89 2
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 440 8 0 6 4.7 COCCOc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4643961 177939 None 0 Human Functional pEC50 = 6.7 6.7 89 2
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 440 8 0 6 4.7 COCCOc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/acs.jmedchem.0c01058
42610167 80832 None 0 Human Functional pEC50 = 5.7 5.7 - 1
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 420 3 0 5 4.5 N#Cc1c(-c2ccc(N3CCOCC3)c(Cl)c2)ccn2c(CC(F)(F)F)cnc12 10.1021/jm201561r
CHEMBL2152109 80832 None 0 Human Functional pEC50 = 5.7 5.7 - 1
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 420 3 0 5 4.5 N#Cc1c(-c2ccc(N3CCOCC3)c(Cl)c2)ccn2c(CC(F)(F)F)cnc12 10.1021/jm201561r
71117258 146637 None 0 Human Functional pEC50 = 5.7 5.7 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 467 6 1 8 3.2 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3CCC(C)(C)C(NC(=O)CCn4cncn4)C3)nc21 nan
CHEMBL3922773 146637 None 0 Human Functional pEC50 = 5.7 5.7 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 467 6 1 8 3.2 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3CCC(C)(C)C(NC(=O)CCn4cncn4)C3)nc21 nan
46887416 8545 None 0 Human Functional pEC50 = 5.7 5.7 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 299 5 0 4 3.1 COc1ccc(OCC2CN(c3ccccc3)C(=O)O2)cc1 10.1016/j.bmcl.2010.03.089
CHEMBL1094416 8545 None 0 Human Functional pEC50 = 5.7 5.7 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 299 5 0 4 3.1 COc1ccc(OCC2CN(c3ccccc3)C(=O)O2)cc1 10.1016/j.bmcl.2010.03.089
51357936 61997 None 0 Rat Functional pEC50 = 7.7 7.7 3 2
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 418 4 0 5 4.6 COc1cc(C(F)(F)F)ccc1[C@@H]1CCN(Cc2nc3ncccc3n2C)C[C@@H]1C 10.1021/jm101414h
CHEMBL1774231 61997 None 0 Rat Functional pEC50 = 7.7 7.7 3 2
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 418 4 0 5 4.6 COc1cc(C(F)(F)F)ccc1[C@@H]1CCN(Cc2nc3ncccc3n2C)C[C@@H]1C 10.1021/jm101414h
24815439 204392 None 1 Rat Functional pEC50 = 7.7 7.7 18 2
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 323 3 0 3 4.1 Cn1c(CN2CCC(c3ccccc3F)CC2)nc2ccccc21 10.1021/jm101414h
CHEMBL607689 204392 None 1 Rat Functional pEC50 = 7.7 7.7 18 2
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 323 3 0 3 4.1 Cn1c(CN2CCC(c3ccccc3F)CC2)nc2ccccc21 10.1021/jm101414h
53240406 123463 None 21 Human Functional pEC50 = 7.7 7.7 107 4
Agonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616847 123463 None 21 Human Functional pEC50 = 7.7 7.7 107 4
Agonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
25173773 185030 None 0 Human Functional pEC50 = 7.7 7.7 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 317 5 0 3 4.4 CC(Oc1ccc(CN2C[C@H](C)OC2=O)cc1)C1CCCCC1 10.1016/j.bmcl.2009.03.032
CHEMBL485336 185030 None 0 Human Functional pEC50 = 7.7 7.7 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 317 5 0 3 4.4 CC(Oc1ccc(CN2C[C@H](C)OC2=O)cc1)C1CCCCC1 10.1016/j.bmcl.2009.03.032
71117730 144018 None 0 Human Functional pEC50 = 7.6 7.6 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 421 3 0 7 3.1 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3ncco3)nc21 nan
CHEMBL3902193 144018 None 0 Human Functional pEC50 = 7.6 7.6 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 421 3 0 7 3.1 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3ncco3)nc21 nan
66784890 156141 None 0 Human Functional pEC50 = 6.7 6.7 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 358 5 1 4 5.0 CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2Cl)cc1F 10.1021/acs.jmedchem.7b00669
CHEMBL4062535 156141 None 0 Human Functional pEC50 = 6.7 6.7 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 358 5 1 4 5.0 CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2Cl)cc1F 10.1021/acs.jmedchem.7b00669
68109425 158382 None 0 Human Functional pEC50 = 6.7 6.7 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 417 5 0 5 5.2 Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1OC1CCOCC1 10.1021/acs.jmedchem.7b00669
CHEMBL4088960 158382 None 0 Human Functional pEC50 = 6.7 6.7 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 417 5 0 5 5.2 Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1OC1CCOCC1 10.1021/acs.jmedchem.7b00669
155560108 175013 None 3 Human Functional pEC50 = 5.7 5.7 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 225 1 0 3 2.2 CCn1nnc2c(Br)cccc21 10.1021/acs.jmedchem.8b00161
CHEMBL4564533 175013 None 3 Human Functional pEC50 = 5.7 5.7 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 225 1 0 3 2.2 CCn1nnc2c(Br)cccc21 10.1021/acs.jmedchem.8b00161
11950745 123711 None 0 Human Functional pEC50 = 5.6 5.6 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 497 9 1 6 5.9 CC(C)(C)Cn1ccc2c(Br)c(OCCCCOc3ccc(-c4nn[nH]n4)cc3)ccc21 10.1016/j.bmcl.2005.06.017
CHEMBL361934 123711 None 0 Human Functional pEC50 = 5.6 5.6 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 497 9 1 6 5.9 CC(C)(C)Cn1ccc2c(Br)c(OCCCCOc3ccc(-c4nn[nH]n4)cc3)ccc21 10.1016/j.bmcl.2005.06.017
59599555 153637 None 0 Human Functional pEC50 = 6.6 6.6 1 2
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 445 9 2 8 4.5 CCCc1c(OCc2cccc(Oc3ncccc3-c3nn[nH]n3)c2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2016.11.049
CHEMBL3980125 153637 None 0 Human Functional pEC50 = 6.6 6.6 1 2
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 445 9 2 8 4.5 CCCc1c(OCc2cccc(Oc3ncccc3-c3nn[nH]n3)c2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2016.11.049
11951806 66826 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 487 12 1 6 6.6 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC1CCCCC1 10.1016/j.bmcl.2005.06.017
CHEMBL186018 66826 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 487 12 1 6 6.6 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC1CCCCC1 10.1016/j.bmcl.2005.06.017
162654261 180760 None 0 Human Functional pEC50 = 5.6 5.6 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 335 6 0 4 3.9 COc1ccc(CCCCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
CHEMBL4755053 180760 None 0 Human Functional pEC50 = 5.6 5.6 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 335 6 0 4 3.9 COc1ccc(CCCCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
9979770 66359 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 424 11 2 7 4.3 Cc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
CHEMBL185054 66359 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 424 11 2 7 4.3 Cc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
46227789 202173 None 0 Human Functional pEC50 = 5.6 5.6 - 1
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 361 3 0 7 2.5 CCc1cnc2c(C#N)c(N3CCN(c4nc(C)cc(C)n4)CC3)ccn12 10.1016/j.bmcl.2009.11.008
CHEMBL593399 202173 None 0 Human Functional pEC50 = 5.6 5.6 - 1
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 361 3 0 7 2.5 CCc1cnc2c(C#N)c(N3CCN(c4nc(C)cc(C)n4)CC3)ccn12 10.1016/j.bmcl.2009.11.008
155531064 171741 None 0 Human Functional pEC50 = 7.6 7.6 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 339 2 0 3 4.0 Fc1cc(Cl)ccc1Cn1nnc2c(Br)cccc21 10.1021/acs.jmedchem.8b00161
CHEMBL4465783 171741 None 0 Human Functional pEC50 = 7.6 7.6 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 339 2 0 3 4.0 Fc1cc(Cl)ccc1Cn1nnc2c(Br)cccc21 10.1021/acs.jmedchem.8b00161
9834591 137687 None 46 Human Functional pEC50 = 7.6 7.6 2 3
Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells
ChEMBL 235 2 3 5 -2.1 N[C@@]1(C(=O)O)CS(=O)(=O)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm060917u
CHEMBL375611 137687 None 46 Human Functional pEC50 = 7.6 7.6 2 3
Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells
ChEMBL 235 2 3 5 -2.1 N[C@@]1(C(=O)O)CS(=O)(=O)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm060917u
46215709 80834 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 354 2 0 4 4.5 Cn1ccc2cc(-c3ccn4c(CC(F)(F)F)cnc4c3C#N)ccc21 10.1021/jm201561r
CHEMBL2152112 80834 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 354 2 0 4 4.5 Cn1ccc2cc(-c3ccn4c(CC(F)(F)F)cnc4c3C#N)ccc21 10.1021/jm201561r
156013901 177343 None 0 Human Functional pEC50 = 6.6 6.6 114 2
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 440 8 0 6 4.7 COCCOc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1 10.1021/acs.jmedchem.0c01058
CHEMBL4635729 177343 None 0 Human Functional pEC50 = 6.6 6.6 114 2
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 440 8 0 6 4.7 COCCOc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1 10.1021/acs.jmedchem.0c01058
70685768 74639 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 391 5 0 5 4.9 Cc1ncccc1Oc1ccc(-c2ccn(CC3CC3)c(=O)c2C#N)cc1Cl 10.1021/jm2016864
CHEMBL2029818 74639 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 391 5 0 5 4.9 Cc1ncccc1Oc1ccc(-c2ccn(CC3CC3)c(=O)c2C#N)cc1Cl 10.1021/jm2016864
134130478 142412 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 364 5 0 5 4.5 Clc1c(OCc2cccc3ccncc23)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
CHEMBL3885493 142412 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 364 5 0 5 4.5 Clc1c(OCc2cccc3ccncc23)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
44300122 13134 None 0 Rat Functional pEC50 = 5.6 5.6 - 1
Effective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonistEffective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonist
ChEMBL 279 4 4 5 -0.3 Nc1ccc(CN2C[C@@](N)(C(=O)O)C[C@@H]2C(=O)O)cc1 10.1016/s0960-894x(01)00329-8
CHEMBL1190517 13134 None 0 Rat Functional pEC50 = 5.6 5.6 - 1
Effective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonistEffective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonist
ChEMBL 279 4 4 5 -0.3 Nc1ccc(CN2C[C@@](N)(C(=O)O)C[C@@H]2C(=O)O)cc1 10.1016/s0960-894x(01)00329-8
CHEMBL541050 13134 None 0 Rat Functional pEC50 = 5.6 5.6 - 1
Effective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonistEffective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonist
ChEMBL 279 4 4 5 -0.3 Nc1ccc(CN2C[C@@](N)(C(=O)O)C[C@@H]2C(=O)O)cc1 10.1016/s0960-894x(01)00329-8
156013901 177343 None 0 Human Functional pEC50 = 6.6 6.6 114 2
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 440 8 0 6 4.7 COCCOc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1 10.1021/acs.jmedchem.0c01058
CHEMBL4635729 177343 None 0 Human Functional pEC50 = 6.6 6.6 114 2
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 440 8 0 6 4.7 COCCOc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1 10.1021/acs.jmedchem.0c01058
42610166 204126 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 384 3 0 4 5.0 N#Cc1c(-c2ccc(N3CCCCC3)cc2)ccn2c(CC(F)(F)F)cnc12 10.1016/j.bmcl.2009.11.008
CHEMBL606153 204126 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 384 3 0 4 5.0 N#Cc1c(-c2ccc(N3CCCCC3)cc2)ccn2c(CC(F)(F)F)cnc12 10.1016/j.bmcl.2009.11.008
1310 2315 None 61 Human Functional pEC50 = 5.6 5.6 -389 17
Agonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
1369 2315 None 61 Human Functional pEC50 = 5.6 5.6 -389 17
Agonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
33032 2315 None 61 Human Functional pEC50 = 5.6 5.6 -389 17
Agonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
44272391 2315 None 61 Human Functional pEC50 = 5.6 5.6 -389 17
Agonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
88747398 2315 None 61 Human Functional pEC50 = 5.6 5.6 -389 17
Agonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
CHEMBL575060 2315 None 61 Human Functional pEC50 = 5.6 5.6 -389 17
Agonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
DB00142 2315 None 61 Human Functional pEC50 = 5.6 5.6 -389 17
Agonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
68107863 192481 None 0 Human Functional pEC50 = 5.6 5.6 - 1
Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay
ChEMBL 467 5 0 5 4.8 Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(Cl)c1 10.1021/acs.jmedchem.2c00593
CHEMBL5207431 192481 None 0 Human Functional pEC50 = 5.6 5.6 - 1
Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay
ChEMBL 467 5 0 5 4.8 Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(Cl)c1 10.1021/acs.jmedchem.2c00593
25173617 188763 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 289 4 0 3 3.7 CC1CN(Cc2ccc(OC3CCCCC3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL503572 188763 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 289 4 0 3 3.7 CC1CN(Cc2ccc(OC3CCCCC3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
57459501 82675 None 0 Human Functional pEC50 = 7.6 7.6 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 402 5 0 4 5.5 CCCCc1nnc2c(C(F)(F)F)c(N3CCC(c4ccccc4)CC3)ccn12 10.1021/jm3010724
CHEMBL2179321 82675 None 0 Human Functional pEC50 = 7.6 7.6 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 402 5 0 4 5.5 CCCCc1nnc2c(C(F)(F)F)c(N3CCC(c4ccccc4)CC3)ccn12 10.1021/jm3010724
46887372 8806 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 325 4 0 3 4.4 CC(C)(C)c1ccc(OCC2CN(c3ccccc3)C(=O)O2)cc1 10.1016/j.bmcl.2010.03.089
CHEMBL1096713 8806 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 325 4 0 3 4.4 CC(C)(C)c1ccc(OCC2CN(c3ccccc3)C(=O)O2)cc1 10.1016/j.bmcl.2010.03.089
162669368 182874 None 0 Human Functional pEC50 = 5.6 5.6 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 330 5 0 4 3.7 N#Cc1ccc(CCCCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
CHEMBL4790241 182874 None 0 Human Functional pEC50 = 5.6 5.6 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 330 5 0 4 3.7 N#Cc1ccc(CCCCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
44300605 13360 None 0 Rat Functional pEC50 = 4.6 4.6 -3 3
Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2
ChEMBL 280 4 4 5 -0.2 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccc(O)cc2)C1 10.1016/s0960-894x(01)00329-8
CHEMBL1192345 13360 None 0 Rat Functional pEC50 = 4.6 4.6 -3 3
Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2
ChEMBL 280 4 4 5 -0.2 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccc(O)cc2)C1 10.1016/s0960-894x(01)00329-8
CHEMBL543568 13360 None 0 Rat Functional pEC50 = 4.6 4.6 -3 3
Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2
ChEMBL 280 4 4 5 -0.2 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccc(O)cc2)C1 10.1016/s0960-894x(01)00329-8
71136654 123475 None 0 Human Functional pEC50 = 6.6 6.6 3 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 326 5 4 6 0.5 CC(C)c1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
CHEMBL3616859 123475 None 0 Human Functional pEC50 = 6.6 6.6 3 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 326 5 4 6 0.5 CC(C)c1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
162659966 181357 None 0 Human Functional pEC50 = 5.6 5.6 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 291 3 0 3 3.4 Cc1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
CHEMBL4761771 181357 None 0 Human Functional pEC50 = 5.6 5.6 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 291 3 0 3 3.4 Cc1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
156014680 177355 None 0 Human Functional pEC50 = 5.6 5.6 -2 2
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 1250 48 0 20 8.6 COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4635960 177355 None 0 Human Functional pEC50 = 5.6 5.6 -2 2
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 1250 48 0 20 8.6 COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
51357400 61991 None 0 Rat Functional pEC50 = 7.6 7.6 - 1
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 408 4 0 5 4.4 Cn1c(CN2CCC(c3ccc(OC(F)(F)F)cc3F)CC2)nc2ncccc21 10.1021/jm101414h
CHEMBL1774222 61991 None 0 Rat Functional pEC50 = 7.6 7.6 - 1
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 408 4 0 5 4.4 Cn1c(CN2CCC(c3ccc(OC(F)(F)F)cc3F)CC2)nc2ncccc21 10.1021/jm101414h
51357399 61990 None 0 Rat Functional pEC50 = 7.6 7.6 - 1
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 392 3 0 4 4.5 Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3F)CC2)nc2ncccc21 10.1021/jm101414h
CHEMBL1774221 61990 None 0 Rat Functional pEC50 = 7.6 7.6 - 1
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 392 3 0 4 4.5 Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3F)CC2)nc2ncccc21 10.1021/jm101414h
68108857 157430 None 0 Human Functional pEC50 = 7.6 7.6 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 465 5 1 5 5.7 O[C@H]1CC[C@H](Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4077609 157430 None 0 Human Functional pEC50 = 7.6 7.6 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 465 5 1 5 5.7 O[C@H]1CC[C@H](Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
71458417 80844 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 437 4 0 3 6.8 FC(F)(F)Cc1cnc2c(Cl)c(-c3cc(Cl)c4c(ccn4CC4CC4)c3)ccn12 10.1021/jm201561r
CHEMBL2152122 80844 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 437 4 0 3 6.8 FC(F)(F)Cc1cnc2c(Cl)c(-c3cc(Cl)c4c(ccn4CC4CC4)c3)ccn12 10.1021/jm201561r
44155645 8698 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 272 6 0 3 3.9 CCCCCCC1CN(c2cccc(C#N)c2)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1095745 8698 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 272 6 0 3 3.9 CCCCCCC1CN(c2cccc(C#N)c2)C(=O)O1 10.1016/j.bmcl.2010.03.089
51030965 167246 None 0 Rat Functional pEC50 = 6.6 6.6 -1 2
Positive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis
ChEMBL 312 3 0 5 2.3 CC1(C)CCc2cc(OC[C@@H]3Cn4ccc(=O)nc4O3)ccc21 10.1016/j.bmcl.2018.08.022
CHEMBL4290744 167246 None 0 Rat Functional pEC50 = 6.6 6.6 -1 2
Positive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis
ChEMBL 312 3 0 5 2.3 CC1(C)CCc2cc(OC[C@@H]3Cn4ccc(=O)nc4O3)ccc21 10.1016/j.bmcl.2018.08.022
CHEMBL5083384 217346 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL None None None O=C1c2nc3cccc(Br)c3n2CCN1Cc1ccccc1 10.1021/acs.jmedchem.1c00563
CHEMBL5090853 217772 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL None None None O=C1c2nc3cccc(Br)c3n2CCN1Cc1ccccc1F 10.1021/acs.jmedchem.1c00563
156014680 177355 None 0 Human Functional pEC50 = 5.6 5.6 -2 2
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 1250 48 0 20 8.6 COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4635960 177355 None 0 Human Functional pEC50 = 5.6 5.6 -2 2
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 1250 48 0 20 8.6 COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
59497075 114645 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 376 4 0 3 4.7 O=c1c(C(F)(F)F)c(N2CCC(c3ccccc3)CC2)ccn1CC1CC1 10.1021/jm500496m
CHEMBL3337525 114645 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 376 4 0 3 4.7 O=c1c(C(F)(F)F)c(N2CCC(c3ccccc3)CC2)ccn1CC1CC1 10.1021/jm500496m
46917791 57762 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 472 6 0 4 6.7 CCCn1ccc2cc(-c3ccc(OCc4ccc(C(F)(F)F)nc4)cc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669400 57762 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 472 6 0 4 6.7 CCCn1ccc2cc(-c3ccc(OCc4ccc(C(F)(F)F)nc4)cc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
90668094 109595 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 336 7 1 4 4.1 CCCn1ccc2c(NCCc3cccc(OC)c3)cccc2c1=O 10.1039/C0MD00200C
CHEMBL3221833 109595 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 336 7 1 4 4.1 CCCn1ccc2c(NCCc3cccc(OC)c3)cccc2c1=O 10.1039/C0MD00200C
69344751 109596 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 336 7 1 4 4.1 CCCn1ccc2c(NCCc3ccc(OC)cc3)cccc2c1=O 10.1039/C0MD00200C
CHEMBL3221834 109596 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 336 7 1 4 4.1 CCCn1ccc2c(NCCc3ccc(OC)cc3)cccc2c1=O 10.1039/C0MD00200C
58966955 109599 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 337 7 0 4 4.0 CCCn1ccc2c(OCCc3ccc(OC)cc3)cccc2c1=O 10.1039/C0MD00200C
CHEMBL3221837 109599 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 337 7 0 4 4.0 CCCn1ccc2c(OCCc3ccc(OC)cc3)cccc2c1=O 10.1039/C0MD00200C
90668103 109608 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 340 6 0 3 4.6 CCCn1ccc2c(N(Cl)CCc3ccccc3)cccc2c1=O 10.1039/C0MD00200C
CHEMBL3221845 109608 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 340 6 0 3 4.6 CCCn1ccc2c(N(Cl)CCc3ccccc3)cccc2c1=O 10.1039/C0MD00200C
49801371 158833 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 408 5 0 5 5.6 Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)ccn1 10.1021/acs.jmedchem.7b00669
CHEMBL4093620 158833 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 408 5 0 5 5.6 Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)ccn1 10.1021/acs.jmedchem.7b00669
53326074 57745 None 0 Human Functional pEC50 = 5.6 5.6 - 1
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 328 5 0 4 4.0 CCCn1ccc2cc(OCc3cccnc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669384 57745 None 0 Human Functional pEC50 = 5.6 5.6 - 1
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 328 5 0 4 4.0 CCCn1ccc2cc(OCc3cccnc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
46225334 202502 None 0 Human Functional pEC50 = 5.6 5.6 - 1
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 358 3 0 4 3.7 Cn1c(CN2CCN(c3ccc(Cl)cc3F)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL595607 202502 None 0 Human Functional pEC50 = 5.6 5.6 - 1
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 358 3 0 4 3.7 Cn1c(CN2CCN(c3ccc(Cl)cc3F)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
46225583 202630 None 0 Human Functional pEC50 = 5.6 5.6 - 1
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 362 3 0 5 4.6 Cn1c(CN2CCC(c3nsc4ccccc34)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL596527 202630 None 0 Human Functional pEC50 = 5.6 5.6 - 1
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 362 3 0 5 4.6 Cn1c(CN2CCC(c3nsc4ccccc34)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
24815883 203919 None 0 Human Functional pEC50 = 5.6 5.6 - 1
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 373 3 0 3 5.0 Cn1c(CN2CCC(c3cccc(C(F)(F)F)c3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL604993 203919 None 0 Human Functional pEC50 = 5.6 5.6 - 1
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 373 3 0 3 5.0 Cn1c(CN2CCC(c3cccc(C(F)(F)F)c3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
53325603 57739 None 0 Human Functional pEC50 = 5.6 5.6 - 1
Agonist activity at human mGluR2 expressed in HEK293 cells assessed as induction of calcium release by FLIPR assayAgonist activity at human mGluR2 expressed in HEK293 cells assessed as induction of calcium release by FLIPR assay
ChEMBL 306 3 0 4 2.9 CCCn1ccc2cc(N3CCOCC3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669377 57739 None 0 Human Functional pEC50 = 5.6 5.6 - 1
Agonist activity at human mGluR2 expressed in HEK293 cells assessed as induction of calcium release by FLIPR assayAgonist activity at human mGluR2 expressed in HEK293 cells assessed as induction of calcium release by FLIPR assay
ChEMBL 306 3 0 4 2.9 CCCn1ccc2cc(N3CCOCC3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
21393580 8695 None 0 Human Functional pEC50 = 4.6 4.6 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 253 3 0 2 3.3 O=C1OC(Cc2ccccc2)CN1c1ccccc1 10.1016/j.bmcl.2010.03.089
CHEMBL1095704 8695 None 0 Human Functional pEC50 = 4.6 4.6 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 253 3 0 2 3.3 O=C1OC(Cc2ccccc2)CN1c1ccccc1 10.1016/j.bmcl.2010.03.089
60096211 90093 None 0 Human Functional pEC50 = 6.6 6.6 -1 4
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 242 3 4 4 -1.4 CC(=O)N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/acs.jmedchem.7b01481
CHEMBL2381649 90093 None 0 Human Functional pEC50 = 6.6 6.6 -1 4
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 242 3 4 4 -1.4 CC(=O)N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/acs.jmedchem.7b01481
1310 2315 None 61 Human Functional pEC50 = 5.6 5.6 -389 17
Agonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
1369 2315 None 61 Human Functional pEC50 = 5.6 5.6 -389 17
Agonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
33032 2315 None 61 Human Functional pEC50 = 5.6 5.6 -389 17
Agonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
44272391 2315 None 61 Human Functional pEC50 = 5.6 5.6 -389 17
Agonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
88747398 2315 None 61 Human Functional pEC50 = 5.6 5.6 -389 17
Agonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
CHEMBL575060 2315 None 61 Human Functional pEC50 = 5.6 5.6 -389 17
Agonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
DB00142 2315 None 61 Human Functional pEC50 = 5.6 5.6 -389 17
Agonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01124
69093106 83940 None 0 Human Functional pEC50 = 7.6 7.6 - 1
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 432 5 0 5 5.0 COc1c(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)ccc(F)c1F 10.1021/jm300912k
CHEMBL2206444 83940 None 0 Human Functional pEC50 = 7.6 7.6 - 1
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 432 5 0 5 5.0 COc1c(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)ccc(F)c1F 10.1021/jm300912k
44591748 185147 None 0 Human Functional pEC50 = 7.6 7.6 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 311 5 0 3 4.1 CCOc1ccccc1-c1ccc(CN2C[C@@H](C)OC2=O)cc1 10.1016/j.bmcl.2009.03.032
CHEMBL485528 185147 None 0 Human Functional pEC50 = 7.6 7.6 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 311 5 0 3 4.1 CCOc1ccccc1-c1ccc(CN2C[C@@H](C)OC2=O)cc1 10.1016/j.bmcl.2009.03.032
60096183 159377 None 0 Human Functional pEC50 = 7.6 7.6 -3 2
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 334 5 4 5 -0.1 COc1ccccc1C(=O)N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/acs.jmedchem.7b01481
CHEMBL4099470 159377 None 0 Human Functional pEC50 = 7.6 7.6 -3 2
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 334 5 4 5 -0.1 COc1ccccc1C(=O)N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/acs.jmedchem.7b01481
24809650 74611 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 326 6 0 5 3.5 COc1ccc(-c2ccn(CCC(C)C)c(=O)c2C#N)cc1OC 10.1021/jm2016864
CHEMBL2029792 74611 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 326 6 0 5 3.5 COc1ccc(-c2ccn(CCC(C)C)c(=O)c2C#N)cc1OC 10.1021/jm2016864
162665716 182475 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 323 5 0 4 4.0 c1ccc(SCCCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
CHEMBL4784990 182475 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 323 5 0 4 4.0 c1ccc(SCCCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
1310 2315 None 61 Human Functional pEC50 = 4.6 4.6 -389 17
Activity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assayActivity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmcl.2005.09.014
1369 2315 None 61 Human Functional pEC50 = 4.6 4.6 -389 17
Activity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assayActivity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmcl.2005.09.014
33032 2315 None 61 Human Functional pEC50 = 4.6 4.6 -389 17
Activity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assayActivity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmcl.2005.09.014
44272391 2315 None 61 Human Functional pEC50 = 4.6 4.6 -389 17
Activity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assayActivity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmcl.2005.09.014
88747398 2315 None 61 Human Functional pEC50 = 4.6 4.6 -389 17
Activity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assayActivity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmcl.2005.09.014
CHEMBL575060 2315 None 61 Human Functional pEC50 = 4.6 4.6 -389 17
Activity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assayActivity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmcl.2005.09.014
DB00142 2315 None 61 Human Functional pEC50 = 4.6 4.6 -389 17
Activity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assayActivity at human mGluR2 from BHK cells in [35S]GTP-gamma-S stimulation assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmcl.2005.09.014
1310 2315 None 61 Human Functional pEC50 = 4.6 4.6 -389 17
Activity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S bindingActivity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S binding
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmc.2007.02.040
1369 2315 None 61 Human Functional pEC50 = 4.6 4.6 -389 17
Activity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S bindingActivity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S binding
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmc.2007.02.040
33032 2315 None 61 Human Functional pEC50 = 4.6 4.6 -389 17
Activity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S bindingActivity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S binding
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmc.2007.02.040
44272391 2315 None 61 Human Functional pEC50 = 4.6 4.6 -389 17
Activity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S bindingActivity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S binding
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmc.2007.02.040
88747398 2315 None 61 Human Functional pEC50 = 4.6 4.6 -389 17
Activity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S bindingActivity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S binding
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmc.2007.02.040
CHEMBL575060 2315 None 61 Human Functional pEC50 = 4.6 4.6 -389 17
Activity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S bindingActivity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S binding
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmc.2007.02.040
DB00142 2315 None 61 Human Functional pEC50 = 4.6 4.6 -389 17
Activity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S bindingActivity at human recombinant mGluR2 expressed in BHK cells assessed as stimulation of [35S]GTP-gamma-S binding
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmc.2007.02.040
25173365 184911 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 297 5 0 3 3.6 CC1CN(Cc2ccc(OCc3ccccc3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL485175 184911 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 297 5 0 3 3.6 CC1CN(Cc2ccc(OCc3ccccc3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
70685767 74635 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 371 5 0 5 4.6 Cc1ccc(Oc2ccc(-c3ccn(CC4CC4)c(=O)c3C#N)cc2)c(C)n1 10.1021/jm2016864
CHEMBL2029814 74635 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 371 5 0 5 4.6 Cc1ccc(Oc2ccc(-c3ccn(CC4CC4)c(=O)c3C#N)cc2)c(C)n1 10.1021/jm2016864
CHEMBL5073573 216788 None 0 Human Functional pEC50 = 5.6 5.6 - 1
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL None None None O=C1c2nc3cccc([N+](=O)[O-])c3n2CCN1CC1CC1 10.1021/acs.jmedchem.1c00563
9815616 114864 None 4 Rat Functional pEC50 = 5.6 5.6 -2 4
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 203 2 3 3 -0.5 N[C@@]1(C(=O)O)[C@@H](F)C[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm000346k
CHEMBL334014 114864 None 4 Rat Functional pEC50 = 5.6 5.6 -2 4
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 203 2 3 3 -0.5 N[C@@]1(C(=O)O)[C@@H](F)C[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm000346k
71136188 145843 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 384 3 1 6 1.6 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)CO)CC4C3)nc21 nan
CHEMBL3916627 145843 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 384 3 1 6 1.6 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)CO)CC4C3)nc21 nan
155515810 170117 None 0 Human Functional pEC50 = 7.6 7.6 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 356 3 0 4 4.5 Fc1cc(Cl)ccc1-c1ccc(Cn2nnc3c(F)cccc32)cn1 10.1021/acs.jmedchem.8b00161
CHEMBL4442487 170117 None 0 Human Functional pEC50 = 7.6 7.6 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 356 3 0 4 4.5 Fc1cc(Cl)ccc1-c1ccc(Cn2nnc3c(F)cccc32)cn1 10.1021/acs.jmedchem.8b00161
3954 664 None 44 Human Functional pEC50 = 7.6 7.6 6 3
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 454 6 1 3 6.8 Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1 10.1016/j.bmcl.2009.11.008
9868580 664 None 44 Human Functional pEC50 = 7.6 7.6 6 3
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 454 6 1 3 6.8 Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1 10.1016/j.bmcl.2009.11.008
CHEMBL593013 664 None 44 Human Functional pEC50 = 7.6 7.6 6 3
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 454 6 1 3 6.8 Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1 10.1016/j.bmcl.2009.11.008
49765871 2145 None 41 Human Functional pEC50 = 6.6 6.6 - 1
Agonist activity at human mGlu2R expressed in CHO cellsAgonist activity at human mGlu2R expressed in CHO cells
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/jm3010724
6317 2145 None 41 Human Functional pEC50 = 6.6 6.6 - 1
Agonist activity at human mGlu2R expressed in CHO cellsAgonist activity at human mGlu2R expressed in CHO cells
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/jm3010724
CHEMBL2179319 2145 None 41 Human Functional pEC50 = 6.6 6.6 - 1
Agonist activity at human mGlu2R expressed in CHO cellsAgonist activity at human mGlu2R expressed in CHO cells
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/jm3010724
162677102 183632 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 401 5 0 4 4.8 Brc1ccc(SCCCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
CHEMBL4799882 183632 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 401 5 0 4 4.8 Brc1ccc(SCCCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
155511507 169697 None 1 Human Functional pEC50 = 6.6 6.6 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 239 2 0 3 2.6 CCCn1nnc2c(Br)cccc21 10.1021/acs.jmedchem.8b00161
CHEMBL4436220 169697 None 1 Human Functional pEC50 = 6.6 6.6 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 239 2 0 3 2.6 CCCn1nnc2c(Br)cccc21 10.1021/acs.jmedchem.8b00161
44156621 8738 None 0 Human Functional pEC50 = 5.6 5.6 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 325 7 0 4 3.4 CCCCCCC1CN(c2cccc(S(C)(=O)=O)c2)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1096080 8738 None 0 Human Functional pEC50 = 5.6 5.6 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 325 7 0 4 3.4 CCCCCCC1CN(c2cccc(S(C)(=O)=O)c2)C(=O)O1 10.1016/j.bmcl.2010.03.089
134131309 142261 None 0 Human Functional pEC50 = 5.6 5.6 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells assessed as inhibition of forskolin-stimulated cAMP production by high throughput screening assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells assessed as inhibition of forskolin-stimulated cAMP production by high throughput screening assay
ChEMBL 359 2 0 3 6.1 Clc1cccc(Cl)c1-c1ccn2c(C3CCCCCC3)nnc2c1 10.1016/j.bmc.2016.11.018
CHEMBL3883923 142261 None 0 Human Functional pEC50 = 5.6 5.6 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells assessed as inhibition of forskolin-stimulated cAMP production by high throughput screening assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells assessed as inhibition of forskolin-stimulated cAMP production by high throughput screening assay
ChEMBL 359 2 0 3 6.1 Clc1cccc(Cl)c1-c1ccn2c(C3CCCCCC3)nnc2c1 10.1016/j.bmc.2016.11.018
67060140 167493 None 0 Human Functional pEC50 = 6.6 6.6 -26 2
Positive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis
ChEMBL 362 4 0 5 3.7 Cc1cccc(-c2ccc(OC[C@@H]3Cn4c(C)cc(=O)nc4O3)cc2)c1C 10.1016/j.bmcl.2018.08.022
CHEMBL4295230 167493 None 0 Human Functional pEC50 = 6.6 6.6 -26 2
Positive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis
ChEMBL 362 4 0 5 3.7 Cc1cccc(-c2ccc(OC[C@@H]3Cn4c(C)cc(=O)nc4O3)cc2)c1C 10.1016/j.bmcl.2018.08.022
162661604 181609 None 0 Human Functional pEC50 = 5.6 5.6 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 307 4 0 4 3.1 COc1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
CHEMBL4764905 181609 None 0 Human Functional pEC50 = 5.6 5.6 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 307 4 0 4 3.1 COc1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
44591746 185021 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 297 4 0 3 3.7 COc1cccc(-c2ccc(CN3C[C@@H](C)OC3=O)cc2)c1 10.1016/j.bmcl.2009.03.032
CHEMBL485330 185021 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 297 4 0 3 3.7 COc1cccc(-c2ccc(CN3C[C@@H](C)OC3=O)cc2)c1 10.1016/j.bmcl.2009.03.032
70685766 74631 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 373 6 0 5 4.9 Cc1ncccc1Oc1ccc(-c2ccn(CCC(C)C)c(=O)c2C#N)cc1 10.1021/jm2016864
CHEMBL2029810 74631 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 373 6 0 5 4.9 Cc1ncccc1Oc1ccc(-c2ccn(CCC(C)C)c(=O)c2C#N)cc1 10.1021/jm2016864
60096231 157747 None 19 Human Functional pEC50 = 6.6 6.6 -48 4
Agonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing rat EAAT1/Galpha15 assessed as induction of increase in Ca2+ flux after 2.5 mins by Fluo-3 AM dye-based FLIPR assayAgonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing rat EAAT1/Galpha15 assessed as induction of increase in Ca2+ flux after 2.5 mins by Fluo-3 AM dye-based FLIPR assay
ChEMBL 334 5 4 5 -0.1 COc1cccc(C(=O)N[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)c1 10.1021/acs.jmedchem.7b01481
CHEMBL4081453 157747 None 19 Human Functional pEC50 = 6.6 6.6 -48 4
Agonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing rat EAAT1/Galpha15 assessed as induction of increase in Ca2+ flux after 2.5 mins by Fluo-3 AM dye-based FLIPR assayAgonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing rat EAAT1/Galpha15 assessed as induction of increase in Ca2+ flux after 2.5 mins by Fluo-3 AM dye-based FLIPR assay
ChEMBL 334 5 4 5 -0.1 COc1cccc(C(=O)N[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)c1 10.1021/acs.jmedchem.7b01481
44591715 191584 None 0 Human Functional pEC50 = 7.6 7.6 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 301 3 0 2 4.3 C[C@@H]1CN(Cc2ccc(-c3ccccc3Cl)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL519341 191584 None 0 Human Functional pEC50 = 7.6 7.6 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 301 3 0 2 4.3 C[C@@H]1CN(Cc2ccc(-c3ccccc3Cl)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
117967312 142397 None 4 Human Functional pEC50 = 7.6 7.6 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells assessed as inhibition of forskolin-stimulated cAMP production by high throughput screening assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells assessed as inhibition of forskolin-stimulated cAMP production by high throughput screening assay
ChEMBL 347 5 0 4 4.3 FC(F)(F)c1c(OCc2ccccc2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
CHEMBL3885353 142397 None 4 Human Functional pEC50 = 7.6 7.6 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells assessed as inhibition of forskolin-stimulated cAMP production by high throughput screening assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells assessed as inhibition of forskolin-stimulated cAMP production by high throughput screening assay
ChEMBL 347 5 0 4 4.3 FC(F)(F)c1c(OCc2ccccc2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
117967312 142397 None 4 Human Functional pEC50 = 7.6 7.6 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 347 5 0 4 4.3 FC(F)(F)c1c(OCc2ccccc2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
CHEMBL3885353 142397 None 4 Human Functional pEC50 = 7.6 7.6 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 347 5 0 4 4.3 FC(F)(F)c1c(OCc2ccccc2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
155551721 175533 None 0 Human Functional pEC50 = 7.6 7.6 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 337 3 0 3 4.9 Fc1cc(Cl)ccc1-c1ccc(Cn2nnc3ccccc32)cc1 10.1021/acs.jmedchem.8b00161
CHEMBL4576215 175533 None 0 Human Functional pEC50 = 7.6 7.6 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 337 3 0 3 4.9 Fc1cc(Cl)ccc1-c1ccc(Cn2nnc3ccccc32)cc1 10.1021/acs.jmedchem.8b00161
51357935 61996 None 0 Rat Functional pEC50 = 7.6 7.6 - 1
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 372 3 0 4 4.4 C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(Cl)cc1F 10.1021/jm101414h
CHEMBL1774229 61996 None 0 Rat Functional pEC50 = 7.6 7.6 - 1
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 372 3 0 4 4.4 C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(Cl)cc1F 10.1021/jm101414h
168299593 192841 None 0 Human Functional pEC50 = 7.6 7.6 - 1
Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding
ChEMBL 385 7 0 5 4.7 CCCCn1ccn2c(-c3ccc(OCC4CC4)c(Cl)c3)c(C)nc2c1=O 10.1021/acs.jmedchem.2c00969
CHEMBL5220316 192841 None 0 Human Functional pEC50 = 7.6 7.6 - 1
Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding
ChEMBL 385 7 0 5 4.7 CCCCn1ccn2c(-c3ccc(OCC4CC4)c(Cl)c3)c(C)nc2c1=O 10.1021/acs.jmedchem.2c00969
71116726 145364 None 0 Human Functional pEC50 = 7.6 7.6 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 438 3 0 8 3.0 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3csnn3)nc21 nan
CHEMBL3912982 145364 None 0 Human Functional pEC50 = 7.6 7.6 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 438 3 0 8 3.0 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3csnn3)nc21 nan
137652500 157281 None 0 Human Functional pEC50 = 7.6 7.6 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 430 6 0 5 6.4 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(C)C)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4075697 157281 None 0 Human Functional pEC50 = 7.6 7.6 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 430 6 0 5 6.4 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(C)C)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
71128768 144668 None 0 Human Functional pEC50 = 7.5 7.5 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 441 4 0 7 2.7 Cn1c(=O)n(CC2CC2(F)F)c2ccc(C3=CC4CCC3CN4C(=O)c3ccon3)nc21 nan
CHEMBL3907644 144668 None 0 Human Functional pEC50 = 7.5 7.5 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 441 4 0 7 2.7 Cn1c(=O)n(CC2CC2(F)F)c2ccc(C3=CC4CCC3CN4C(=O)c3ccon3)nc21 nan
44591714 184407 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 285 3 0 2 3.8 C[C@@H]1CN(Cc2ccc(-c3cccc(F)c3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL484127 184407 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 285 3 0 2 3.8 C[C@@H]1CN(Cc2ccc(-c3cccc(F)c3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL5069547 216707 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL None None None O=C1c2nc3cccc(Br)c3n2CCN1Cc1ccc(F)cc1 10.1021/acs.jmedchem.1c00563
118714743 114630 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 335 4 0 4 3.8 CC(C)Cn1ccc(N2CCC(c3ccccc3)CC2)c(C#N)c1=O 10.1021/jm500496m
CHEMBL3337509 114630 None 0 Human Functional pEC50 = 6.6 6.6 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 335 4 0 4 3.8 CC(C)Cn1ccc(N2CCC(c3ccccc3)CC2)c(C#N)c1=O 10.1021/jm500496m
25010196 61983 None 0 Rat Functional pEC50 = 6.5 6.5 - 1
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 374 3 0 4 4.4 Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2cccnc21 10.1021/jm101414h
CHEMBL1774111 61983 None 0 Rat Functional pEC50 = 6.5 6.5 - 1
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 374 3 0 4 4.4 Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2cccnc21 10.1021/jm101414h
134131502 142239 None 0 Human Functional pEC50 = 7.5 7.5 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 363 5 0 4 5.1 Clc1c(OCc2ccc3ccccc3c2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
CHEMBL3883585 142239 None 0 Human Functional pEC50 = 7.5 7.5 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 363 5 0 4 5.1 Clc1c(OCc2ccc3ccccc3c2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
155525998 171138 None 0 Human Functional pEC50 = 7.5 7.5 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 371 3 0 3 5.3 Fc1cc(C(F)(F)F)ccc1-c1ccc(Cn2nnc3ccccc32)cc1 10.1021/acs.jmedchem.8b00161
CHEMBL4456816 171138 None 0 Human Functional pEC50 = 7.5 7.5 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 371 3 0 3 5.3 Fc1cc(C(F)(F)F)ccc1-c1ccc(Cn2nnc3ccccc32)cc1 10.1021/acs.jmedchem.8b00161
9815616 114864 None 4 Rat Functional pEC50 = 7.5 7.5 -2 4
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 203 2 3 3 -0.5 N[C@@]1(C(=O)O)[C@@H](F)C[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm000346k
CHEMBL334014 114864 None 4 Rat Functional pEC50 = 7.5 7.5 -2 4
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 203 2 3 3 -0.5 N[C@@]1(C(=O)O)[C@@H](F)C[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm000346k
66785010 155953 None 0 Human Functional pEC50 = 7.5 7.5 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 372 5 1 4 5.2 Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4060306 155953 None 0 Human Functional pEC50 = 7.5 7.5 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 372 5 1 4 5.2 Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CC1 10.1021/acs.jmedchem.7b00669
66787433 156554 None 0 Human Functional pEC50 = 7.5 7.5 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 460 6 0 6 5.9 CCOCc1nnc2c(C(F)(F)F)c(-c3ccc(Oc4ccc(C)nc4C)c(F)c3)ccn12 10.1021/acs.jmedchem.7b00669
CHEMBL4067298 156554 None 0 Human Functional pEC50 = 7.5 7.5 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 460 6 0 6 5.9 CCOCc1nnc2c(C(F)(F)F)c(-c3ccc(Oc4ccc(C)nc4C)c(F)c3)ccn12 10.1021/acs.jmedchem.7b00669
49801369 158841 None 0 Human Functional pEC50 = 7.5 7.5 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 450 4 0 5 6.1 Cc1ccc(Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4093792 158841 None 0 Human Functional pEC50 = 7.5 7.5 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 450 4 0 5 6.1 Cc1ccc(Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
25073303 167129 None 0 Rat Functional pEC50 = 7.5 7.5 11 2
Positive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis
ChEMBL 348 4 0 5 3.4 Cc1cccc(-c2ccc(OC[C@@H]3Cn4ccc(=O)nc4O3)cc2)c1C 10.1016/j.bmcl.2018.08.022
CHEMBL4288731 167129 None 0 Rat Functional pEC50 = 7.5 7.5 11 2
Positive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis
ChEMBL 348 4 0 5 3.4 Cc1cccc(-c2ccc(OC[C@@H]3Cn4ccc(=O)nc4O3)cc2)c1C 10.1016/j.bmcl.2018.08.022
156018381 178027 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 440 8 0 6 4.7 COCCOc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1 10.1021/acs.jmedchem.0c01058
CHEMBL4645305 178027 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 440 8 0 6 4.7 COCCOc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1 10.1021/acs.jmedchem.0c01058
70689923 74612 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 336 7 0 4 4.2 CC(C)CCn1ccc(-c2ccc(OCC3CC3)cc2)c(C#N)c1=O 10.1021/jm2016864
CHEMBL2029793 74612 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 336 7 0 4 4.2 CC(C)CCn1ccc(-c2ccc(OCC3CC3)cc2)c(C#N)c1=O 10.1021/jm2016864
155524603 171029 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 322 2 0 4 3.3 Clc1ccc(Cn2nnc3c(Br)cccc32)cn1 10.1021/acs.jmedchem.8b00161
CHEMBL4455228 171029 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 322 2 0 4 3.3 Clc1ccc(Cn2nnc3c(Br)cccc32)cn1 10.1021/acs.jmedchem.8b00161
CHEMBL5091768 217815 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL None None None O=C1c2nc3cccc(-c4ccc(Cl)cc4)c3n2CCN1CC1CC1 10.1021/acs.jmedchem.1c00563
11690196 142853 None 0 Human Functional pEC50 = 6.5 6.5 4 2
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 416 7 2 7 4.5 CC(=O)c1ccc(OCc2ccc(Oc3cccc(-c4nn[nH]n4)c3)cc2)c(C)c1O 10.1016/j.bmcl.2016.11.049
CHEMBL3892611 142853 None 0 Human Functional pEC50 = 6.5 6.5 4 2
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 416 7 2 7 4.5 CC(=O)c1ccc(OCc2ccc(Oc3cccc(-c4nn[nH]n4)c3)cc2)c(C)c1O 10.1016/j.bmcl.2016.11.049
156018381 178027 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 440 8 0 6 4.7 COCCOc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1 10.1021/acs.jmedchem.0c01058
CHEMBL4645305 178027 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 440 8 0 6 4.7 COCCOc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1 10.1021/acs.jmedchem.0c01058
118714734 114620 None 0 Human Functional pEC50 = 5.5 5.5 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 296 6 0 4 3.3 CC(C)CCn1ccc(OCc2ccccc2)c(C#N)c1=O 10.1021/jm500496m
CHEMBL3337499 114620 None 0 Human Functional pEC50 = 5.5 5.5 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 296 6 0 4 3.3 CC(C)CCn1ccc(OCc2ccccc2)c(C#N)c1=O 10.1021/jm500496m
57459483 82685 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 345 4 0 5 3.9 CCCc1nnc2c(C#N)c(N3CCC(c4ccccc4)CC3)ccn12 10.1021/jm3010724
CHEMBL2179331 82685 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 345 4 0 5 3.9 CCCc1nnc2c(C#N)c(N3CCC(c4ccccc4)CC3)ccn12 10.1021/jm3010724
51357937 61999 None 0 Human Functional pEC50 = 8.5 8.5 2 2
Positive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 406 3 0 4 4.8 C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(C(F)(F)F)cc1F 10.1021/jm101414h
CHEMBL1774233 61999 None 0 Human Functional pEC50 = 8.5 8.5 2 2
Positive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 406 3 0 4 4.8 C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(C(F)(F)F)cc1F 10.1021/jm101414h
60096201 158660 None 0 Human Functional pEC50 = 8.4 8.4 -5 2
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 320 4 5 5 -0.4 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2cccc(O)c2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4091735 158660 None 0 Human Functional pEC50 = 8.4 8.4 -5 2
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 320 4 5 5 -0.4 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2cccc(O)c2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
10198133 208966 None 10 Human Functional pEC50 = 8.4 8.4 1 4
Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells
ChEMBL 203 2 3 4 -0.8 N[C@@]1(C(=O)O)CS[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm060917u
CHEMBL8839 208966 None 10 Human Functional pEC50 = 8.4 8.4 1 4
Agonist activity at human mGluR2 assessed as effect on cAMP production in RGT cellsAgonist activity at human mGluR2 assessed as effect on cAMP production in RGT cells
ChEMBL 203 2 3 4 -0.8 N[C@@]1(C(=O)O)CS[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm060917u
10198133 208966 None 10 Human Functional pEC50 = 8.4 8.4 1 4
Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2
ChEMBL 203 2 3 4 -0.8 N[C@@]1(C(=O)O)CS[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm980616n
CHEMBL8839 208966 None 10 Human Functional pEC50 = 8.4 8.4 1 4
Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2Inhibition of forskolin stimulated cAMP production in RGT cells expressing recombinant human Metabotropic glutamate receptor 2
ChEMBL 203 2 3 4 -0.8 N[C@@]1(C(=O)O)CS[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm980616n
42629118 184365 None 0 Human Functional pEC50 = 7.5 7.5 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 319 3 0 2 4.5 C[C@@H]1CN(Cc2ccc(-c3ccc(F)c(Cl)c3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL483750 184365 None 0 Human Functional pEC50 = 7.5 7.5 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 319 3 0 2 4.5 C[C@@H]1CN(Cc2ccc(-c3ccc(F)c(Cl)c3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
70696264 74640 None 0 Human Functional pEC50 = 7.5 7.5 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 407 6 0 5 5.6 CCCCn1ccc(-c2ccc(Oc3ccc(C)nc3C)c(Cl)c2)c(C#N)c1=O 10.1021/jm2016864
CHEMBL2029819 74640 None 0 Human Functional pEC50 = 7.5 7.5 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 407 6 0 5 5.6 CCCCn1ccc(-c2ccc(Oc3ccc(C)nc3C)c(Cl)c2)c(C#N)c1=O 10.1021/jm2016864
162662455 182128 None 4 Human Functional pEC50 = 7.5 7.5 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 419 7 0 5 4.3 O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(OC(F)(F)F)cc1 10.1016/j.ejmech.2019.111881
CHEMBL4780781 182128 None 4 Human Functional pEC50 = 7.5 7.5 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 419 7 0 5 4.3 O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(OC(F)(F)F)cc1 10.1016/j.ejmech.2019.111881
146036862 175742 None 6 Human Functional pEC50 = 7.5 7.5 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 279 2 0 3 3.4 Brc1cccc2c1nnn2CC1CCCC1 10.1021/acs.jmedchem.8b00161
CHEMBL4580916 175742 None 6 Human Functional pEC50 = 7.5 7.5 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 279 2 0 3 3.4 Brc1cccc2c1nnn2CC1CCCC1 10.1021/acs.jmedchem.8b00161
162662455 182128 None 4 Human Functional pEC50 = 7.5 7.5 - 1
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL 419 7 0 5 4.3 O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(OC(F)(F)F)cc1 10.1021/acs.jmedchem.1c00563
CHEMBL4780781 182128 None 4 Human Functional pEC50 = 7.5 7.5 - 1
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL 419 7 0 5 4.3 O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(OC(F)(F)F)cc1 10.1021/acs.jmedchem.1c00563
CHEMBL5085978 217495 None 0 Human Functional pEC50 = 7.5 7.5 - 1
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL None None None O=C1c2nc3cccc(Br)c3n2CCN1Cc1ccc(Cl)cc1 10.1021/acs.jmedchem.1c00563
66785087 158232 None 0 Human Functional pEC50 = 7.5 7.5 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 390 5 1 4 5.1 Fc1cc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)ccc1NC1CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4087196 158232 None 0 Human Functional pEC50 = 7.5 7.5 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 390 5 1 4 5.1 Fc1cc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)ccc1NC1CC1 10.1021/acs.jmedchem.7b00669
11362035 42 None 1 Human Functional pEC50 = 7.5 7.5 - 1
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 416 9 0 4 4.5 CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C 10.1016/j.bmcl.2009.11.008
6328 42 None 1 Human Functional pEC50 = 7.5 7.5 - 1
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 416 9 0 4 4.5 CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C 10.1016/j.bmcl.2009.11.008
6329 42 None 1 Human Functional pEC50 = 7.5 7.5 - 1
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 416 9 0 4 4.5 CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C 10.1016/j.bmcl.2009.11.008
CHEMBL105296 42 None 1 Human Functional pEC50 = 7.5 7.5 - 1
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 416 9 0 4 4.5 CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C 10.1016/j.bmcl.2009.11.008
156010124 177136 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 396 5 0 5 4.7 COc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1 10.1021/acs.jmedchem.0c01058
CHEMBL4632373 177136 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 396 5 0 5 4.7 COc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1 10.1021/acs.jmedchem.0c01058
1377 1340 None 23 Rat Functional pEC50 = 6.5 6.5 1 8
Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells
ChEMBL 203 4 4 4 -1.6 N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O 10.1021/jm030967o
5310979 1340 None 23 Rat Functional pEC50 = 6.5 6.5 1 8
Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells
ChEMBL 203 4 4 4 -1.6 N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O 10.1021/jm030967o
CHEMBL284193 1340 None 23 Rat Functional pEC50 = 6.5 6.5 1 8
Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells
ChEMBL 203 4 4 4 -1.6 N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O 10.1021/jm030967o
1368 2290 None 30 Rat Functional pEC50 = 6.5 6.5 -1 11
Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells
ChEMBL 159 3 3 3 -0.9 N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O 10.1021/jm030967o
5310956 2290 None 30 Rat Functional pEC50 = 6.5 6.5 -1 11
Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells
ChEMBL 159 3 3 3 -0.9 N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O 10.1021/jm030967o
CHEMBL280563 2290 None 30 Rat Functional pEC50 = 6.5 6.5 -1 11
Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells
ChEMBL 159 3 3 3 -0.9 N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O 10.1021/jm030967o
44361316 34981 None 2 Rat Functional pEC50 = 6.5 6.5 - 1
Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells
ChEMBL 217 5 4 4 -1.2 N[C@H](C(=O)O)[C@H]1[C@H](CC(=O)O)[C@@H]1C(=O)O 10.1021/jm030967o
CHEMBL143267 34981 None 2 Rat Functional pEC50 = 6.5 6.5 - 1
Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells
ChEMBL 217 5 4 4 -1.2 N[C@H](C(=O)O)[C@H]1[C@H](CC(=O)O)[C@@H]1C(=O)O 10.1021/jm030967o
1392 73 None 32 Rat Functional pEC50 = 6.5 6.5 5 4
Tested for the agonistic activity against Metabotropic glutamate receptor 2Tested for the agonistic activity against Metabotropic glutamate receptor 2
ChEMBL 174 2 4 4 -1.8 OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O 10.1016/S0960-894X(97)00068-1
5310984 73 None 32 Rat Functional pEC50 = 6.5 6.5 5 4
Tested for the agonistic activity against Metabotropic glutamate receptor 2Tested for the agonistic activity against Metabotropic glutamate receptor 2
ChEMBL 174 2 4 4 -1.8 OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O 10.1016/S0960-894X(97)00068-1
CHEMBL40086 73 None 32 Rat Functional pEC50 = 6.5 6.5 5 4
Tested for the agonistic activity against Metabotropic glutamate receptor 2Tested for the agonistic activity against Metabotropic glutamate receptor 2
ChEMBL 174 2 4 4 -1.8 OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O 10.1016/S0960-894X(97)00068-1
521212 67355 None 45 Human Functional pEC50 = 5.5 5.5 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 209 2 0 3 2.5 c1ccc(Cn2nnc3ccccc32)cc1 10.1021/acs.jmedchem.8b00161
CHEMBL1884989 67355 None 45 Human Functional pEC50 = 5.5 5.5 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 209 2 0 3 2.5 c1ccc(Cn2nnc3ccccc32)cc1 10.1021/acs.jmedchem.8b00161
156010124 177136 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 396 5 0 5 4.7 COc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1 10.1021/acs.jmedchem.0c01058
CHEMBL4632373 177136 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 396 5 0 5 4.7 COc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1 10.1021/acs.jmedchem.0c01058
44591812 192662 None 0 Human Functional pEC50 = 5.5 5.5 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 324 5 0 3 3.8 C[C@@H]1CN(Cc2ccc(-c3ccc(CN(C)C)cc3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL521175 192662 None 0 Human Functional pEC50 = 5.5 5.5 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 324 5 0 3 3.8 C[C@@H]1CN(Cc2ccc(-c3ccc(CN(C)C)cc3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
59599459 149517 None 0 Human Functional pEC50 = 6.5 6.5 1 2
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 445 9 2 8 4.5 CCCc1c(OCc2ccc(Oc3ncccc3-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2016.11.049
CHEMBL3945882 149517 None 0 Human Functional pEC50 = 6.5 6.5 1 2
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 445 9 2 8 4.5 CCCc1c(OCc2ccc(Oc3ncccc3-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2016.11.049
118714740 114627 None 0 Human Functional pEC50 = 5.5 5.5 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 351 5 0 6 2.5 CC(C)CCn1ccc(N2CCN(c3ccccn3)CC2)c(C#N)c1=O 10.1021/jm500496m
CHEMBL3337506 114627 None 0 Human Functional pEC50 = 5.5 5.5 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 351 5 0 6 2.5 CC(C)CCn1ccc(N2CCN(c3ccccn3)CC2)c(C#N)c1=O 10.1021/jm500496m
57459482 83934 None 0 Human Functional pEC50 = 7.5 7.5 - 1
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 433 4 0 6 4.2 COc1c(F)cccc1C1CCN(c2ccn3c(CC(F)(F)F)nnc3c2C#N)CC1 10.1021/jm300912k
CHEMBL2206438 83934 None 0 Human Functional pEC50 = 7.5 7.5 - 1
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 433 4 0 6 4.2 COc1c(F)cccc1C1CCN(c2ccn3c(CC(F)(F)F)nnc3c2C#N)CC1 10.1021/jm300912k
118714756 114642 None 0 Human Functional pEC50 = 7.5 7.5 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 369 4 0 4 3.8 N#Cc1c(N2CCC(c3c(F)cccc3F)CC2)ccn(CC2CC2)c1=O 10.1021/jm500496m
CHEMBL3337522 114642 None 0 Human Functional pEC50 = 7.5 7.5 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 369 4 0 4 3.8 N#Cc1c(N2CCC(c3c(F)cccc3F)CC2)ccn(CC2CC2)c1=O 10.1021/jm500496m
44178197 62001 None 0 Human Functional pEC50 = 7.5 7.5 1 2
Positive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 422 4 0 5 4.6 C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(OC(F)(F)F)cc1F 10.1021/jm101414h
CHEMBL1774235 62001 None 0 Human Functional pEC50 = 7.5 7.5 1 2
Positive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 422 4 0 5 4.6 C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(OC(F)(F)F)cc1F 10.1021/jm101414h
CHEMBL5078863 217079 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL None None None O=C1c2nc3cccc(C(F)(F)F)c3n2CCN1CC1CC1 10.1021/acs.jmedchem.1c00563
25073615 166559 None 0 Rat Functional pEC50 = 6.5 6.5 4 2
Positive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis
ChEMBL 300 3 0 5 2.4 CC(C)(C)c1ccc(OC[C@@H]2Cn3ccc(=O)nc3O2)cc1 10.1016/j.bmcl.2018.08.022
CHEMBL4278070 166559 None 0 Rat Functional pEC50 = 6.5 6.5 4 2
Positive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis
ChEMBL 300 3 0 5 2.4 CC(C)(C)c1ccc(OC[C@@H]2Cn3ccc(=O)nc3O2)cc1 10.1016/j.bmcl.2018.08.022
25002940 1105 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 377 6 0 5 4.8 CCCCn1ccc(c(c1=O)C#N)c1ccc(c(c1)F)Oc1ccnc(c1)C 10.1021/jm2016864
6320 1105 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 377 6 0 5 4.8 CCCCn1ccc(c(c1=O)C#N)c1ccc(c(c1)F)Oc1ccnc(c1)C 10.1021/jm2016864
CHEMBL2029821 1105 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 377 6 0 5 4.8 CCCCn1ccc(c(c1=O)C#N)c1ccc(c(c1)F)Oc1ccnc(c1)C 10.1021/jm2016864
53326709 57756 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 405 6 0 5 5.1 CCCn1ccc2cc(-c3ccc(OCc4cccnc4)nc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669394 57756 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 405 6 0 5 5.1 CCCn1ccc2cc(-c3ccc(OCc4cccnc4)nc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
53324151 57757 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 327 4 0 3 4.7 CCCn1ccc2cc(-c3ccc(OC)cc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669395 57757 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 327 4 0 3 4.7 CCCn1ccc2cc(-c3ccc(OC)cc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
90668099 109603 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 322 6 1 4 4.0 CCCn1ccc2c(NCc3cccc(OC)c3)cccc2c1=O 10.1039/C0MD00200C
CHEMBL3221840 109603 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 322 6 1 4 4.0 CCCn1ccc2c(NCc3cccc(OC)c3)cccc2c1=O 10.1039/C0MD00200C
156017237 177866 None 0 Human Functional pEC50 = 6.5 6.5 1 2
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 853 21 0 11 8.5 COc1c(OCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4642761 177866 None 0 Human Functional pEC50 = 6.5 6.5 1 2
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 853 21 0 11 8.5 COc1c(OCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
53317704 57746 None 0 Human Functional pEC50 = 5.5 5.5 - 1
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 327 5 1 4 4.1 CCCn1ccc2cc(NCc3cccnc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669385 57746 None 0 Human Functional pEC50 = 5.5 5.5 - 1
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 327 5 1 4 4.1 CCCn1ccc2cc(NCc3cccnc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
46225582 204072 None 0 Human Functional pEC50 = 5.5 5.5 - 1
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 362 3 0 5 4.6 Cn1c(CN2CCC(c3nc4ccccc4s3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL605831 204072 None 0 Human Functional pEC50 = 5.5 5.5 - 1
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 362 3 0 5 4.6 Cn1c(CN2CCC(c3nc4ccccc4s3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
118714738 114625 None 0 Human Functional pEC50 = 4.5 4.5 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 273 4 0 4 2.8 CC(C)CCn1ccc(N2CCCCC2)c(C#N)c1=O 10.1021/jm500496m
CHEMBL3337504 114625 None 0 Human Functional pEC50 = 4.5 4.5 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 273 4 0 4 2.8 CC(C)CCn1ccc(N2CCCCC2)c(C#N)c1=O 10.1021/jm500496m
70683629 74608 None 0 Human Functional pEC50 = 5.5 5.5 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 296 5 0 4 3.4 COc1cccc(-c2ccn(CCC(C)C)c(=O)c2C#N)c1 10.1021/jm2016864
CHEMBL2029788 74608 None 0 Human Functional pEC50 = 5.5 5.5 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 296 5 0 4 3.4 COc1cccc(-c2ccn(CCC(C)C)c(=O)c2C#N)c1 10.1021/jm2016864
11951099 67500 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 479 8 1 5 7.1 CCCc1c(OCc2cccc(-c3ccc(-c4nn[nH]n4)cc3)c2)ccc2c1ccn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
CHEMBL189264 67500 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 479 8 1 5 7.1 CCCc1c(OCc2cccc(-c3ccc(-c4nn[nH]n4)cc3)c2)ccc2c1ccn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
59599568 146138 None 0 Human Functional pEC50 = 6.5 6.5 -1 2
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 445 9 2 8 4.5 CCCc1c(OCc2cccc(Oc3ccc(-c4nn[nH]n4)cn3)c2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2016.11.049
CHEMBL3918914 146138 None 0 Human Functional pEC50 = 6.5 6.5 -1 2
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 445 9 2 8 4.5 CCCc1c(OCc2cccc(Oc3ccc(-c4nn[nH]n4)cn3)c2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2016.11.049
44591772 191576 None 0 Human Functional pEC50 = 7.5 7.5 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 369 4 0 3 4.7 C[C@@H]1CN(Cc2ccc(-c3ccc(OC(F)(F)F)cc3F)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL519332 191576 None 0 Human Functional pEC50 = 7.5 7.5 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 369 4 0 3 4.7 C[C@@H]1CN(Cc2ccc(-c3ccc(OC(F)(F)F)cc3F)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
117972047 142258 None 0 Human Functional pEC50 = 7.5 7.5 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 327 6 0 4 4.0 Clc1c(OCCc2ccccc2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
CHEMBL3883827 142258 None 0 Human Functional pEC50 = 7.5 7.5 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 327 6 0 4 4.0 Clc1c(OCCc2ccccc2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
46215876 80838 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 374 2 1 3 5.1 N#Cc1c(-c2cc(Cl)c3[nH]ccc3c2)ccn2c(CC(F)(F)F)cnc12 10.1021/jm201561r
CHEMBL2152116 80838 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 374 2 1 3 5.1 N#Cc1c(-c2cc(Cl)c3[nH]ccc3c2)ccn2c(CC(F)(F)F)cnc12 10.1021/jm201561r
162670769 183074 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 341 5 0 4 4.2 Fc1ccc(SCCCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
CHEMBL4793069 183074 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 341 5 0 4 4.2 Fc1ccc(SCCCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
156016100 177792 None 0 Human Functional pEC50 = 6.5 6.5 -1 2
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 1162 42 0 18 8.6 COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4641860 177792 None 0 Human Functional pEC50 = 6.5 6.5 -1 2
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 1162 42 0 18 8.6 COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
156017237 177866 None 0 Human Functional pEC50 = 6.5 6.5 1 2
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 853 21 0 11 8.5 COc1c(OCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4642761 177866 None 0 Human Functional pEC50 = 6.5 6.5 1 2
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 853 21 0 11 8.5 COc1c(OCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
71136746 148688 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 421 3 0 7 3.1 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3ccon3)nc21 nan
CHEMBL3939174 148688 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 421 3 0 7 3.1 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3ccon3)nc21 nan
156015654 177626 None 0 Human Functional pEC50 = 6.5 6.5 -1 2
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 897 24 0 12 8.5 COc1c(OCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4639821 177626 None 0 Human Functional pEC50 = 6.5 6.5 -1 2
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 897 24 0 12 8.5 COc1c(OCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
156016100 177792 None 0 Human Functional pEC50 = 6.5 6.5 -1 2
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 1162 42 0 18 8.6 COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4641860 177792 None 0 Human Functional pEC50 = 6.5 6.5 -1 2
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 1162 42 0 18 8.6 COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
11631795 64820 None 0 Human Functional pEC50 = 5.5 5.5 - 1
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 357 10 1 5 4.6 Cc1c(OCCCCOc2ccccn2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
CHEMBL181953 64820 None 0 Human Functional pEC50 = 5.5 5.5 - 1
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 357 10 1 5 4.6 Cc1c(OCCCCOc2ccccn2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
155531978 171835 None 0 Human Functional pEC50 = 7.5 7.5 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 363 3 0 5 4.2 N#Cc1cccc2c1nnn2Cc1ccc(-c2ccc(Cl)cc2F)nc1 10.1021/acs.jmedchem.8b00161
CHEMBL4467158 171835 None 0 Human Functional pEC50 = 7.5 7.5 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 363 3 0 5 4.2 N#Cc1cccc2c1nnn2Cc1ccc(-c2ccc(Cl)cc2F)nc1 10.1021/acs.jmedchem.8b00161
51357934 61995 None 0 Rat Functional pEC50 = 7.5 7.5 - 1
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 388 3 0 4 4.6 C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(C(F)(F)F)cc1 10.1021/jm101414h
CHEMBL1774227 61995 None 0 Rat Functional pEC50 = 7.5 7.5 - 1
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 388 3 0 4 4.6 C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(C(F)(F)F)cc1 10.1021/jm101414h
66784529 157185 None 0 Human Functional pEC50 = 7.5 7.5 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 430 5 2 5 5.4 O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4074421 157185 None 0 Human Functional pEC50 = 7.5 7.5 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 430 5 2 5 5.4 O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
71451227 80837 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 438 3 1 5 5.4 N#Cc1c(-c2ccc3c(ccn3[C@H]3CC[C@H](O)CC3)c2)ccn2c(CC(F)(F)F)cnc12 10.1021/jm201561r
CHEMBL2152115 80837 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 438 3 1 5 5.4 N#Cc1c(-c2ccc3c(ccn3[C@H]3CC[C@H](O)CC3)c2)ccn2c(CC(F)(F)F)cnc12 10.1021/jm201561r
25073303 167129 None 0 Human Functional pEC50 = 6.5 6.5 -11 2
Positive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis
ChEMBL 348 4 0 5 3.4 Cc1cccc(-c2ccc(OC[C@@H]3Cn4ccc(=O)nc4O3)cc2)c1C 10.1016/j.bmcl.2018.08.022
CHEMBL4288731 167129 None 0 Human Functional pEC50 = 6.5 6.5 -11 2
Positive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant human Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis
ChEMBL 348 4 0 5 3.4 Cc1cccc(-c2ccc(OC[C@@H]3Cn4ccc(=O)nc4O3)cc2)c1C 10.1016/j.bmcl.2018.08.022
156015654 177626 None 0 Human Functional pEC50 = 6.5 6.5 -1 2
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 897 24 0 12 8.5 COc1c(OCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4639821 177626 None 0 Human Functional pEC50 = 6.5 6.5 -1 2
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 897 24 0 12 8.5 COc1c(OCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
44155754 8514 None 0 Human Functional pEC50 = 5.5 5.5 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 262 6 1 3 3.6 CCCCCCC1CN(c2cccc(N)c2)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1094146 8514 None 0 Human Functional pEC50 = 5.5 5.5 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 262 6 1 3 3.6 CCCCCCC1CN(c2cccc(N)c2)C(=O)O1 10.1016/j.bmcl.2010.03.089
44300258 13656 None 0 Rat Functional pEC50 = 4.5 4.5 - 1
Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2
ChEMBL 308 5 4 5 -0.2 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2C(=O)O)C1 10.1016/s0960-894x(01)00329-8
CHEMBL1194540 13656 None 0 Rat Functional pEC50 = 4.5 4.5 - 1
Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2
ChEMBL 308 5 4 5 -0.2 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2C(=O)O)C1 10.1016/s0960-894x(01)00329-8
CHEMBL552836 13656 None 0 Rat Functional pEC50 = 4.5 4.5 - 1
Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2
ChEMBL 308 5 4 5 -0.2 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2C(=O)O)C1 10.1016/s0960-894x(01)00329-8
51357396 61975 None 0 Rat Functional pEC50 = 5.5 5.5 - 1
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 323 3 0 3 4.1 Cn1c(CN2CCC(c3cccc(F)c3)CC2)nc2ccccc21 10.1021/jm101414h
CHEMBL1774102 61975 None 0 Rat Functional pEC50 = 5.5 5.5 - 1
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 323 3 0 3 4.1 Cn1c(CN2CCC(c3cccc(F)c3)CC2)nc2ccccc21 10.1021/jm101414h
118714737 114624 None 0 Human Functional pEC50 = 5.5 5.5 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 349 5 0 4 4.2 CC(C)CCn1ccc(N2CCCC(c3ccccc3)C2)c(C#N)c1=O 10.1021/jm500496m
CHEMBL3337503 114624 None 0 Human Functional pEC50 = 5.5 5.5 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 349 5 0 4 4.2 CC(C)CCn1ccc(N2CCCC(c3ccccc3)C2)c(C#N)c1=O 10.1021/jm500496m
71117091 149437 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 412 4 1 6 3.0 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CCC(NC(=O)C4CCCO4)CC3)nc21 nan
CHEMBL3945222 149437 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 412 4 1 6 3.0 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CCC(NC(=O)C4CCCO4)CC3)nc21 nan
127030385 139250 None 0 Rat Functional pEC50 = 4.5 4.5 - 1
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assay
ChEMBL 217 5 4 4 -1.0 N[C@@H](C[C@]1(C(=O)O)C[C@@H]1C(=O)O)C(=O)O 10.1021/acs.jmedchem.5b01333
CHEMBL3787264 139250 None 0 Rat Functional pEC50 = 4.5 4.5 - 1
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assay
ChEMBL 217 5 4 4 -1.0 N[C@@H](C[C@]1(C(=O)O)C[C@@H]1C(=O)O)C(=O)O 10.1021/acs.jmedchem.5b01333
137635882 155984 None 0 Human Functional pEC50 = 5.5 5.5 1 2
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 310 4 4 4 0.2 N[C@@]1(C(=O)O)C[C@H](NC(=O)C2CCCCC2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4060567 155984 None 0 Human Functional pEC50 = 5.5 5.5 1 2
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 310 4 4 4 0.2 N[C@@]1(C(=O)O)C[C@H](NC(=O)C2CCCCC2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
9815617 114563 None 3 Rat Functional pEC50 = 7.5 7.5 -1 2
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 203 2 3 3 -0.4 N[C@@]1(C(=O)O)CC[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm000346k
CHEMBL333519 114563 None 3 Rat Functional pEC50 = 7.5 7.5 -1 2
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 203 2 3 3 -0.4 N[C@@]1(C(=O)O)CC[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm000346k
1393 1539 None 42 Human Functional pEC50 = 7.5 7.5 2 6
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/acs.jmedchem.5b01124
1396 1539 None 42 Human Functional pEC50 = 7.5 7.5 2 6
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/acs.jmedchem.5b01124
213056 1539 None 42 Human Functional pEC50 = 7.5 7.5 2 6
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/acs.jmedchem.5b01124
CHEMBL8759 1539 None 42 Human Functional pEC50 = 7.5 7.5 2 6
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/acs.jmedchem.5b01124
11187949 65624 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 373 10 1 5 5.3 Cc1c(OCCCCSc2ccncc2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
CHEMBL183319 65624 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 373 10 1 5 5.3 Cc1c(OCCCCSc2ccncc2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
162649047 179897 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 341 5 0 3 4.2 Fc1ccc(CCCCN2CCn3c(nc4ccccc43)C2)c(F)c1 10.1016/j.ejmech.2019.111881
CHEMBL4744761 179897 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 341 5 0 3 4.2 Fc1ccc(CCCCN2CCn3c(nc4ccccc43)C2)c(F)c1 10.1016/j.ejmech.2019.111881
44591796 184749 None 0 Human Functional pEC50 = 5.5 5.5 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 304 3 0 3 3.4 C[C@@H]1CN(Cc2ccc(-c3ccc(F)c(F)c3)nc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL484957 184749 None 0 Human Functional pEC50 = 5.5 5.5 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 304 3 0 3 3.4 C[C@@H]1CN(Cc2ccc(-c3ccc(F)c(F)c3)nc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
24905705 184128 None 0 Rat Functional pEC50 = 4.5 4.5 - 1
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assay
ChEMBL 219 7 4 4 -0.6 N[C@@H](C[C@@H](CCC(=O)O)C(=O)O)C(=O)O 10.1021/acs.jmedchem.5b01333
CHEMBL482081 184128 None 0 Rat Functional pEC50 = 4.5 4.5 - 1
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as IP1 accumulation by IP-One functional assay
ChEMBL 219 7 4 4 -0.6 N[C@@H](C[C@@H](CCC(=O)O)C(=O)O)C(=O)O 10.1021/acs.jmedchem.5b01333
46887319 8995 None 0 Human Functional pEC50 = 5.5 5.5 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 283 4 0 3 3.4 Cc1cccc(OCC2CN(c3ccccc3)C(=O)O2)c1 10.1016/j.bmcl.2010.03.089
CHEMBL1098388 8995 None 0 Human Functional pEC50 = 5.5 5.5 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 283 4 0 3 3.4 Cc1cccc(OCC2CN(c3ccccc3)C(=O)O2)c1 10.1016/j.bmcl.2010.03.089
25003298 74630 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 359 6 0 5 4.7 CCCCn1ccc(-c2ccc(Oc3cccnc3C)cc2)c(C#N)c1=O 10.1021/jm2016864
CHEMBL2029809 74630 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 359 6 0 5 4.7 CCCCn1ccc(-c2ccc(Oc3cccnc3C)cc2)c(C#N)c1=O 10.1021/jm2016864
10047169 3224 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 410 11 2 7 4.0 CCCc1c(OCCCCOc2ccc(cc2)c2n[nH]nn2)ccc(c1O)C(=O)C 10.1016/j.bmcl.2004.09.028
1403 3224 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 410 11 2 7 4.0 CCCc1c(OCCCCOc2ccc(cc2)c2n[nH]nn2)ccc(c1O)C(=O)C 10.1016/j.bmcl.2004.09.028
CHEMBL182371 3224 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 410 11 2 7 4.0 CCCc1c(OCCCCOc2ccc(cc2)c2n[nH]nn2)ccc(c1O)C(=O)C 10.1016/j.bmcl.2004.09.028
10047169 3224 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 410 11 2 7 4.0 CCCc1c(OCCCCOc2ccc(cc2)c2n[nH]nn2)ccc(c1O)C(=O)C 10.1016/j.bmcl.2005.06.017
1403 3224 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 410 11 2 7 4.0 CCCc1c(OCCCCOc2ccc(cc2)c2n[nH]nn2)ccc(c1O)C(=O)C 10.1016/j.bmcl.2005.06.017
CHEMBL182371 3224 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 410 11 2 7 4.0 CCCc1c(OCCCCOc2ccc(cc2)c2n[nH]nn2)ccc(c1O)C(=O)C 10.1016/j.bmcl.2005.06.017
44591713 184406 None 0 Human Functional pEC50 = 7.5 7.5 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 285 3 0 2 3.8 C[C@@H]1CN(Cc2ccc(-c3ccccc3F)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL484126 184406 None 0 Human Functional pEC50 = 7.5 7.5 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 285 3 0 2 3.8 C[C@@H]1CN(Cc2ccc(-c3ccccc3F)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
118714753 114639 None 0 Human Functional pEC50 = 7.5 7.5 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 363 5 0 5 3.5 COc1ccccc1C1CCN(c2ccn(CC3CC3)c(=O)c2C#N)CC1 10.1021/jm500496m
CHEMBL3337519 114639 None 0 Human Functional pEC50 = 7.5 7.5 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 363 5 0 5 3.5 COc1ccccc1C1CCN(c2ccn(CC3CC3)c(=O)c2C#N)CC1 10.1021/jm500496m
44178197 62001 None 0 Rat Functional pEC50 = 7.5 7.5 -1 2
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 422 4 0 5 4.6 C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(OC(F)(F)F)cc1F 10.1021/jm101414h
CHEMBL1774235 62001 None 0 Rat Functional pEC50 = 7.5 7.5 -1 2
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 422 4 0 5 4.6 C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(OC(F)(F)F)cc1F 10.1021/jm101414h
51354020 62002 None 0 Human Functional pEC50 = 7.5 7.5 23 2
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL 422 4 0 5 4.6 C[C@@H]1CN(Cc2nc3ncccc3n2C)CC[C@@H]1c1ccc(OC(F)(F)F)cc1F 10.1021/acs.jmedchem.1c00563
CHEMBL1774236 62002 None 0 Human Functional pEC50 = 7.5 7.5 23 2
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL 422 4 0 5 4.6 C[C@@H]1CN(Cc2nc3ncccc3n2C)CC[C@@H]1c1ccc(OC(F)(F)F)cc1F 10.1021/acs.jmedchem.1c00563
1393 1539 None 42 Rat Functional pEC50 = 7.5 7.5 -2 6
Tested for the agonistic activity against Metabotropic glutamate receptor 2Tested for the agonistic activity against Metabotropic glutamate receptor 2
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1016/S0960-894X(97)00068-1
1396 1539 None 42 Rat Functional pEC50 = 7.5 7.5 -2 6
Tested for the agonistic activity against Metabotropic glutamate receptor 2Tested for the agonistic activity against Metabotropic glutamate receptor 2
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1016/S0960-894X(97)00068-1
213056 1539 None 42 Rat Functional pEC50 = 7.5 7.5 -2 6
Tested for the agonistic activity against Metabotropic glutamate receptor 2Tested for the agonistic activity against Metabotropic glutamate receptor 2
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1016/S0960-894X(97)00068-1
CHEMBL8759 1539 None 42 Rat Functional pEC50 = 7.5 7.5 -2 6
Tested for the agonistic activity against Metabotropic glutamate receptor 2Tested for the agonistic activity against Metabotropic glutamate receptor 2
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1016/S0960-894X(97)00068-1
71457756 83936 None 0 Human Functional pEC50 = 7.5 7.5 66 2
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 396 5 0 5 4.7 COc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL2206440 83936 None 0 Human Functional pEC50 = 7.5 7.5 66 2
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 396 5 0 5 4.7 COc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/acs.jmedchem.0c01058
46887371 8805 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 325 4 0 3 4.4 CC(C)(C)c1cccc(OCC2CN(c3ccccc3)C(=O)O2)c1 10.1016/j.bmcl.2010.03.089
CHEMBL1096712 8805 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 325 4 0 3 4.4 CC(C)(C)c1cccc(OCC2CN(c3ccccc3)C(=O)O2)c1 10.1016/j.bmcl.2010.03.089
162661233 181618 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 359 5 0 4 4.3 Fc1ccc(SCCCN2CCn3c(nc4ccccc43)C2)c(F)c1 10.1016/j.ejmech.2019.111881
CHEMBL4765006 181618 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 359 5 0 4 4.3 Fc1ccc(SCCCN2CCn3c(nc4ccccc43)C2)c(F)c1 10.1016/j.ejmech.2019.111881
CHEMBL5076606 216940 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL None None None O=C1c2nc3cccc(Br)c3n2CCN1CC1CC1 10.1021/acs.jmedchem.1c00563
136950 8696 None 24 Human Functional pEC50 = 5.5 5.5 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 269 4 0 3 3.1 O=C1OC(COc2ccccc2)CN1c1ccccc1 10.1016/j.bmcl.2010.03.089
CHEMBL1095705 8696 None 24 Human Functional pEC50 = 5.5 5.5 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 269 4 0 3 3.1 O=C1OC(COc2ccccc2)CN1c1ccccc1 10.1016/j.bmcl.2010.03.089
59066632 209028 None 52 Human Functional pEC50 = 4.5 4.5 1 2
Agonistic activity at mGlu2 receptor expressed in CHO cellsAgonistic activity at mGlu2 receptor expressed in CHO cells
ChEMBL 161 5 3 3 -0.3 N[C@@H](CCCC(=O)O)C(=O)O 10.1021/jm9602569
92136 209028 None 52 Human Functional pEC50 = 4.5 4.5 1 2
Agonistic activity at mGlu2 receptor expressed in CHO cellsAgonistic activity at mGlu2 receptor expressed in CHO cells
ChEMBL 161 5 3 3 -0.3 N[C@@H](CCCC(=O)O)C(=O)O 10.1021/jm9602569
CHEMBL88804 209028 None 52 Human Functional pEC50 = 4.5 4.5 1 2
Agonistic activity at mGlu2 receptor expressed in CHO cellsAgonistic activity at mGlu2 receptor expressed in CHO cells
ChEMBL 161 5 3 3 -0.3 N[C@@H](CCCC(=O)O)C(=O)O 10.1021/jm9602569
44300135 13289 None 0 Rat Functional pEC50 = 4.5 4.5 - 1
Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2
ChEMBL 279 4 4 5 -0.3 Nc1ccccc1CN1C[C@@](N)(C(=O)O)C[C@@H]1C(=O)O 10.1016/s0960-894x(01)00329-8
CHEMBL1191723 13289 None 0 Rat Functional pEC50 = 4.5 4.5 - 1
Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2
ChEMBL 279 4 4 5 -0.3 Nc1ccccc1CN1C[C@@](N)(C(=O)O)C[C@@H]1C(=O)O 10.1016/s0960-894x(01)00329-8
CHEMBL542862 13289 None 0 Rat Functional pEC50 = 4.5 4.5 - 1
Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2
ChEMBL 279 4 4 5 -0.3 Nc1ccccc1CN1C[C@@](N)(C(=O)O)C[C@@H]1C(=O)O 10.1016/s0960-894x(01)00329-8
11951271 67532 None 0 Human Functional pEC50 = 5.5 5.5 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 447 10 1 6 5.7 CCCc1c(OCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
CHEMBL189516 67532 None 0 Human Functional pEC50 = 5.5 5.5 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 447 10 1 6 5.7 CCCc1c(OCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
118714746 114632 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 389 5 0 4 4.4 N#Cc1c(N2CCC(c3ccccc3)CC2)ccn(CCCC(F)(F)F)c1=O 10.1021/jm500496m
CHEMBL3337512 114632 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 389 5 0 4 4.4 N#Cc1c(N2CCC(c3ccccc3)CC2)ccn(CCCC(F)(F)F)c1=O 10.1021/jm500496m
71117198 150386 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 358 3 1 4 1.7 CN1c2nc(C3CCCNC3)ccc2N(CC2CC2(F)F)S1(=O)=O nan
CHEMBL3952803 150386 None 0 Human Functional pEC50 = 6.5 6.5 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 358 3 1 4 1.7 CN1c2nc(C3CCCNC3)ccc2N(CC2CC2(F)F)S1(=O)=O nan
11950746 67114 None 0 Human Functional pEC50 = 5.5 5.5 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 419 9 1 6 5.1 CC(C)(C)Cn1ccc2cc(OCCCCOc3ccc(-c4nn[nH]n4)cc3)ccc21 10.1016/j.bmcl.2005.06.017
CHEMBL187342 67114 None 0 Human Functional pEC50 = 5.5 5.5 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 419 9 1 6 5.1 CC(C)(C)Cn1ccc2cc(OCCCCOc3ccc(-c4nn[nH]n4)cc3)ccc21 10.1016/j.bmcl.2005.06.017
627502 8584 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 303 4 0 3 3.7 O=C1OC(COc2ccc(Cl)cc2)CN1c1ccccc1 10.1016/j.bmcl.2010.03.089
CHEMBL1094733 8584 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 303 4 0 3 3.7 O=C1OC(COc2ccc(Cl)cc2)CN1c1ccccc1 10.1016/j.bmcl.2010.03.089
46887370 8804 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 311 5 0 3 4.2 CC(C)c1ccc(OCC2CN(c3ccccc3)C(=O)O2)cc1 10.1016/j.bmcl.2010.03.089
CHEMBL1096711 8804 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 311 5 0 3 4.2 CC(C)c1ccc(OCC2CN(c3ccccc3)C(=O)O2)cc1 10.1016/j.bmcl.2010.03.089
46887322 8998 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 297 5 0 3 3.7 CCc1cccc(OCC2CN(c3ccccc3)C(=O)O2)c1 10.1016/j.bmcl.2010.03.089
CHEMBL1098391 8998 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 297 5 0 3 3.7 CCc1cccc(OCC2CN(c3ccccc3)C(=O)O2)c1 10.1016/j.bmcl.2010.03.089
59391336 114619 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 294 6 0 3 3.6 CC(C)CCn1ccc(CCc2ccccc2)c(C#N)c1=O 10.1021/jm500496m
CHEMBL3337498 114619 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 294 6 0 3 3.6 CC(C)CCn1ccc(CCc2ccccc2)c(C#N)c1=O 10.1021/jm500496m
10176836 35883 None 0 Rat Functional pEC50 = 4.4 4.4 - 1
Antagonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated in presence of 30 uM glutamic acidAntagonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated in presence of 30 uM glutamic acid
ChEMBL 221 2 3 3 -0.2 N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2CC1(F)F 10.1021/jm000346k
CHEMBL144201 35883 None 0 Rat Functional pEC50 = 4.4 4.4 - 1
Antagonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated in presence of 30 uM glutamic acidAntagonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated in presence of 30 uM glutamic acid
ChEMBL 221 2 3 3 -0.2 N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2CC1(F)F 10.1021/jm000346k
70685762 74610 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 330 5 0 4 4.1 COc1ccc(-c2ccn(CCC(C)C)c(=O)c2C#N)cc1Cl 10.1021/jm2016864
CHEMBL2029791 74610 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 330 5 0 4 4.1 COc1ccc(-c2ccn(CCC(C)C)c(=O)c2C#N)cc1Cl 10.1021/jm2016864
69093439 83939 None 0 Human Functional pEC50 = 7.4 7.4 - 1
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 414 5 0 5 4.9 COc1c(F)cccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm300912k
CHEMBL2206443 83939 None 0 Human Functional pEC50 = 7.4 7.4 - 1
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 414 5 0 5 4.9 COc1c(F)cccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm300912k
71457756 83936 None 0 Human Functional pEC50 = 7.4 7.4 66 2
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 396 5 0 5 4.7 COc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL2206440 83936 None 0 Human Functional pEC50 = 7.4 7.4 66 2
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 396 5 0 5 4.7 COc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/acs.jmedchem.0c01058
155560423 175179 None 0 Human Functional pEC50 = 7.4 7.4 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 387 3 0 3 5.8 FC(F)(F)c1ccc(-c2ccc(Cn3nnc4ccccc43)cc2)c(Cl)c1 10.1021/acs.jmedchem.8b00161
CHEMBL4568356 175179 None 0 Human Functional pEC50 = 7.4 7.4 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 387 3 0 3 5.8 FC(F)(F)c1ccc(-c2ccc(Cn3nnc4ccccc43)cc2)c(Cl)c1 10.1021/acs.jmedchem.8b00161
44300820 13383 None 0 Rat Functional pEC50 = 4.4 4.4 -1 2
Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2
ChEMBL 265 4 3 5 -0.5 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccn2)C1 10.1016/s0960-894x(01)00329-8
CHEMBL1192558 13383 None 0 Rat Functional pEC50 = 4.4 4.4 -1 2
Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2
ChEMBL 265 4 3 5 -0.5 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccn2)C1 10.1016/s0960-894x(01)00329-8
CHEMBL543811 13383 None 0 Rat Functional pEC50 = 4.4 4.4 -1 2
Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2
ChEMBL 265 4 3 5 -0.5 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccn2)C1 10.1016/s0960-894x(01)00329-8
68108457 148644 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay
ChEMBL 450 5 0 4 5.4 Fc1ccc(C2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.2c00593
CHEMBL3938796 148644 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay
ChEMBL 450 5 0 4 5.4 Fc1ccc(C2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.2c00593
25002941 74643 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 391 6 0 5 5.1 CCCCn1ccc(-c2ccc(Oc3cc(C)nc(C)c3)c(F)c2)c(C#N)c1=O 10.1021/jm2016864
CHEMBL2029823 74643 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 391 6 0 5 5.1 CCCCn1ccc(-c2ccc(Oc3cc(C)nc(C)c3)c(F)c2)c(C#N)c1=O 10.1021/jm2016864
66786069 156552 None 0 Human Functional pEC50 = 7.4 7.4 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 451 5 0 5 5.6 FC(F)(F)c1c(-c2ccc(OC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
CHEMBL4067290 156552 None 0 Human Functional pEC50 = 7.4 7.4 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 451 5 0 5 5.6 FC(F)(F)c1c(-c2ccc(OC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
44591794 184747 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 370 4 0 4 4.1 C[C@@H]1CN(Cc2ccc(-c3ccc(OC(F)(F)F)cc3F)nc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL484956 184747 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 370 4 0 4 4.1 C[C@@H]1CN(Cc2ccc(-c3ccc(OC(F)(F)F)cc3F)nc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
44155534 8686 None 0 Human Functional pEC50 = 5.4 5.4 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 261 6 0 2 4.3 CCCCCCC1CN(c2ccc(C)cc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1095638 8686 None 0 Human Functional pEC50 = 5.4 5.4 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 261 6 0 2 4.3 CCCCCCC1CN(c2ccc(C)cc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
44591647 184913 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 359 5 0 4 4.1 O=C1OC2(CCOCC2)CN1Cc1ccc(OCC2CCCCC2)cc1 10.1016/j.bmcl.2009.03.032
CHEMBL485176 184913 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 359 5 0 4 4.1 O=C1OC2(CCOCC2)CN1Cc1ccc(OCC2CCCCC2)cc1 10.1016/j.bmcl.2009.03.032
11531272 65223 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 392 10 1 4 5.4 Cc1c(OCCCCOc2cccc(F)c2F)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
CHEMBL182511 65223 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 392 10 1 4 5.4 Cc1c(OCCCCOc2cccc(F)c2F)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
11710164 66357 None 0 Human Functional pEC50 = 5.4 5.4 - 1
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 357 10 1 5 4.6 Cc1c(OCCCCOc2ccncc2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
CHEMBL185046 66357 None 0 Human Functional pEC50 = 5.4 5.4 - 1
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 357 10 1 5 4.6 Cc1c(OCCCCOc2ccncc2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
57459481 82670 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 340 3 0 4 4.3 CCc1nnc2c(Cl)c(N3CCC(c4ccccc4)CC3)ccn12 10.1021/jm3010724
CHEMBL2179315 82670 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 340 3 0 4 4.3 CCc1nnc2c(Cl)c(N3CCC(c4ccccc4)CC3)ccn12 10.1021/jm3010724
23770349 8912 None 0 Human Functional pEC50 = 5.4 5.4 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 303 4 0 3 3.7 O=C1OC(COc2ccccc2Cl)CN1c1ccccc1 10.1016/j.bmcl.2010.03.089
CHEMBL1097656 8912 None 0 Human Functional pEC50 = 5.4 5.4 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 303 4 0 3 3.7 O=C1OC(COc2ccccc2Cl)CN1c1ccccc1 10.1016/j.bmcl.2010.03.089
57459635 82676 None 0 Human Functional pEC50 = 7.4 7.4 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 418 4 0 4 5.2 FC(F)(F)c1c(N2CCC(F)(c3ccccc3)CC2)ccn2c(CC3CC3)nnc12 10.1021/jm3010724
CHEMBL2179322 82676 None 0 Human Functional pEC50 = 7.4 7.4 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 418 4 0 4 5.2 FC(F)(F)c1c(N2CCC(F)(c3ccccc3)CC2)ccn2c(CC3CC3)nnc12 10.1021/jm3010724
59599552 148391 None 0 Human Functional pEC50 = 7.4 7.4 12 2
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 437 7 2 8 4.2 CC(=O)c1ccc(OCc2cccc(Oc3ccc(-c4nn[nH]n4)cn3)c2)c(Cl)c1O 10.1016/j.bmcl.2016.11.049
CHEMBL3936830 148391 None 0 Human Functional pEC50 = 7.4 7.4 12 2
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 437 7 2 8 4.2 CC(=O)c1ccc(OCc2cccc(Oc3ccc(-c4nn[nH]n4)cn3)c2)c(Cl)c1O 10.1016/j.bmcl.2016.11.049
71135411 123464 None 0 Human Functional pEC50 = 7.4 7.4 5 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 298 4 4 6 -0.3 Cc1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
CHEMBL3616848 123464 None 0 Human Functional pEC50 = 7.4 7.4 5 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 298 4 4 6 -0.3 Cc1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
25002939 74642 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 377 6 0 5 4.8 CCCCn1ccc(-c2ccc(Oc3ccnc(C)c3)cc2F)c(C#N)c1=O 10.1021/jm2016864
CHEMBL2029822 74642 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 377 6 0 5 4.8 CCCCn1ccc(-c2ccc(Oc3ccnc(C)c3)cc2F)c(C#N)c1=O 10.1021/jm2016864
CHEMBL5083201 217340 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL None None None O=C1c2nc3cccc(Cl)c3n2CCN1CC1CC1 10.1021/acs.jmedchem.1c00563
71136199 142774 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 423 3 0 7 3.0 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3CC4CN(C(=O)c5ncco5)CC4C3)nc21 nan
CHEMBL3892060 142774 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 423 3 0 7 3.0 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3CC4CN(C(=O)c5ncco5)CC4C3)nc21 nan
11310142 2422 None 14 Human Functional pEC50 = 6.4 6.4 13 3
Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor
ChEMBL 199 2 3 3 -0.2 C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O 10.1021/jm040222y
11614 2422 None 14 Human Functional pEC50 = 6.4 6.4 13 3
Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor
ChEMBL 199 2 3 3 -0.2 C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O 10.1021/jm040222y
CHEMBL192051 2422 None 14 Human Functional pEC50 = 6.4 6.4 13 3
Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor
ChEMBL 199 2 3 3 -0.2 C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O 10.1021/jm040222y
25002587 74628 None 4 Human Functional pEC50 = 6.4 6.4 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 359 6 0 5 4.7 CCCCn1ccc(-c2ccc(Oc3ccnc(C)c3)cc2)c(C#N)c1=O 10.1021/jm2016864
CHEMBL2029807 74628 None 4 Human Functional pEC50 = 6.4 6.4 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 359 6 0 5 4.7 CCCCn1ccc(-c2ccc(Oc3ccnc(C)c3)cc2)c(C#N)c1=O 10.1021/jm2016864
53320818 57753 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 346 4 0 4 4.3 CCCn1ccc2cc(-c3cnc(OC)c(F)c3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669391 57753 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 346 4 0 4 4.3 CCCn1ccc2cc(-c3cnc(OC)c(F)c3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
53325452 57761 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 438 6 0 4 6.4 CCCn1ccc2cc(-c3ccc(OCc4ccc(Cl)nc4)cc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669399 57761 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 438 6 0 4 6.4 CCCn1ccc2cc(-c3ccc(OCc4ccc(Cl)nc4)cc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
90668096 109598 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 350 7 0 4 4.1 CCCn1ccc2c(N(C)CCc3ccc(OC)cc3)cccc2c1=O 10.1039/C0MD00200C
CHEMBL3221836 109598 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 350 7 0 4 4.1 CCCn1ccc2c(N(C)CCc3ccc(OC)cc3)cccc2c1=O 10.1039/C0MD00200C
53324803 57743 None 0 Human Functional pEC50 = 5.4 5.4 - 1
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 299 3 0 4 3.5 CCCn1ccc2cc(-c3cncnc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669382 57743 None 0 Human Functional pEC50 = 5.4 5.4 - 1
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 299 3 0 4 3.5 CCCn1ccc2cc(-c3cncnc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
24815439 204392 None 1 Human Functional pEC50 = 5.4 5.4 -18 2
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 323 3 0 3 4.1 Cn1c(CN2CCC(c3ccccc3F)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL607689 204392 None 1 Human Functional pEC50 = 5.4 5.4 -18 2
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 323 3 0 3 4.1 Cn1c(CN2CCC(c3ccccc3F)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
46225581 204444 None 0 Human Functional pEC50 = 5.4 5.4 - 1
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 339 3 0 3 4.6 Cn1c(CN2CCC(c3cccc(Cl)c3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL608103 204444 None 0 Human Functional pEC50 = 5.4 5.4 - 1
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 339 3 0 3 4.6 Cn1c(CN2CCC(c3cccc(Cl)c3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
44361401 31349 None 0 Rat Functional pEC50 = 8.4 8.4 1 5
Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells
ChEMBL 175 3 4 4 -1.9 N[C@H](C(=O)O)[C@H]1[C@@H](O)[C@@H]1C(=O)O 10.1021/jm030967o
CHEMBL140197 31349 None 0 Rat Functional pEC50 = 8.4 8.4 1 5
Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells
ChEMBL 175 3 4 4 -1.9 N[C@H](C(=O)O)[C@H]1[C@@H](O)[C@@H]1C(=O)O 10.1021/jm030967o
117972155 142342 None 0 Human Functional pEC50 = 8.4 8.4 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 421 6 0 4 5.5 FC(F)(F)c1c(OC[C@@H]2C[C@H]2c2ccc(Cl)cc2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
CHEMBL3884833 142342 None 0 Human Functional pEC50 = 8.4 8.4 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 421 6 0 4 5.5 FC(F)(F)c1c(OC[C@@H]2C[C@H]2c2ccc(Cl)cc2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
71457757 83945 None 0 Human Functional pEC50 = 8.4 8.4 - 1
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 466 5 0 5 5.4 COc1c(F)ccc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1 10.1021/jm300912k
CHEMBL2206449 83945 None 0 Human Functional pEC50 = 8.4 8.4 - 1
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 466 5 0 5 5.4 COc1c(F)ccc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1 10.1021/jm300912k
71137012 123467 None 0 Human Functional pEC50 = 8.4 8.4 11 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 299 4 5 7 -1.0 Nc1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
CHEMBL3616851 123467 None 0 Human Functional pEC50 = 8.4 8.4 11 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 299 4 5 7 -1.0 Nc1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
162654912 180758 None 0 Human Functional pEC50 = 7.4 7.4 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 387 6 0 4 4.1 O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(F)c(Cl)c1 10.1016/j.ejmech.2019.111881
CHEMBL4755035 180758 None 0 Human Functional pEC50 = 7.4 7.4 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 387 6 0 4 4.1 O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(F)c(Cl)c1 10.1016/j.ejmech.2019.111881
162674461 183437 None 0 Human Functional pEC50 = 7.4 7.4 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 403 6 0 4 4.4 O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(C(F)(F)F)cc1 10.1016/j.ejmech.2019.111881
CHEMBL4797417 183437 None 0 Human Functional pEC50 = 7.4 7.4 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 403 6 0 4 4.4 O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(C(F)(F)F)cc1 10.1016/j.ejmech.2019.111881
CHEMBL5083122 217331 None 0 Human Functional pEC50 = 7.4 7.4 - 1
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL None None None O=C1c2nc3cccc(C(F)(F)F)c3n2CCN1Cc1ccc(Cl)cc1 10.1021/acs.jmedchem.1c00563
66785551 157245 None 0 Human Functional pEC50 = 7.4 7.4 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 422 5 0 5 5.9 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4075258 157245 None 0 Human Functional pEC50 = 7.4 7.4 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 422 5 0 5 5.9 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
66784675 157266 None 0 Human Functional pEC50 = 7.4 7.4 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 472 7 0 6 5.5 COc1ccc(COc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cn1 10.1021/acs.jmedchem.7b00669
CHEMBL4075537 157266 None 0 Human Functional pEC50 = 7.4 7.4 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 472 7 0 6 5.5 COc1ccc(COc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cn1 10.1021/acs.jmedchem.7b00669
162642952 181843 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 373 5 0 3 5.2 Clc1ccc(CCCCN2CCn3c(nc4ccccc43)C2)c(Cl)c1 10.1016/j.ejmech.2019.111881
CHEMBL4777206 181843 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 373 5 0 3 5.2 Clc1ccc(CCCCN2CCn3c(nc4ccccc43)C2)c(Cl)c1 10.1016/j.ejmech.2019.111881
155554782 174702 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 203 3 0 4 1.9 COc1cccc2c1nnn2CC1CC1 10.1021/acs.jmedchem.8b00161
CHEMBL4557213 174702 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 203 3 0 4 1.9 COc1cccc2c1nnn2CC1CC1 10.1021/acs.jmedchem.8b00161
57459524 82678 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 358 3 0 4 4.2 FC(F)(F)c1c(N2Cc3ccccc3C2)ccn2c(CC3CC3)nnc12 10.1021/jm3010724
CHEMBL2179324 82678 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 358 3 0 4 4.2 FC(F)(F)c1c(N2Cc3ccccc3C2)ccn2c(CC3CC3)nnc12 10.1021/jm3010724
10474978 13464 None 0 Rat Functional pEC50 = 5.4 5.4 1 2
Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2
ChEMBL 309 5 3 6 0.0 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2[N+](=O)[O-])C1 10.1016/s0960-894x(01)00329-8
CHEMBL1193146 13464 None 0 Rat Functional pEC50 = 5.4 5.4 1 2
Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2
ChEMBL 309 5 3 6 0.0 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2[N+](=O)[O-])C1 10.1016/s0960-894x(01)00329-8
CHEMBL544508 13464 None 0 Rat Functional pEC50 = 5.4 5.4 1 2
Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2
ChEMBL 309 5 3 6 0.0 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2[N+](=O)[O-])C1 10.1016/s0960-894x(01)00329-8
59599576 142626 None 0 Human Functional pEC50 = 6.4 6.4 -5 2
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 421 9 2 6 5.0 CCCc1c(OCc2cccc(Oc3cc(C(=O)O)ccn3)c2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2016.11.049
CHEMBL3890848 142626 None 0 Human Functional pEC50 = 6.4 6.4 -5 2
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 421 9 2 6 5.0 CCCc1c(OCc2cccc(Oc3cc(C(=O)O)ccn3)c2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2016.11.049
44591745 192453 None 0 Human Functional pEC50 = 7.4 7.4 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 297 4 0 3 3.7 COc1ccccc1-c1ccc(CN2C[C@@H](C)OC2=O)cc1 10.1016/j.bmcl.2009.03.032
CHEMBL520677 192453 None 0 Human Functional pEC50 = 7.4 7.4 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 297 4 0 3 3.7 COc1ccccc1-c1ccc(CN2C[C@@H](C)OC2=O)cc1 10.1016/j.bmcl.2009.03.032
68109677 157285 None 0 Human Functional pEC50 = 7.4 7.4 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 458 4 2 5 5.5 O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4075762 157285 None 0 Human Functional pEC50 = 7.4 7.4 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 458 4 2 5 5.5 O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
66786493 157352 None 0 Human Functional pEC50 = 7.4 7.4 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 464 5 2 5 5.7 O[C@H]1CC[C@@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4076639 157352 None 0 Human Functional pEC50 = 7.4 7.4 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 464 5 2 5 5.7 O[C@H]1CC[C@@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
46887415 8544 None 0 Human Functional pEC50 = 5.4 5.4 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 299 5 0 4 3.1 COc1cccc(OCC2CN(c3ccccc3)C(=O)O2)c1 10.1016/j.bmcl.2010.03.089
CHEMBL1094415 8544 None 0 Human Functional pEC50 = 5.4 5.4 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 299 5 0 4 3.1 COc1cccc(OCC2CN(c3ccccc3)C(=O)O2)c1 10.1016/j.bmcl.2010.03.089
70685764 74616 None 0 Human Functional pEC50 = 7.4 7.4 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 358 6 0 4 5.2 CC(C)CCn1ccc(-c2ccc(Oc3ccccc3)cc2)c(C#N)c1=O 10.1021/jm2016864
CHEMBL2029797 74616 None 0 Human Functional pEC50 = 7.4 7.4 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 358 6 0 4 5.2 CC(C)CCn1ccc(-c2ccc(Oc3ccccc3)cc2)c(C#N)c1=O 10.1021/jm2016864
137659992 159329 None 0 Human Functional pEC50 = 7.4 7.4 -8 2
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 338 4 4 4 0.6 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2Cl)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4098939 159329 None 0 Human Functional pEC50 = 7.4 7.4 -8 2
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 338 4 4 4 0.6 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2Cl)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
162645511 179704 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 305 5 0 3 3.9 c1ccc(CCCCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
CHEMBL4742196 179704 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 305 5 0 3 3.9 c1ccc(CCCCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
44392708 66101 None 0 Human Functional pEC50 = 5.4 5.4 - 1
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 423 11 1 7 4.7 Cc1c(OCCCCOc2ccc(-n3cncn3)cc2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
CHEMBL183807 66101 None 0 Human Functional pEC50 = 5.4 5.4 - 1
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 423 11 1 7 4.7 Cc1c(OCCCCOc2ccc(-n3cncn3)cc2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
25008615 61980 None 0 Human Functional pEC50 = 7.4 7.4 1 2
Positive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 374 3 0 4 4.4 Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2ncccc21 10.1021/jm101414h
CHEMBL1774108 61980 None 0 Human Functional pEC50 = 7.4 7.4 1 2
Positive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 374 3 0 4 4.4 Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2ncccc21 10.1021/jm101414h
71116772 147757 None 0 Human Functional pEC50 = 7.4 7.4 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 456 4 1 8 3.7 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3CCC(C)(C)C(NC(=O)c4cnsn4)C3)nc21 nan
CHEMBL3931730 147757 None 0 Human Functional pEC50 = 7.4 7.4 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 456 4 1 8 3.7 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3CCC(C)(C)C(NC(=O)c4cnsn4)C3)nc21 nan
44591793 184458 None 0 Human Functional pEC50 = 5.4 5.4 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 269 3 0 4 2.5 C[C@@H]1CN(Cc2ccc(-c3cncnc3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL484403 184458 None 0 Human Functional pEC50 = 5.4 5.4 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 269 3 0 4 2.5 C[C@@H]1CN(Cc2ccc(-c3cncnc3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
71137008 123471 None 0 Human Functional pEC50 = 7.4 7.4 7 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 298 4 4 6 -0.3 Cc1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
CHEMBL3616855 123471 None 0 Human Functional pEC50 = 7.4 7.4 7 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 298 4 4 6 -0.3 Cc1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
156019582 178116 None 0 Human Functional pEC50 = 6.4 6.4 2 2
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 382 4 1 5 4.4 Oc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1 10.1021/acs.jmedchem.0c01058
CHEMBL4646555 178116 None 0 Human Functional pEC50 = 6.4 6.4 2 2
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 382 4 1 5 4.4 Oc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1 10.1021/acs.jmedchem.0c01058
3954 664 None 44 Rat Functional pEC50 = 6.4 6.4 -6 3
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293A cells by calcium mobilization assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293A cells by calcium mobilization assay
ChEMBL 454 6 1 3 6.8 Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1 10.1021/jm5000563
9868580 664 None 44 Rat Functional pEC50 = 6.4 6.4 -6 3
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293A cells by calcium mobilization assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293A cells by calcium mobilization assay
ChEMBL 454 6 1 3 6.8 Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1 10.1021/jm5000563
CHEMBL593013 664 None 44 Rat Functional pEC50 = 6.4 6.4 -6 3
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293A cells by calcium mobilization assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293A cells by calcium mobilization assay
ChEMBL 454 6 1 3 6.8 Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1 10.1021/jm5000563
44155643 8851 None 0 Human Functional pEC50 = 5.4 5.4 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 281 6 0 2 4.6 CCCCCCC1CN(c2ccc(Cl)cc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1097053 8851 None 0 Human Functional pEC50 = 5.4 5.4 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 281 6 0 2 4.6 CCCCCCC1CN(c2ccc(Cl)cc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
156019582 178116 None 0 Human Functional pEC50 = 6.4 6.4 2 2
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 382 4 1 5 4.4 Oc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1 10.1021/acs.jmedchem.0c01058
CHEMBL4646555 178116 None 0 Human Functional pEC50 = 6.4 6.4 2 2
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 382 4 1 5 4.4 Oc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1 10.1021/acs.jmedchem.0c01058
46227795 202419 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 357 2 0 3 5.3 CC(C)(C)c1ccc(-c2ccn3c(CC(F)(F)F)cnc3c2C#N)cc1 10.1016/j.bmcl.2009.11.008
CHEMBL595043 202419 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 357 2 0 3 5.3 CC(C)(C)c1ccc(-c2ccn3c(CC(F)(F)F)cnc3c2C#N)cc1 10.1016/j.bmcl.2009.11.008
46227792 202548 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 415 3 0 7 3.0 Cc1cc(C)nc(N2CCN(c3ccn4c(CC(F)(F)F)cnc4c3C#N)CC2)n1 10.1016/j.bmcl.2009.11.008
CHEMBL595967 202548 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 415 3 0 7 3.0 Cc1cc(C)nc(N2CCN(c3ccn4c(CC(F)(F)F)cnc4c3C#N)CC2)n1 10.1016/j.bmcl.2009.11.008
70689927 74626 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 373 6 0 5 4.9 Cc1cc(Oc2ccc(-c3ccn(CCC(C)C)c(=O)c3C#N)cc2)ccn1 10.1021/jm2016864
CHEMBL2029805 74626 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 373 6 0 5 4.9 Cc1cc(Oc2ccc(-c3ccn(CCC(C)C)c(=O)c3C#N)cc2)ccn1 10.1021/jm2016864
10822010 36396 None 0 Rat Functional pEC50 = 5.4 5.4 - 1
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 203 2 3 3 -0.5 N[C@@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2C[C@H]1F 10.1021/jm000346k
CHEMBL144678 36396 None 0 Rat Functional pEC50 = 5.4 5.4 - 1
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 203 2 3 3 -0.5 N[C@@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2C[C@H]1F 10.1021/jm000346k
1377 1340 None 23 Rat Functional pEC50 = 7.4 7.4 1 8
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate readerAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate reader
ChEMBL 203 4 4 4 -1.6 N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O 10.1021/jm901523t
5310979 1340 None 23 Rat Functional pEC50 = 7.4 7.4 1 8
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate readerAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate reader
ChEMBL 203 4 4 4 -1.6 N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O 10.1021/jm901523t
CHEMBL284193 1340 None 23 Rat Functional pEC50 = 7.4 7.4 1 8
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate readerAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate reader
ChEMBL 203 4 4 4 -1.6 N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O 10.1021/jm901523t
11344646 126844 None 0 Human Functional pEC50 = 7.4 7.4 2 3
Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor
ChEMBL 199 2 3 3 -0.2 C[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/jm040222y
CHEMBL365368 126844 None 0 Human Functional pEC50 = 7.4 7.4 2 3
Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor
ChEMBL 199 2 3 3 -0.2 C[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/jm040222y
46887493 8586 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 247 6 0 2 4.0 CCCCCC[C@@H]1CN(c2ccccc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1094762 8586 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 247 6 0 2 4.0 CCCCCC[C@@H]1CN(c2ccccc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
11951449 66743 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 495 9 1 6 7.2 CCCc1c(OCc2cccc(Oc3ccc(-c4nn[nH]n4)cc3)c2)ccc2c1ccn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
CHEMBL185659 66743 None 0 Human Functional pEC50 = 6.4 6.4 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 495 9 1 6 7.2 CCCc1c(OCc2cccc(Oc3ccc(-c4nn[nH]n4)cc3)c2)ccc2c1ccn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
51356571 61992 None 0 Rat Functional pEC50 = 6.3 6.3 - 1
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 388 3 0 4 4.8 C[C@@H]1C[C@H](c2ccc(C(F)(F)F)cc2)CCN1Cc1nc2ncccc2n1C 10.1021/jm101414h
CHEMBL1774224 61992 None 0 Rat Functional pEC50 = 6.3 6.3 - 1
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 388 3 0 4 4.8 C[C@@H]1C[C@H](c2ccc(C(F)(F)F)cc2)CCN1Cc1nc2ncccc2n1C 10.1021/jm101414h
11494153 66102 None 0 Human Functional pEC50 = 5.3 5.3 - 1
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 356 10 1 4 5.2 Cc1c(OCCCCOc2ccccc2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
CHEMBL183808 66102 None 0 Human Functional pEC50 = 5.3 5.3 - 1
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 356 10 1 4 5.2 Cc1c(OCCCCOc2ccccc2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
118714752 114638 None 0 Human Functional pEC50 = 7.3 7.3 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 401 4 0 4 4.5 N#Cc1c(N2CCC(c3cccc(C(F)(F)F)c3)CC2)ccn(CC2CC2)c1=O 10.1021/jm500496m
CHEMBL3337518 114638 None 0 Human Functional pEC50 = 7.3 7.3 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 401 4 0 4 4.5 N#Cc1c(N2CCC(c3cccc(C(F)(F)F)c3)CC2)ccn(CC2CC2)c1=O 10.1021/jm500496m
71136640 123469 None 0 Human Functional pEC50 = 7.3 7.3 60 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@@H](Sc2c[nH]nn2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616853 123469 None 0 Human Functional pEC50 = 7.3 7.3 60 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@@H](Sc2c[nH]nn2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
53240406 123463 None 21 Human Functional pEC50 = 7.3 7.3 107 4
Agonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616847 123463 None 21 Human Functional pEC50 = 7.3 7.3 107 4
Agonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
70689925 74622 None 0 Human Functional pEC50 = 6.3 6.3 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 295 5 1 4 3.5 CNc1ccc(-c2ccn(CCC(C)C)c(=O)c2C#N)cc1 10.1021/jm2016864
CHEMBL2029801 74622 None 0 Human Functional pEC50 = 6.3 6.3 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 295 5 1 4 3.5 CNc1ccc(-c2ccn(CCC(C)C)c(=O)c2C#N)cc1 10.1021/jm2016864
118714741 114628 None 0 Human Functional pEC50 = 5.3 5.3 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 364 6 0 5 3.1 CC(C)CCn1ccc(N2CCN(Cc3ccccc3)CC2)c(C#N)c1=O 10.1021/jm500496m
CHEMBL3337507 114628 None 0 Human Functional pEC50 = 5.3 5.3 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 364 6 0 5 3.1 CC(C)CCn1ccc(N2CCN(Cc3ccccc3)CC2)c(C#N)c1=O 10.1021/jm500496m
57459480 82666 None 0 Human Functional pEC50 = 6.3 6.3 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 347 4 0 6 3.1 COCc1nnc2c(C#N)c(N3CCC(c4ccccc4)CC3)ccn12 10.1021/jm3010724
CHEMBL2179311 82666 None 0 Human Functional pEC50 = 6.3 6.3 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 347 4 0 6 3.1 COCc1nnc2c(C#N)c(N3CCC(c4ccccc4)CC3)ccn12 10.1021/jm3010724
60096231 157747 None 19 Human Functional pEC50 = 7.3 7.3 -48 4
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 334 5 4 5 -0.1 COc1cccc(C(=O)N[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)c1 10.1021/acs.jmedchem.7b01481
CHEMBL4081453 157747 None 19 Human Functional pEC50 = 7.3 7.3 -48 4
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 334 5 4 5 -0.1 COc1cccc(C(=O)N[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)c1 10.1021/acs.jmedchem.7b01481
59599565 145403 None 0 Human Functional pEC50 = 6.3 6.3 -2 2
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 445 9 2 8 4.5 CCCc1c(OCc2ccc(Oc3cc(-c4nn[nH]n4)ccn3)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2016.11.049
CHEMBL3913281 145403 None 0 Human Functional pEC50 = 6.3 6.3 -2 2
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 445 9 2 8 4.5 CCCc1c(OCc2ccc(Oc3cc(-c4nn[nH]n4)ccn3)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2016.11.049
44300587 13038 None 0 Rat Functional pEC50 = 5.3 5.3 12 2
Effective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonistEffective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonist
ChEMBL 308 5 4 5 -0.2 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccc(C(=O)O)cc2)C1 10.1016/s0960-894x(01)00329-8
CHEMBL1189911 13038 None 0 Rat Functional pEC50 = 5.3 5.3 12 2
Effective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonistEffective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonist
ChEMBL 308 5 4 5 -0.2 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccc(C(=O)O)cc2)C1 10.1016/s0960-894x(01)00329-8
CHEMBL539761 13038 None 0 Rat Functional pEC50 = 5.3 5.3 12 2
Effective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonistEffective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonist
ChEMBL 308 5 4 5 -0.2 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccc(C(=O)O)cc2)C1 10.1016/s0960-894x(01)00329-8
162647052 179735 None 0 Human Functional pEC50 = 5.3 5.3 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 295 3 0 3 3.2 Fc1cccc(CCN2CCn3c(nc4ccccc43)C2)c1 10.1016/j.ejmech.2019.111881
CHEMBL4742843 179735 None 0 Human Functional pEC50 = 5.3 5.3 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 295 3 0 3 3.2 Fc1cccc(CCN2CCn3c(nc4ccccc43)C2)c1 10.1016/j.ejmech.2019.111881
156014680 177355 None 0 Human Functional pEC50 = 6.3 6.3 -2 2
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 1250 48 0 20 8.6 COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4635960 177355 None 0 Human Functional pEC50 = 6.3 6.3 -2 2
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 1250 48 0 20 8.6 COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
70692086 74618 None 0 Human Functional pEC50 = 6.3 6.3 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 359 6 0 5 4.6 CC(C)CCn1ccc(-c2ccc(Oc3cccnc3)cc2)c(C#N)c1=O 10.1021/jm2016864
CHEMBL2029799 74618 None 0 Human Functional pEC50 = 6.3 6.3 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 359 6 0 5 4.6 CC(C)CCn1ccc(-c2ccc(Oc3cccnc3)cc2)c(C#N)c1=O 10.1021/jm2016864
44591774 192202 None 0 Human Functional pEC50 = 5.3 5.3 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 268 3 0 3 3.1 C[C@@H]1CN(Cc2ccc(-c3ccncc3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL520300 192202 None 0 Human Functional pEC50 = 5.3 5.3 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 268 3 0 3 3.1 C[C@@H]1CN(Cc2ccc(-c3ccncc3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
54583299 61973 None 0 Rat Functional pEC50 = 5.3 5.3 - 1
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 390 4 0 6 3.7 Cc1cc(C2CCN(Cc3nc4ccccc4n3C)CC2)nc(N2CCCC2)n1 10.1021/jm101414h
CHEMBL1774100 61973 None 0 Rat Functional pEC50 = 5.3 5.3 - 1
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 390 4 0 6 3.7 Cc1cc(C2CCN(Cc3nc4ccccc4n3C)CC2)nc(N2CCCC2)n1 10.1021/jm101414h
118714751 114637 None 0 Human Functional pEC50 = 7.3 7.3 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 367 4 0 4 4.2 N#Cc1c(N2CCC(c3ccc(Cl)cc3)CC2)ccn(CC2CC2)c1=O 10.1021/jm500496m
CHEMBL3337517 114637 None 0 Human Functional pEC50 = 7.3 7.3 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 367 4 0 4 4.2 N#Cc1c(N2CCC(c3ccc(Cl)cc3)CC2)ccn(CC2CC2)c1=O 10.1021/jm500496m
25008615 61980 None 0 Rat Functional pEC50 = 7.3 7.3 -1 2
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 374 3 0 4 4.4 Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2ncccc21 10.1021/jm101414h
CHEMBL1774108 61980 None 0 Rat Functional pEC50 = 7.3 7.3 -1 2
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 374 3 0 4 4.4 Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2ncccc21 10.1021/jm101414h
53240406 123463 None 21 Human Functional pEC50 = 7.3 7.3 107 4
Agonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616847 123463 None 21 Human Functional pEC50 = 7.3 7.3 107 4
Agonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor E273D and L300Q mutant expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
71119170 148860 None 0 Human Functional pEC50 = 7.3 7.3 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 468 4 1 5 1.9 CN1c2nc(C3=CC4CN(C(=O)C(C)(C)O)CC4C3)ccc2N(CC2CC2(F)F)S1(=O)=O nan
CHEMBL3940610 148860 None 0 Human Functional pEC50 = 7.3 7.3 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 468 4 1 5 1.9 CN1c2nc(C3=CC4CN(C(=O)C(C)(C)O)CC4C3)ccc2N(CC2CC2(F)F)S1(=O)=O nan
1392 73 None 32 Rat Functional pEC50 = 6.3 6.3 5 4
Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2
ChEMBL 174 2 4 4 -1.8 OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O 10.1016/s0960-894x(01)00329-8
5310984 73 None 32 Rat Functional pEC50 = 6.3 6.3 5 4
Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2
ChEMBL 174 2 4 4 -1.8 OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O 10.1016/s0960-894x(01)00329-8
CHEMBL40086 73 None 32 Rat Functional pEC50 = 6.3 6.3 5 4
Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2
ChEMBL 174 2 4 4 -1.8 OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O 10.1016/s0960-894x(01)00329-8
156014680 177355 None 0 Human Functional pEC50 = 6.3 6.3 -2 2
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 1250 48 0 20 8.6 COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4635960 177355 None 0 Human Functional pEC50 = 6.3 6.3 -2 2
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 1250 48 0 20 8.6 COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
10330132 101437 None 1 Rat Functional pEC50 = 5.3 5.3 10 2
Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor
ChEMBL 189 2 4 5 -2.2 NN1C[C@@](N)(C(=O)O)C[C@@H]1C(=O)O 10.1016/s0960-894x(99)00266-8
CHEMBL297150 101437 None 1 Rat Functional pEC50 = 5.3 5.3 10 2
Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor
ChEMBL 189 2 4 5 -2.2 NN1C[C@@](N)(C(=O)O)C[C@@H]1C(=O)O 10.1016/s0960-894x(99)00266-8
1374 2081 None 25 Human Functional pEC50 = 4.3 4.3 -19 4
Agonist activity at mGlu2 receptorAgonist activity at mGlu2 receptor
ChEMBL 211 3 4 4 0.2 N[C@@H](c1ccc(c(c1)O)C(=O)O)C(=O)O 10.1021/jm060950g
5311455 2081 None 25 Human Functional pEC50 = 4.3 4.3 -19 4
Agonist activity at mGlu2 receptorAgonist activity at mGlu2 receptor
ChEMBL 211 3 4 4 0.2 N[C@@H](c1ccc(c(c1)O)C(=O)O)C(=O)O 10.1021/jm060950g
CHEMBL39372 2081 None 25 Human Functional pEC50 = 4.3 4.3 -19 4
Agonist activity at mGlu2 receptorAgonist activity at mGlu2 receptor
ChEMBL 211 3 4 4 0.2 N[C@@H](c1ccc(c(c1)O)C(=O)O)C(=O)O 10.1021/jm060950g
168299034 192790 None 0 Human Functional pEC50 = 6.3 6.3 - 1
Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding
ChEMBL 372 7 0 6 3.8 CCCCn1ncn2c(-c3ccc(OCC4CC4)c(Cl)c3)cnc2c1=O 10.1021/acs.jmedchem.2c00969
CHEMBL5219080 192790 None 0 Human Functional pEC50 = 6.3 6.3 - 1
Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding
ChEMBL 372 7 0 6 3.8 CCCCn1ncn2c(-c3ccc(OCC4CC4)c(Cl)c3)cnc2c1=O 10.1021/acs.jmedchem.2c00969
118714750 114636 None 0 Human Functional pEC50 = 7.3 7.3 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 367 4 0 4 4.2 N#Cc1c(N2CCC(c3ccccc3Cl)CC2)ccn(CC2CC2)c1=O 10.1021/jm500496m
CHEMBL3337516 114636 None 0 Human Functional pEC50 = 7.3 7.3 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 367 4 0 4 4.2 N#Cc1c(N2CCC(c3ccccc3Cl)CC2)ccn(CC2CC2)c1=O 10.1021/jm500496m
168295099 193159 None 0 Human Functional pEC50 = 6.3 6.3 - 1
Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding
ChEMBL 378 6 0 5 4.0 CCCCn1ccn2c(CN3CCC(c4ccccc4)CC3)c(C)nc2c1=O 10.1021/acs.jmedchem.2c00969
CHEMBL5219090 193159 None 0 Human Functional pEC50 = 6.3 6.3 - 1
Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding
ChEMBL 378 6 0 5 4.0 CCCCn1ccn2c(CN3CCC(c4ccccc4)CC3)c(C)nc2c1=O 10.1021/acs.jmedchem.2c00969
CHEMBL5223017 193159 None 0 Human Functional pEC50 = 6.3 6.3 - 1
Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding
ChEMBL 378 6 0 5 4.0 CCCCn1ccn2c(CN3CCC(c4ccccc4)CC3)c(C)nc2c1=O 10.1021/acs.jmedchem.2c00969
46830123 1073 None 0 Human Functional pEC50 = 5.3 5.3 - 1
Agonist activity at human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by LIPR assayAgonist activity at human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by LIPR assay
ChEMBL 350 4 0 4 4.3 N#Cc1cccc(c1)N1C[C@H](OC1=O)COc1ccc(cc1)C(C)(C)C 10.1016/j.bmcl.2010.03.089
6321 1073 None 0 Human Functional pEC50 = 5.3 5.3 - 1
Agonist activity at human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by LIPR assayAgonist activity at human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by LIPR assay
ChEMBL 350 4 0 4 4.3 N#Cc1cccc(c1)N1C[C@H](OC1=O)COc1ccc(cc1)C(C)(C)C 10.1016/j.bmcl.2010.03.089
CHEMBL1094763 1073 None 0 Human Functional pEC50 = 5.3 5.3 - 1
Agonist activity at human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by LIPR assayAgonist activity at human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by LIPR assay
ChEMBL 350 4 0 4 4.3 N#Cc1cccc(c1)N1C[C@H](OC1=O)COc1ccc(cc1)C(C)(C)C 10.1016/j.bmcl.2010.03.089
46197780 5584 None 0 Rat Functional pEC50 = 4.3 4.3 -25 4
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate readerAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate reader
ChEMBL 273 7 4 4 -0.2 N[C@@H](CCP(=O)(O)CC(Cl)C(=O)O)C(=O)O 10.1021/jm901523t
CHEMBL1076865 5584 None 0 Rat Functional pEC50 = 4.3 4.3 -25 4
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate readerAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate reader
ChEMBL 273 7 4 4 -0.2 N[C@@H](CCP(=O)(O)CC(Cl)C(=O)O)C(=O)O 10.1021/jm901523t
44591684 184442 None 0 Human Functional pEC50 = 8.3 8.3 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 317 5 0 3 4.4 CC(Oc1ccc(CN2C[C@@H](C)OC2=O)cc1)C1CCCCC1 10.1016/j.bmcl.2009.03.032
CHEMBL484340 184442 None 0 Human Functional pEC50 = 8.3 8.3 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 317 5 0 3 4.4 CC(Oc1ccc(CN2C[C@@H](C)OC2=O)cc1)C1CCCCC1 10.1016/j.bmcl.2009.03.032
44361401 31349 None 0 Rat Functional pEC50 = 8.3 8.3 1 5
Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells
ChEMBL 175 3 4 4 -1.9 N[C@H](C(=O)O)[C@H]1[C@@H](O)[C@@H]1C(=O)O 10.1021/jm030967o
CHEMBL140197 31349 None 0 Rat Functional pEC50 = 8.3 8.3 1 5
Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells
ChEMBL 175 3 4 4 -1.9 N[C@H](C(=O)O)[C@H]1[C@@H](O)[C@@H]1C(=O)O 10.1021/jm030967o
1393 1539 None 42 Human Functional pEC50 = 8.3 8.3 2 6
Agonistic activity against Human Metabotropic glutamate receptor 2Agonistic activity against Human Metabotropic glutamate receptor 2
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm970719q
1396 1539 None 42 Human Functional pEC50 = 8.3 8.3 2 6
Agonistic activity against Human Metabotropic glutamate receptor 2Agonistic activity against Human Metabotropic glutamate receptor 2
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm970719q
213056 1539 None 42 Human Functional pEC50 = 8.3 8.3 2 6
Agonistic activity against Human Metabotropic glutamate receptor 2Agonistic activity against Human Metabotropic glutamate receptor 2
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm970719q
CHEMBL8759 1539 None 42 Human Functional pEC50 = 8.3 8.3 2 6
Agonistic activity against Human Metabotropic glutamate receptor 2Agonistic activity against Human Metabotropic glutamate receptor 2
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm970719q
1393 1539 None 42 Human Functional pEC50 = 8.3 8.3 2 6
Compound was evaluated for agonist activity against human mGluR2Compound was evaluated for agonist activity against human mGluR2
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1016/s0960-894x(98)00146-2
1396 1539 None 42 Human Functional pEC50 = 8.3 8.3 2 6
Compound was evaluated for agonist activity against human mGluR2Compound was evaluated for agonist activity against human mGluR2
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1016/s0960-894x(98)00146-2
213056 1539 None 42 Human Functional pEC50 = 8.3 8.3 2 6
Compound was evaluated for agonist activity against human mGluR2Compound was evaluated for agonist activity against human mGluR2
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1016/s0960-894x(98)00146-2
CHEMBL8759 1539 None 42 Human Functional pEC50 = 8.3 8.3 2 6
Compound was evaluated for agonist activity against human mGluR2Compound was evaluated for agonist activity against human mGluR2
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1016/s0960-894x(98)00146-2
71476419 123476 None 0 Human Functional pEC50 = 8.3 8.3 51 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@H](Sc2c[nH]nn2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616860 123476 None 0 Human Functional pEC50 = 8.3 8.3 51 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@H](Sc2c[nH]nn2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
71457756 83936 None 0 Human Functional pEC50 = 8.3 8.3 66 2
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 396 5 0 5 4.7 COc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL2206440 83936 None 0 Human Functional pEC50 = 8.3 8.3 66 2
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 396 5 0 5 4.7 COc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/acs.jmedchem.0c01058
71457756 83936 None 0 Human Functional pEC50 = 8.3 8.3 66 2
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 396 5 0 5 4.7 COc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL2206440 83936 None 0 Human Functional pEC50 = 8.3 8.3 66 2
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 396 5 0 5 4.7 COc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/acs.jmedchem.0c01058
117968589 142355 None 0 Human Functional pEC50 = 8.3 8.3 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 423 6 0 4 5.7 CC(C)(COc1ccn2c(CC3CC3)nnc2c1C(F)(F)F)c1ccc(Cl)cc1 10.1016/j.bmc.2016.11.018
CHEMBL3884936 142355 None 0 Human Functional pEC50 = 8.3 8.3 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 423 6 0 4 5.7 CC(C)(COc1ccn2c(CC3CC3)nnc2c1C(F)(F)F)c1ccc(Cl)cc1 10.1016/j.bmc.2016.11.018
53240406 123463 None 21 Human Functional pEC50 = 8.3 8.3 107 4
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616847 123463 None 21 Human Functional pEC50 = 8.3 8.3 107 4
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
68109580 158617 None 0 Human Functional pEC50 = 8.2 8.2 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 471 7 1 6 5.5 COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cn1 10.1021/acs.jmedchem.7b00669
CHEMBL4091370 158617 None 0 Human Functional pEC50 = 8.2 8.2 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 471 7 1 6 5.5 COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cn1 10.1021/acs.jmedchem.7b00669
162650622 180156 None 0 Human Functional pEC50 = 7.3 7.3 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 431 6 0 4 4.3 O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(F)cc1Br 10.1016/j.ejmech.2019.111881
CHEMBL4747716 180156 None 0 Human Functional pEC50 = 7.3 7.3 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 431 6 0 4 4.3 O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(F)cc1Br 10.1016/j.ejmech.2019.111881
162662472 182159 None 0 Human Functional pEC50 = 7.3 7.3 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 371 6 0 4 3.6 O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(F)cc1F 10.1016/j.ejmech.2019.111881
CHEMBL4781224 182159 None 0 Human Functional pEC50 = 7.3 7.3 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 371 6 0 4 3.6 O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(F)cc1F 10.1016/j.ejmech.2019.111881
155513095 169807 None 0 Human Functional pEC50 = 7.3 7.3 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 329 2 0 3 3.4 Brc1cc(Br)c2nnn(CC3CC3)c2c1 10.1021/acs.jmedchem.8b00161
CHEMBL4437986 169807 None 0 Human Functional pEC50 = 7.3 7.3 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 329 2 0 3 3.4 Brc1cc(Br)c2nnn(CC3CC3)c2c1 10.1021/acs.jmedchem.8b00161
155540333 172599 None 0 Human Functional pEC50 = 7.3 7.3 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 338 3 0 4 4.3 Fc1cc(Cl)ccc1-c1ccc(Cn2nnc3ccccc32)cn1 10.1021/acs.jmedchem.8b00161
CHEMBL4483344 172599 None 0 Human Functional pEC50 = 7.3 7.3 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 338 3 0 4 4.3 Fc1cc(Cl)ccc1-c1ccc(Cn2nnc3ccccc32)cn1 10.1021/acs.jmedchem.8b00161
CHEMBL5074997 216839 None 0 Human Functional pEC50 = 7.3 7.3 - 1
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL None None None O=C1c2nc3cccc(Br)c3n2CCN1CC1CCC1 10.1021/acs.jmedchem.1c00563
CHEMBL5091657 217809 None 0 Human Functional pEC50 = 7.3 7.3 - 1
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL None None None O=C1c2nc3cccc(Br)c3n2CCN1Cc1ccc(Br)cc1F 10.1021/acs.jmedchem.1c00563
10807972 35826 None 1 Rat Functional pEC50 = 7.3 7.3 -3 4
Antagonist activity against Metabotropic glutamate receptor 2<br>expressed in CHO cells was evaluated in presence of 30 uM glutamic acidAntagonist activity against Metabotropic glutamate receptor 2<br>expressed in CHO cells was evaluated in presence of 30 uM glutamic acid
ChEMBL 353 5 3 4 2.8 N[C@@](CC1c2ccccc2Oc2ccccc21)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm000346k
CHEMBL144151 35826 None 1 Rat Functional pEC50 = 7.3 7.3 -3 4
Antagonist activity against Metabotropic glutamate receptor 2<br>expressed in CHO cells was evaluated in presence of 30 uM glutamic acidAntagonist activity against Metabotropic glutamate receptor 2<br>expressed in CHO cells was evaluated in presence of 30 uM glutamic acid
ChEMBL 353 5 3 4 2.8 N[C@@](CC1c2ccccc2Oc2ccccc21)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm000346k
104766 33 None 30 Rat Functional pEC50 = 5.3 5.3 2 14
Tested for the agonistic activity against Metabotropic glutamate receptor 2Tested for the agonistic activity against Metabotropic glutamate receptor 2
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1016/S0960-894X(97)00068-1
1365 33 None 30 Rat Functional pEC50 = 5.3 5.3 2 14
Tested for the agonistic activity against Metabotropic glutamate receptor 2Tested for the agonistic activity against Metabotropic glutamate receptor 2
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1016/S0960-894X(97)00068-1
CHEMBL34453 33 None 30 Rat Functional pEC50 = 5.3 5.3 2 14
Tested for the agonistic activity against Metabotropic glutamate receptor 2Tested for the agonistic activity against Metabotropic glutamate receptor 2
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1016/S0960-894X(97)00068-1
46215708 80836 None 0 Human Functional pEC50 = 6.3 6.3 - 1
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 424 3 0 5 5.3 N#Cc1c(-c2ccc3c(ccn3C3CCOCC3)c2)ccn2c(CC(F)(F)F)cnc12 10.1021/jm201561r
CHEMBL2152114 80836 None 0 Human Functional pEC50 = 6.3 6.3 - 1
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 424 3 0 5 5.3 N#Cc1c(-c2ccc3c(ccn3C3CCOCC3)c2)ccn2c(CC(F)(F)F)cnc12 10.1021/jm201561r
71450118 82682 None 0 Human Functional pEC50 = 6.3 6.3 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 330 3 0 4 4.2 CCc1cnc2c(C#N)c(N3CCC(c4ccccc4)CC3)ccn12 10.1021/jm3010724
CHEMBL2179328 82682 None 0 Human Functional pEC50 = 6.3 6.3 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 330 3 0 4 4.2 CCc1cnc2c(C#N)c(N3CCC(c4ccccc4)CC3)ccn12 10.1021/jm3010724
53320175 57754 None 0 Human Functional pEC50 = 6.3 6.3 - 1
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 390 5 0 4 5.9 CCCn1ccc2cc(-c3ccc(Oc4ccccc4)nc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669392 57754 None 0 Human Functional pEC50 = 6.3 6.3 - 1
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 390 5 0 4 5.9 CCCn1ccc2cc(-c3ccc(Oc4ccccc4)nc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
90668092 109593 None 0 Human Functional pEC50 = 6.3 6.3 - 1
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 306 6 1 3 4.1 CCCn1ccc2c(NCCc3ccccc3)cccc2c1=O 10.1039/C0MD00200C
CHEMBL3221831 109593 None 0 Human Functional pEC50 = 6.3 6.3 - 1
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 306 6 1 3 4.1 CCCn1ccc2c(NCCc3ccccc3)cccc2c1=O 10.1039/C0MD00200C
90668100 109604 None 0 Human Functional pEC50 = 6.3 6.3 - 1
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 322 6 1 4 4.0 CCCn1ccc2c(NCc3ccc(OC)cc3)cccc2c1=O 10.1039/C0MD00200C
CHEMBL3221841 109604 None 0 Human Functional pEC50 = 6.3 6.3 - 1
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 322 6 1 4 4.0 CCCn1ccc2c(NCc3ccc(OC)cc3)cccc2c1=O 10.1039/C0MD00200C
90668105 109610 None 0 Human Functional pEC50 = 6.3 6.3 - 1
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 356 6 0 4 4.6 CCCn1ccc2c(N(Cl)Cc3cccc(OC)c3)cccc2c1=O 10.1039/C0MD00200C
CHEMBL3221847 109610 None 0 Human Functional pEC50 = 6.3 6.3 - 1
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 356 6 0 4 4.6 CCCn1ccc2c(N(Cl)Cc3cccc(OC)c3)cccc2c1=O 10.1039/C0MD00200C
53325603 57739 None 0 Human Functional pEC50 = 5.3 5.3 - 1
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 306 3 0 4 2.9 CCCn1ccc2cc(N3CCOCC3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669377 57739 None 0 Human Functional pEC50 = 5.3 5.3 - 1
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 306 3 0 4 2.9 CCCn1ccc2cc(N3CCOCC3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
53316861 57740 None 0 Human Functional pEC50 = 5.3 5.3 - 1
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 320 3 1 4 3.0 CCCn1ccc2cc(N3CCC(O)CC3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669378 57740 None 0 Human Functional pEC50 = 5.3 5.3 - 1
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 320 3 1 4 3.0 CCCn1ccc2cc(N3CCC(O)CC3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
53323493 57749 None 0 Human Functional pEC50 = 5.3 5.3 - 1
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 341 4 0 4 4.2 CCCn1ccc2cc(-c3ccc(N(C)C)nc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669388 57749 None 0 Human Functional pEC50 = 5.3 5.3 - 1
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 341 4 0 4 4.2 CCCn1ccc2cc(-c3ccc(N(C)C)nc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
24849462 202214 None 0 Human Functional pEC50 = 5.3 5.3 - 1
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 339 3 0 3 4.6 Cn1c(CN2CCC(c3ccc(Cl)cc3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL593744 202214 None 0 Human Functional pEC50 = 5.3 5.3 - 1
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 339 3 0 3 4.6 Cn1c(CN2CCC(c3ccc(Cl)cc3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
90668104 109609 None 0 Human Functional pEC50 = 4.3 4.3 - 1
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 326 5 0 3 4.6 CCCn1ccc2c(N(Cl)Cc3ccccc3)cccc2c1=O 10.1039/C0MD00200C
CHEMBL3221846 109609 None 0 Human Functional pEC50 = 4.3 4.3 - 1
Positive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysisPositive allosteric modulation of human mGluR2 expressed in CHO cells assessed as incorporation of [35S]GTPgammaS after 30 mins by scintillation counting analysis
ChEMBL 326 5 0 3 4.6 CCCn1ccc2c(N(Cl)Cc3ccccc3)cccc2c1=O 10.1039/C0MD00200C
60096194 156679 None 0 Human Functional pEC50 = 6.3 6.3 -1 2
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 290 5 4 4 0.3 N[C@@]1(C(=O)O)C[C@H](NCc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4068679 156679 None 0 Human Functional pEC50 = 6.3 6.3 -1 2
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 290 5 4 4 0.3 N[C@@]1(C(=O)O)C[C@H](NCc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
156014194 177315 None 0 Human Functional pEC50 = 6.3 6.3 -2 2
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 941 27 0 13 8.5 COc1c(OCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4635373 177315 None 0 Human Functional pEC50 = 6.3 6.3 -2 2
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 941 27 0 13 8.5 COc1c(OCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
156018860 178019 None 0 Human Functional pEC50 = 6.3 6.3 -2 2
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 1074 36 0 16 8.6 COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4645193 178019 None 0 Human Functional pEC50 = 6.3 6.3 -2 2
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 1074 36 0 16 8.6 COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
71117065 149363 None 0 Human Functional pEC50 = 6.3 6.3 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 539 3 1 8 3.0 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)C5(O)CCN(C(=O)OC(C)(C)C)C5)CC4C3)nc21 nan
CHEMBL3944557 149363 None 0 Human Functional pEC50 = 6.3 6.3 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 539 3 1 8 3.0 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)C5(O)CCN(C(=O)OC(C)(C)C)C5)CC4C3)nc21 nan
156014194 177315 None 0 Human Functional pEC50 = 6.3 6.3 -2 2
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 941 27 0 13 8.5 COc1c(OCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4635373 177315 None 0 Human Functional pEC50 = 6.3 6.3 -2 2
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 941 27 0 13 8.5 COc1c(OCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
156018860 178019 None 0 Human Functional pEC50 = 6.3 6.3 -2 2
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 1074 36 0 16 8.6 COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4645193 178019 None 0 Human Functional pEC50 = 6.3 6.3 -2 2
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 1074 36 0 16 8.6 COc1c(OCCOCCOCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
57459542 82681 None 0 Human Functional pEC50 = 6.3 6.3 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 401 4 0 5 4.5 FC(F)(F)c1c(N2CCC(c3cccnc3)CC2)ccn2c(CC3CC3)nnc12 10.1021/jm3010724
CHEMBL2179327 82681 None 0 Human Functional pEC50 = 6.3 6.3 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 401 4 0 5 4.5 FC(F)(F)c1c(N2CCC(c3cccnc3)CC2)ccn2c(CC3CC3)nnc12 10.1021/jm3010724
28407322 182943 None 7 Human Functional pEC50 = 5.3 5.3 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 277 3 0 3 3.1 c1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
CHEMBL4791292 182943 None 7 Human Functional pEC50 = 5.3 5.3 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 277 3 0 3 3.1 c1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
3756397 8316 None 0 Rat Functional pEC50 = 4.3 4.3 -7 4
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate readerAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate reader
ChEMBL 239 7 4 4 -0.5 NC(CCP(=O)(O)CCC(=O)O)C(=O)O 10.1021/jm901523t
4041087 8316 None 0 Rat Functional pEC50 = 4.3 4.3 -7 4
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate readerAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate reader
ChEMBL 239 7 4 4 -0.5 NC(CCP(=O)(O)CCC(=O)O)C(=O)O 10.1021/jm901523t
CHEMBL1092727 8316 None 0 Rat Functional pEC50 = 4.3 4.3 -7 4
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate readerAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate reader
ChEMBL 239 7 4 4 -0.5 NC(CCP(=O)(O)CCC(=O)O)C(=O)O 10.1021/jm901523t
44591747 185022 None 0 Human Functional pEC50 = 7.3 7.3 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 297 4 0 3 3.7 COc1ccc(-c2ccc(CN3C[C@@H](C)OC3=O)cc2)cc1 10.1016/j.bmcl.2009.03.032
CHEMBL485331 185022 None 0 Human Functional pEC50 = 7.3 7.3 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 297 4 0 3 3.7 COc1ccc(-c2ccc(CN3C[C@@H](C)OC3=O)cc2)cc1 10.1016/j.bmcl.2009.03.032
71137034 123466 None 0 Human Functional pEC50 = 7.3 7.3 7 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 334 5 4 6 0.3 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc(C(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616850 123466 None 0 Human Functional pEC50 = 7.3 7.3 7 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 334 5 4 6 0.3 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc(C(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
156012835 177539 None 0 Human Functional pEC50 = 6.3 6.3 -2 2
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 985 30 0 14 8.5 COc1c(OCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4638687 177539 None 0 Human Functional pEC50 = 6.3 6.3 -2 2
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 985 30 0 14 8.5 COc1c(OCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
156012835 177539 None 0 Human Functional pEC50 = 6.3 6.3 -2 2
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 985 30 0 14 8.5 COc1c(OCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4638687 177539 None 0 Human Functional pEC50 = 6.3 6.3 -2 2
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 985 30 0 14 8.5 COc1c(OCCOCCOCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
71137010 123465 None 0 Human Functional pEC50 = 7.3 7.3 5 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 352 4 4 6 0.4 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc(C(F)(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616849 123465 None 0 Human Functional pEC50 = 7.3 7.3 5 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 352 4 4 6 0.4 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc(C(F)(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
162646719 179715 None 0 Human Functional pEC50 = 6.3 6.3 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 357 5 0 3 4.7 Fc1cc(Cl)ccc1CCCCN1CCn2c(nc3ccccc32)C1 10.1016/j.ejmech.2019.111881
CHEMBL4742364 179715 None 0 Human Functional pEC50 = 6.3 6.3 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 357 5 0 3 4.7 Fc1cc(Cl)ccc1CCCCN1CCn2c(nc3ccccc32)C1 10.1016/j.ejmech.2019.111881
162662970 182038 None 0 Human Functional pEC50 = 6.3 6.3 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 343 5 0 4 3.6 Fc1ccc(OCCCN2CCn3c(nc4ccccc43)C2)cc1F 10.1016/j.ejmech.2019.111881
CHEMBL4779768 182038 None 0 Human Functional pEC50 = 6.3 6.3 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 343 5 0 4 3.6 Fc1ccc(OCCCN2CCn3c(nc4ccccc43)C2)cc1F 10.1016/j.ejmech.2019.111881
CHEMBL5090065 217730 None 0 Human Functional pEC50 = 6.3 6.3 - 1
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL None None None O=C1c2nc3cccc(Br)c3n2CCN1Cc1ccc(Cl)nc1 10.1021/acs.jmedchem.1c00563
156015654 177626 None 0 Human Functional pEC50 = 6.3 6.3 -1 2
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 897 24 0 12 8.5 COc1c(OCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4639821 177626 None 0 Human Functional pEC50 = 6.3 6.3 -1 2
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 897 24 0 12 8.5 COc1c(OCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
118714744 114616 None 0 Human Functional pEC50 = 7.3 7.3 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 347 4 0 4 3.9 N#Cc1c(N2CCC(c3ccccc3)CC2)ccn(CC2CCC2)c1=O 10.1021/jm500496m
CHEMBL3337456 114616 None 0 Human Functional pEC50 = 7.3 7.3 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 347 4 0 4 3.9 N#Cc1c(N2CCC(c3ccccc3)CC2)ccn(CC2CCC2)c1=O 10.1021/jm500496m
66788653 82668 None 0 Human Functional pEC50 = 7.3 7.3 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 394 3 0 4 4.9 FC(F)(F)Cc1nnc2c(Cl)c(N3CCC(c4ccccc4)CC3)ccn12 10.1021/jm3010724
CHEMBL2179313 82668 None 0 Human Functional pEC50 = 7.3 7.3 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 394 3 0 4 4.9 FC(F)(F)Cc1nnc2c(Cl)c(N3CCC(c4ccccc4)CC3)ccn12 10.1021/jm3010724
156015654 177626 None 0 Human Functional pEC50 = 6.3 6.3 -1 2
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 897 24 0 12 8.5 COc1c(OCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4639821 177626 None 0 Human Functional pEC50 = 6.3 6.3 -1 2
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 897 24 0 12 8.5 COc1c(OCCOCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
70681519 74621 None 0 Human Functional pEC50 = 6.3 6.3 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 359 6 0 5 4.6 CC(C)CCn1ccc(-c2ccc(Oc3ccncc3)cc2)c(C#N)c1=O 10.1021/jm2016864
CHEMBL2029800 74621 None 0 Human Functional pEC50 = 6.3 6.3 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 359 6 0 5 4.6 CC(C)CCn1ccc(-c2ccc(Oc3ccncc3)cc2)c(C#N)c1=O 10.1021/jm2016864
162669063 182842 None 0 Human Functional pEC50 = 6.3 6.3 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 357 5 0 4 4.7 Clc1ccc(SCCCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
CHEMBL4789937 182842 None 0 Human Functional pEC50 = 6.3 6.3 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 357 5 0 4 4.7 Clc1ccc(SCCCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
44392629 64789 None 0 Human Functional pEC50 = 6.3 6.3 - 1
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 456 10 1 4 5.9 CC(C)CC(=O)c1ccc(OCCCCOc2cccc(F)c2F)c(Br)c1O 10.1016/j.bmcl.2004.09.028
CHEMBL181921 64789 None 0 Human Functional pEC50 = 6.3 6.3 - 1
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 456 10 1 4 5.9 CC(C)CC(=O)c1ccc(OCCCCOc2cccc(F)c2F)c(Br)c1O 10.1016/j.bmcl.2004.09.028
11271167 66821 None 0 Human Functional pEC50 = 6.3 6.3 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 461 11 1 6 6.1 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
CHEMBL185994 66821 None 0 Human Functional pEC50 = 6.3 6.3 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 461 11 1 6 6.1 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
11950927 123496 None 0 Human Functional pEC50 = 6.3 6.3 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 475 11 1 6 6.4 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1cc(C)n2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
CHEMBL361724 123496 None 0 Human Functional pEC50 = 6.3 6.3 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 475 11 1 6 6.4 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1cc(C)n2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
57459477 82687 None 0 Human Functional pEC50 = 7.3 7.3 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 385 3 0 5 4.1 N#Cc1c(N2CCC(c3ccccc3)CC2)ccn2c(CC(F)(F)F)nnc12 10.1021/jm3010724
CHEMBL2179333 82687 None 0 Human Functional pEC50 = 7.3 7.3 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 385 3 0 5 4.1 N#Cc1c(N2CCC(c3ccccc3)CC2)ccn2c(CC(F)(F)F)nnc12 10.1021/jm3010724
71117141 147537 None 0 Human Functional pEC50 = 7.3 7.3 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 435 4 0 8 2.1 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)Cn3cncn3)nc21 nan
CHEMBL3930164 147537 None 0 Human Functional pEC50 = 7.3 7.3 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 435 4 0 8 2.1 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)Cn3cncn3)nc21 nan
57459477 82687 None 0 Human Functional pEC50 = 7.3 7.3 - 1
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 385 3 0 5 4.1 N#Cc1c(N2CCC(c3ccccc3)CC2)ccn2c(CC(F)(F)F)nnc12 10.1021/jm300912k
CHEMBL2179333 82687 None 0 Human Functional pEC50 = 7.3 7.3 - 1
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 385 3 0 5 4.1 N#Cc1c(N2CCC(c3ccccc3)CC2)ccn2c(CC(F)(F)F)nnc12 10.1021/jm300912k
49801368 159752 None 0 Human Functional pEC50 = 7.3 7.3 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 442 5 0 5 6.0 Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)ccn1 10.1021/acs.jmedchem.7b00669
CHEMBL4103808 159752 None 0 Human Functional pEC50 = 7.3 7.3 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 442 5 0 5 6.0 Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)ccn1 10.1021/acs.jmedchem.7b00669
59599616 146352 None 1 Human Functional pEC50 = 6.3 6.3 -1 2
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 445 9 2 8 4.5 CCCc1c(OCc2ccc(Oc3cccc(-c4nn[nH]n4)c3)nc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2016.11.049
CHEMBL3920609 146352 None 1 Human Functional pEC50 = 6.3 6.3 -1 2
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 445 9 2 8 4.5 CCCc1c(OCc2ccc(Oc3cccc(-c4nn[nH]n4)c3)nc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2016.11.049
25125217 555 None 27 Human Functional pEC50 = 6.3 6.3 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 487 6 1 7 3.5 Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1 10.1021/acs.jmedchem.7b00669
7678 555 None 27 Human Functional pEC50 = 6.3 6.3 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 487 6 1 7 3.5 Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1 10.1021/acs.jmedchem.7b00669
CHEMBL3937907 555 None 27 Human Functional pEC50 = 6.3 6.3 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 487 6 1 7 3.5 Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1 10.1021/acs.jmedchem.7b00669
DB16073 555 None 27 Human Functional pEC50 = 6.3 6.3 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 487 6 1 7 3.5 Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1 10.1021/acs.jmedchem.7b00669
44428730 144794 None 1 Rat Functional pEC50 = 4.3 4.3 - 1
Agonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAgonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level
ChEMBL 185 3 3 5 -0.2 CCc1c(C(N)C(=O)O)cnn1O 10.1016/j.bmc.2007.02.047
CHEMBL390863 144794 None 1 Rat Functional pEC50 = 4.3 4.3 - 1
Agonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAgonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level
ChEMBL 185 3 3 5 -0.2 CCc1c(C(N)C(=O)O)cnn1O 10.1016/j.bmc.2007.02.047
137652320 157366 None 0 Human Functional pEC50 = 7.2 7.2 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 454 7 0 6 5.4 COc1ccc(COc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2)cn1 10.1021/acs.jmedchem.7b00669
CHEMBL4076786 157366 None 0 Human Functional pEC50 = 7.2 7.2 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 454 7 0 6 5.4 COc1ccc(COc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2)cn1 10.1021/acs.jmedchem.7b00669
24779944 7870 None 0 Rat Functional pEC50 = 4.2 4.2 -36 3
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate readerAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate reader
ChEMBL 225 6 4 4 -0.9 N[C@@H](CCP(=O)(O)CC(=O)O)C(=O)O 10.1021/jm901523t
CHEMBL1089852 7870 None 0 Rat Functional pEC50 = 4.2 4.2 -36 3
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate readerAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate reader
ChEMBL 225 6 4 4 -0.9 N[C@@H](CCP(=O)(O)CC(=O)O)C(=O)O 10.1021/jm901523t
44428730 144794 None 1 Rat Functional pEC50 = 4.2 4.2 - 1
Agonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAgonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level
ChEMBL 185 3 3 5 -0.2 CCc1c(C(N)C(=O)O)cnn1O 10.1016/j.bmc.2007.02.047
CHEMBL390863 144794 None 1 Rat Functional pEC50 = 4.2 4.2 - 1
Agonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAgonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level
ChEMBL 185 3 3 5 -0.2 CCc1c(C(N)C(=O)O)cnn1O 10.1016/j.bmc.2007.02.047
11546303 65255 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 421 10 1 5 5.0 CC(C)CC(=O)c1ccc(OCCCCOc2cccnc2)c(Br)c1O 10.1016/j.bmcl.2004.09.028
CHEMBL182668 65255 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 421 10 1 5 5.0 CC(C)CC(=O)c1ccc(OCCCCOc2cccnc2)c(Br)c1O 10.1016/j.bmcl.2004.09.028
44392671 65290 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 421 7 1 5 6.4 Cc1c(OCc2ccc(Sc3ccncc3)cc2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2004.09.028
CHEMBL182822 65290 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 421 7 1 5 6.4 Cc1c(OCc2ccc(Sc3ccncc3)cc2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2004.09.028
46887369 8877 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 311 5 0 3 4.2 CC(C)c1cccc(OCC2CN(c3ccccc3)C(=O)O2)c1 10.1016/j.bmcl.2010.03.089
CHEMBL1097380 8877 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 311 5 0 3 4.2 CC(C)c1cccc(OCC2CN(c3ccccc3)C(=O)O2)c1 10.1016/j.bmcl.2010.03.089
CHEMBL5081320 217230 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL None None None O=C1c2nc3cccc(-c4ccc(F)cc4)c3n2CCN1CC1CC1 10.1021/acs.jmedchem.1c00563
44155863 8548 None 0 Human Functional pEC50 = 5.2 5.2 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 262 6 1 3 3.6 CCCCCCC1CN(c2ccc(N)cc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1094460 8548 None 0 Human Functional pEC50 = 5.2 5.2 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 262 6 1 3 3.6 CCCCCCC1CN(c2ccc(N)cc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
25173209 189131 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 289 5 0 3 3.6 O=C1OCCN1Cc1ccc(OCC2CCCCC2)cc1 10.1016/j.bmcl.2009.03.032
CHEMBL509096 189131 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 289 5 0 3 3.6 O=C1OCCN1Cc1ccc(OCC2CCCCC2)cc1 10.1016/j.bmcl.2009.03.032
44155315 8657 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 247 6 0 2 4.0 CCCCCCC1CN(c2ccccc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1095385 8657 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 247 6 0 2 4.0 CCCCCCC1CN(c2ccccc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
44155642 8850 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 281 6 0 2 4.6 CCCCCCC1CN(c2cccc(Cl)c2)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1097052 8850 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 281 6 0 2 4.6 CCCCCCC1CN(c2cccc(Cl)c2)C(=O)O1 10.1016/j.bmcl.2010.03.089
46887367 8875 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 297 5 0 3 3.7 CCc1ccc(OCC2CN(c3ccccc3)C(=O)O2)cc1 10.1016/j.bmcl.2010.03.089
CHEMBL1097378 8875 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 297 5 0 3 3.7 CCc1ccc(OCC2CN(c3ccccc3)C(=O)O2)cc1 10.1016/j.bmcl.2010.03.089
71117030 145941 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 423 5 1 7 3.3 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CCC(C(=O)NCc4ncco4)CC3)nc21 nan
CHEMBL3917329 145941 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 423 5 1 7 3.3 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CCC(C(=O)NCc4ncco4)CC3)nc21 nan
44591795 192549 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 320 3 0 3 3.9 C[C@@H]1CN(Cc2ccc(-c3ccc(F)c(Cl)c3)nc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL520837 192549 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 320 3 0 3 3.9 C[C@@H]1CN(Cc2ccc(-c3ccc(F)c(Cl)c3)nc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
11952168 67364 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 461 14 1 6 6.2 CCCCCn1ccc2c(CCC)c(OCCCCOc3ccc(-c4nn[nH]n4)cc3)ccc21 10.1016/j.bmcl.2005.06.017
CHEMBL188538 67364 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 461 14 1 6 6.2 CCCCCn1ccc2c(CCC)c(OCCCCOc3ccc(-c4nn[nH]n4)cc3)ccc21 10.1016/j.bmcl.2005.06.017
57459494 83938 None 0 Human Functional pEC50 = 8.2 8.2 - 1
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 414 5 0 5 4.9 COc1cccc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm300912k
CHEMBL2206442 83938 None 0 Human Functional pEC50 = 8.2 8.2 - 1
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 414 5 0 5 4.9 COc1cccc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm300912k
155566352 176038 None 0 Human Functional pEC50 = 8.2 8.2 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 416 3 0 4 5.1 Fc1cc(Cl)ccc1-c1ccc(Cn2nnc3c(Br)cccc32)cn1 10.1021/acs.jmedchem.8b00161
CHEMBL4587631 176038 None 0 Human Functional pEC50 = 8.2 8.2 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 416 3 0 4 5.1 Fc1cc(Cl)ccc1-c1ccc(Cn2nnc3c(Br)cccc32)cn1 10.1021/acs.jmedchem.8b00161
11626955 151900 None 0 Human Functional pEC50 = 8.2 8.2 18 2
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 471 7 2 8 4.6 CC(=O)c1ccc(OCc2cccc(Oc3cc(-c4nn[nH]n4)ccn3)c2)c(C(F)(F)F)c1O 10.1016/j.bmcl.2016.11.049
CHEMBL3965244 151900 None 0 Human Functional pEC50 = 8.2 8.2 18 2
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 471 7 2 8 4.6 CC(=O)c1ccc(OCc2cccc(Oc3cc(-c4nn[nH]n4)ccn3)c2)c(C(F)(F)F)c1O 10.1016/j.bmcl.2016.11.049
117971699 142372 None 0 Human Functional pEC50 = 8.2 8.2 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 397 6 0 4 4.9 FC(F)(F)c1c(OCC(F)(F)c2ccccc2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
CHEMBL3885115 142372 None 0 Human Functional pEC50 = 8.2 8.2 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 397 6 0 4 4.9 FC(F)(F)c1c(OCC(F)(F)c2ccccc2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
71131322 123473 None 0 Human Functional pEC50 = 8.2 8.2 43 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 334 5 4 6 0.3 N[C@@]1(C(=O)O)C[C@H](Sc2nnc(C(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616857 123473 None 0 Human Functional pEC50 = 8.2 8.2 43 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 334 5 4 6 0.3 N[C@@]1(C(=O)O)C[C@H](Sc2nnc(C(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
60096228 156879 None 0 Human Functional pEC50 = 8.2 8.2 -2 2
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 320 4 5 5 -0.4 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccc(O)cc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4070866 156879 None 0 Human Functional pEC50 = 8.2 8.2 -2 2
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 320 4 5 5 -0.4 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccc(O)cc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
71137011 123474 None 0 Human Functional pEC50 = 8.2 8.2 58 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 299 4 5 7 -1.0 Nc1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
CHEMBL3616858 123474 None 0 Human Functional pEC50 = 8.2 8.2 58 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 299 4 5 7 -1.0 Nc1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
134130002 142254 None 0 Human Functional pEC50 = 8.2 8.2 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 389 6 0 4 5.6 Clc1c(OCc2ccc(-c3ccccc3)cc2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
CHEMBL3883801 142254 None 0 Human Functional pEC50 = 8.2 8.2 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 389 6 0 4 5.6 Clc1c(OCc2ccc(-c3ccccc3)cc2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
69093928 83943 None 0 Human Functional pEC50 = 8.2 8.2 - 1
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 432 5 0 5 5.0 COc1cc(F)cc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm300912k
CHEMBL2206447 83943 None 0 Human Functional pEC50 = 8.2 8.2 - 1
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 432 5 0 5 5.0 COc1cc(F)cc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm300912k
60096250 159013 None 0 Human Functional pEC50 = 8.2 8.2 -1 2
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 338 4 4 4 0.6 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccc(Cl)cc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4095567 159013 None 0 Human Functional pEC50 = 8.2 8.2 -1 2
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 338 4 4 4 0.6 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccc(Cl)cc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
117972041 142296 None 0 Human Functional pEC50 = 7.2 7.2 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 347 5 0 4 4.6 Clc1ccc(COc2ccn3c(CC4CC4)nnc3c2Cl)cc1 10.1016/j.bmc.2016.11.018
CHEMBL3884170 142296 None 0 Human Functional pEC50 = 7.2 7.2 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 347 5 0 4 4.6 Clc1ccc(COc2ccn3c(CC4CC4)nnc3c2Cl)cc1 10.1016/j.bmc.2016.11.018
155559961 174999 None 0 Human Functional pEC50 = 7.2 7.2 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 285 2 0 3 3.3 Clc1cc(Br)c2nnn(CC3CC3)c2c1 10.1021/acs.jmedchem.8b00161
CHEMBL4564190 174999 None 0 Human Functional pEC50 = 7.2 7.2 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 285 2 0 3 3.3 Clc1cc(Br)c2nnn(CC3CC3)c2c1 10.1021/acs.jmedchem.8b00161
155567522 176075 None 0 Human Functional pEC50 = 7.2 7.2 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 253 3 0 3 3.0 CCCCn1nnc2c(Br)cccc21 10.1021/acs.jmedchem.8b00161
CHEMBL4588508 176075 None 0 Human Functional pEC50 = 7.2 7.2 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 253 3 0 3 3.0 CCCCn1nnc2c(Br)cccc21 10.1021/acs.jmedchem.8b00161
CHEMBL5086642 217530 None 0 Human Functional pEC50 = 7.2 7.2 - 1
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL None None None O=C1c2nc3cccc(C(F)(F)F)c3n2CCN1CC1CCC1 10.1021/acs.jmedchem.1c00563
CHEMBL5088821 217669 None 0 Human Functional pEC50 = 7.2 7.2 - 1
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL None None None O=C1c2nc3cccc(Br)c3n2CCN1Cc1ccc(Cl)cc1F 10.1021/acs.jmedchem.1c00563
CHEMBL5093895 217942 None 0 Human Functional pEC50 = 7.2 7.2 - 1
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL None None None O=C1c2nc3cccc(C(F)(F)F)c3n2CCN1CC1CC2CCC1C2 10.1021/acs.jmedchem.1c00563
155522079 170804 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 304 3 0 4 3.7 Fc1ccccc1-c1ccc(Cn2nnc3ccccc32)cn1 10.1021/acs.jmedchem.8b00161
CHEMBL4451873 170804 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 304 3 0 4 3.7 Fc1ccccc1-c1ccc(Cn2nnc3ccccc32)cn1 10.1021/acs.jmedchem.8b00161
57459487 83933 None 0 Human Functional pEC50 = 7.2 7.2 - 1
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 402 4 0 4 5.0 Fc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c(F)c1 10.1021/jm300912k
CHEMBL2206437 83933 None 0 Human Functional pEC50 = 7.2 7.2 - 1
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 402 4 0 4 5.0 Fc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c(F)c1 10.1021/jm300912k
1310 2315 None 61 Rat Functional pEC50 = 6.2 6.2 -457 17
Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/s0960-894x(99)00266-8
1369 2315 None 61 Rat Functional pEC50 = 6.2 6.2 -457 17
Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/s0960-894x(99)00266-8
33032 2315 None 61 Rat Functional pEC50 = 6.2 6.2 -457 17
Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/s0960-894x(99)00266-8
44272391 2315 None 61 Rat Functional pEC50 = 6.2 6.2 -457 17
Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/s0960-894x(99)00266-8
88747398 2315 None 61 Rat Functional pEC50 = 6.2 6.2 -457 17
Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/s0960-894x(99)00266-8
CHEMBL575060 2315 None 61 Rat Functional pEC50 = 6.2 6.2 -457 17
Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/s0960-894x(99)00266-8
DB00142 2315 None 61 Rat Functional pEC50 = 6.2 6.2 -457 17
Agonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptorAgonistic activity evaluated in CHO(Chinese hamster ovary) cells expressing mGluR2 receptor
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/s0960-894x(99)00266-8
10376615 80600 None 0 Rat Functional pEC50 = 6.2 6.2 - 1
Effective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonistEffective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonist
ChEMBL 232 4 4 5 -2.0 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(CC(=O)O)C1 10.1016/s0960-894x(01)00329-8
CHEMBL214917 80600 None 0 Rat Functional pEC50 = 6.2 6.2 - 1
Effective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonistEffective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonist
ChEMBL 232 4 4 5 -2.0 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(CC(=O)O)C1 10.1016/s0960-894x(01)00329-8
CHEMBL544505 80600 None 0 Rat Functional pEC50 = 6.2 6.2 - 1
Effective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonistEffective concentration required for partial agonistic activity at Metabotropic glutamate receptor 2; Partial agonist
ChEMBL 232 4 4 5 -2.0 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(CC(=O)O)C1 10.1016/s0960-894x(01)00329-8
CHEMBL5074682 216814 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL None None None O=C1c2nc3cccc(-c4cccc(F)c4)c3n2CCN1CC1CC1 10.1021/acs.jmedchem.1c00563
10473248 14191 None 0 Rat Functional pEC50 = 5.2 5.2 4 3
Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2
ChEMBL 280 4 4 5 -0.2 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2O)C1 10.1016/s0960-894x(01)00329-8
CHEMBL1198741 14191 None 0 Rat Functional pEC50 = 5.2 5.2 4 3
Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2
ChEMBL 280 4 4 5 -0.2 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2O)C1 10.1016/s0960-894x(01)00329-8
CHEMBL540015 14191 None 0 Rat Functional pEC50 = 5.2 5.2 4 3
Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2Effective concentration required for agonistic activity at Metabotropic glutamate receptor 2
ChEMBL 280 4 4 5 -0.2 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2O)C1 10.1016/s0960-894x(01)00329-8
42610165 80830 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 435 4 0 5 5.2 N#Cc1c(-c2ccc(OC3CCOCC3)c(Cl)c2)ccn2c(CC(F)(F)F)cnc12 10.1021/jm201561r
CHEMBL2152107 80830 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 435 4 0 5 5.2 N#Cc1c(-c2ccc(OC3CCOCC3)c(Cl)c2)ccn2c(CC(F)(F)F)cnc12 10.1021/jm201561r
CHEMBL5079928 217142 None 0 Human Functional pEC50 = 5.2 5.2 - 1
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL None None None O=C1c2nc3ccccc3n2CCN1CC1CC1 10.1021/acs.jmedchem.1c00563
155559438 174963 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 198 2 0 4 1.7 N#Cc1cccc2c1nnn2CC1CC1 10.1021/acs.jmedchem.8b00161
CHEMBL4563304 174963 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 198 2 0 4 1.7 N#Cc1cccc2c1nnn2CC1CC1 10.1021/acs.jmedchem.8b00161
66785027 158430 None 0 Human Functional pEC50 = 7.2 7.2 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 356 5 1 4 4.7 Fc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4089416 158430 None 0 Human Functional pEC50 = 7.2 7.2 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 356 5 1 4 4.7 Fc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CC1 10.1021/acs.jmedchem.7b00669
CHEMBL5076356 216919 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL None None None O=C1c2nc3cccc(-c4ccccc4)c3n2CCN1CC1CC1 10.1021/acs.jmedchem.1c00563
53316862 57742 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 298 3 0 3 4.1 CCCn1ccc2cc(-c3cccnc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669381 57742 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 298 3 0 3 4.1 CCCn1ccc2cc(-c3cccnc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
53323492 57748 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 356 7 0 4 4.5 CCCn1ccc2cc(OCCCc3cccnc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669387 57748 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 356 7 0 4 4.5 CCCn1ccc2cc(OCCCc3cccnc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
53325450 57755 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 418 7 0 4 5.7 CCCn1ccc2cc(-c3ccc(OCCc4ccccc4)nc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669393 57755 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 418 7 0 4 5.7 CCCn1ccc2cc(-c3ccc(OCCc4ccccc4)nc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
46225584 202131 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 408 3 0 4 5.0 Cn1c(CN2CCC(c3ncc(C(F)(F)F)cc3Cl)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL593056 202131 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 408 3 0 4 5.0 Cn1c(CN2CCC(c3ncc(C(F)(F)F)cc3Cl)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
46226929 205070 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 366 5 0 7 2.3 CCCCn1ccc(N2CCN(c3nc(C)cc(C)n3)CC2)c(C#N)c1=O 10.1016/j.bmcl.2009.11.008
CHEMBL612133 205070 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 366 5 0 7 2.3 CCCCn1ccc(N2CCN(c3nc(C)cc(C)n3)CC2)c(C#N)c1=O 10.1016/j.bmcl.2009.11.008
68109379 157317 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 464 6 1 5 5.3 FC(F)(F)c1c(-c2ccc(CNC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
CHEMBL4076286 157317 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 464 6 1 5 5.3 FC(F)(F)c1c(-c2ccc(CNC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
24815434 202152 None 0 Human Functional pEC50 = 5.2 5.2 -5 2
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 305 3 0 3 4.0 Cn1c(CN2CCC(c3ccccc3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL593196 202152 None 0 Human Functional pEC50 = 5.2 5.2 -5 2
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 305 3 0 3 4.0 Cn1c(CN2CCC(c3ccccc3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
46225337 202433 None 0 Human Functional pEC50 = 5.2 5.2 - 1
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 375 3 0 5 3.3 Cn1c(CN2CCN(c3ccc(C(F)(F)F)cn3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL595151 202433 None 0 Human Functional pEC50 = 5.2 5.2 - 1
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 375 3 0 5 3.3 Cn1c(CN2CCN(c3ccc(C(F)(F)F)cn3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
46225335 202503 None 0 Human Functional pEC50 = 5.2 5.2 - 1
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 374 3 0 4 3.9 Cn1c(CN2CCN(c3ccc(C(F)(F)F)cc3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL595608 202503 None 0 Human Functional pEC50 = 5.2 5.2 - 1
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 374 3 0 4 3.9 Cn1c(CN2CCN(c3ccc(C(F)(F)F)cc3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
24849789 202590 None 0 Human Functional pEC50 = 5.2 5.2 - 1
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 324 3 0 4 3.0 Cn1c(CN2CCN(c3ccccc3F)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL596270 202590 None 0 Human Functional pEC50 = 5.2 5.2 - 1
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 324 3 0 4 3.0 Cn1c(CN2CCN(c3ccccc3F)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
46225569 203819 None 0 Human Functional pEC50 = 5.2 5.2 -12 2
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 373 3 0 3 5.0 Cn1c(CN2CCC(c3ccccc3C(F)(F)F)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL604467 203819 None 0 Human Functional pEC50 = 5.2 5.2 -12 2
Agonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayAgonist activity at human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 373 3 0 3 5.0 Cn1c(CN2CCC(c3ccccc3C(F)(F)F)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
44591813 184765 None 0 Human Functional pEC50 = 5.2 5.2 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 324 5 0 3 3.8 C[C@@H]1CN(Cc2ccc(-c3ccccc3CN(C)C)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL484972 184765 None 0 Human Functional pEC50 = 5.2 5.2 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 324 5 0 3 3.8 C[C@@H]1CN(Cc2ccc(-c3ccccc3CN(C)C)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
11950742 67128 None 0 Human Functional pEC50 = 5.2 5.2 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 462 11 1 7 5.5 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ncn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
CHEMBL187398 67128 None 0 Human Functional pEC50 = 5.2 5.2 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 462 11 1 7 5.5 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ncn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
70685769 74641 None 0 Human Functional pEC50 = 7.2 7.2 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 405 5 0 5 5.3 Cc1ccc(Oc2ccc(-c3ccn(CC4CC4)c(=O)c3C#N)cc2Cl)c(C)n1 10.1021/jm2016864
CHEMBL2029820 74641 None 0 Human Functional pEC50 = 7.2 7.2 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 405 5 0 5 5.3 Cc1ccc(Oc2ccc(-c3ccn(CC4CC4)c(=O)c3C#N)cc2Cl)c(C)n1 10.1021/jm2016864
155552204 174246 None 0 Human Functional pEC50 = 7.2 7.2 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 305 2 0 3 3.4 Fc1ccccc1Cn1nnc2c(Br)cccc21 10.1021/acs.jmedchem.8b00161
CHEMBL4546388 174246 None 0 Human Functional pEC50 = 7.2 7.2 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 305 2 0 3 3.4 Fc1ccccc1Cn1nnc2c(Br)cccc21 10.1021/acs.jmedchem.8b00161
71136691 143708 None 0 Human Functional pEC50 = 7.2 7.2 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 394 3 0 5 3.2 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)C3CC3)nc21 nan
CHEMBL3899706 143708 None 0 Human Functional pEC50 = 7.2 7.2 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 394 3 0 5 3.2 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)C3CC3)nc21 nan
68109605 158482 None 0 Human Functional pEC50 = 7.2 7.2 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 456 5 0 5 6.3 Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cc(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4089955 158482 None 0 Human Functional pEC50 = 7.2 7.2 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 456 5 0 5 6.3 Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cc(C)n1 10.1021/acs.jmedchem.7b00669
9815616 114864 None 4 Rat Functional pEC50 = 7.2 7.2 -2 4
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 203 2 3 3 -0.5 N[C@@]1(C(=O)O)[C@@H](F)C[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm000346k
CHEMBL334014 114864 None 4 Rat Functional pEC50 = 7.2 7.2 -2 4
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 203 2 3 3 -0.5 N[C@@]1(C(=O)O)[C@@H](F)C[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm000346k
44155538 8510 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 265 6 0 2 4.1 CCCCCCC1CN(c2cccc(F)c2)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1094134 8510 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 265 6 0 2 4.1 CCCCCCC1CN(c2cccc(F)c2)C(=O)O1 10.1016/j.bmcl.2010.03.089
44155316 8700 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 277 7 0 3 4.0 CCCCCCC1CN(c2cccc(OC)c2)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1095749 8700 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 277 7 0 3 4.0 CCCCCCC1CN(c2cccc(OC)c2)C(=O)O1 10.1016/j.bmcl.2010.03.089
44155420 8761 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 261 6 0 2 4.3 CCCCCCC1CN(c2cccc(C)c2)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1096423 8761 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 261 6 0 2 4.3 CCCCCCC1CN(c2cccc(C)c2)C(=O)O1 10.1016/j.bmcl.2010.03.089
46227790 202547 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 375 4 0 7 2.9 CCCc1cnc2c(C#N)c(N3CCN(c4nc(C)cc(C)n4)CC3)ccn12 10.1016/j.bmcl.2009.11.008
CHEMBL595966 202547 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 375 4 0 7 2.9 CCCc1cnc2c(C#N)c(N3CCN(c4nc(C)cc(C)n4)CC3)ccn12 10.1016/j.bmcl.2009.11.008
70689924 74617 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 359 6 0 5 4.6 CC(C)CCn1ccc(-c2ccc(Oc3ccccn3)cc2)c(C#N)c1=O 10.1021/jm2016864
CHEMBL2029798 74617 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 359 6 0 5 4.6 CC(C)CCn1ccc(-c2ccc(Oc3ccccn3)cc2)c(C#N)c1=O 10.1021/jm2016864
162665242 182214 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 391 5 0 4 5.3 Clc1cccc(SCCCN2CCn3c(nc4ccccc43)C2)c1Cl 10.1016/j.ejmech.2019.111881
CHEMBL4781971 182214 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 391 5 0 4 5.3 Clc1cccc(SCCCN2CCn3c(nc4ccccc43)C2)c1Cl 10.1016/j.ejmech.2019.111881
11951987 68254 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 433 12 1 6 5.4 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CCC 10.1016/j.bmcl.2005.06.017
CHEMBL191579 68254 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 433 12 1 6 5.4 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CCC 10.1016/j.bmcl.2005.06.017
46887320 8996 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 283 4 0 3 3.4 Cc1ccc(OCC2CN(c3ccccc3)C(=O)O2)cc1 10.1016/j.bmcl.2010.03.089
CHEMBL1098389 8996 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 283 4 0 3 3.4 Cc1ccc(OCC2CN(c3ccccc3)C(=O)O2)cc1 10.1016/j.bmcl.2010.03.089
118714739 114626 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 350 5 0 5 3.1 CC(C)CCn1ccc(N2CCN(c3ccccc3)CC2)c(C#N)c1=O 10.1021/jm500496m
CHEMBL3337505 114626 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 350 5 0 5 3.1 CC(C)CCn1ccc(N2CCN(c3ccccc3)CC2)c(C#N)c1=O 10.1021/jm500496m
46197778 8220 None 0 Rat Functional pEC50 = 5.2 5.2 -6 5
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate readerAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate reader
ChEMBL 237 6 4 4 -0.3 N[C@@H](CCP(=O)(O)/C=C/C(=O)O)C(=O)O 10.1021/jm901523t
CHEMBL1092243 8220 None 0 Rat Functional pEC50 = 5.2 5.2 -6 5
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate readerAgonist activity at rat mGlu2 receptor expressed in HEK293 cells assessed as increase in intracellular calcium level after 1 hr by fluorescence microplate reader
ChEMBL 237 6 4 4 -0.3 N[C@@H](CCP(=O)(O)/C=C/C(=O)O)C(=O)O 10.1021/jm901523t
11626305 66675 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 437 10 1 5 5.7 CC(C)CC(=O)c1ccc(OCCCCSc2ccncc2)c(Br)c1O 10.1016/j.bmcl.2004.09.028
CHEMBL185290 66675 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 437 10 1 5 5.7 CC(C)CC(=O)c1ccc(OCCCCSc2ccncc2)c(Br)c1O 10.1016/j.bmcl.2004.09.028
44428731 143234 None 0 Rat Functional pEC50 = 4.2 4.2 - 1
Agonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAgonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level
ChEMBL 199 4 3 5 0.2 CCCc1c(C(N)C(=O)O)cnn1O 10.1016/j.bmc.2007.02.047
CHEMBL389585 143234 None 0 Rat Functional pEC50 = 4.2 4.2 - 1
Agonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAgonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level
ChEMBL 199 4 3 5 0.2 CCCc1c(C(N)C(=O)O)cnn1O 10.1016/j.bmc.2007.02.047
11575058 65622 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 407 8 1 5 6.1 Cc1c(OCc2ccccc2Sc2ccncc2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
CHEMBL183304 65622 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 407 8 1 5 6.1 Cc1c(OCc2ccccc2Sc2ccncc2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
118714755 114641 None 0 Human Functional pEC50 = 7.2 7.2 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 369 4 0 4 3.8 N#Cc1c(N2CCC(c3ccc(F)cc3F)CC2)ccn(CC2CC2)c1=O 10.1021/jm500496m
CHEMBL3337521 114641 None 0 Human Functional pEC50 = 7.2 7.2 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 369 4 0 4 3.8 N#Cc1c(N2CCC(c3ccc(F)cc3F)CC2)ccn(CC2CC2)c1=O 10.1021/jm500496m
155550797 175224 None 0 Human Functional pEC50 = 7.2 7.2 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 356 3 0 4 4.5 Fc1ccc2c(c1)nnn2Cc1ccc(-c2ccc(Cl)cc2F)nc1 10.1021/acs.jmedchem.8b00161
CHEMBL4569581 175224 None 0 Human Functional pEC50 = 7.2 7.2 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 356 3 0 4 4.5 Fc1ccc2c(c1)nnn2Cc1ccc(-c2ccc(Cl)cc2F)nc1 10.1021/acs.jmedchem.8b00161
59599538 145133 None 0 Human Functional pEC50 = 6.2 6.2 -1 2
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 445 9 2 8 4.5 CCCc1c(OCc2ccc(Oc3ccc(-c4nn[nH]n4)cn3)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2016.11.049
CHEMBL3911282 145133 None 0 Human Functional pEC50 = 6.2 6.2 -1 2
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 445 9 2 8 4.5 CCCc1c(OCc2ccc(Oc3ccc(-c4nn[nH]n4)cn3)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2016.11.049
71136653 123470 None 0 Human Functional pEC50 = 7.2 7.2 51 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616854 123470 None 0 Human Functional pEC50 = 7.2 7.2 51 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
57459475 82683 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 331 3 0 5 3.5 CCc1nnc2c(C#N)c(N3CCC(c4ccccc4)CC3)ccn12 10.1021/jm3010724
CHEMBL2179329 82683 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 331 3 0 5 3.5 CCc1nnc2c(C#N)c(N3CCC(c4ccccc4)CC3)ccn12 10.1021/jm3010724
1393 1539 None 42 Human Functional pEC50 = 8.2 8.2 2 6
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/acs.jmedchem.7b01481
1396 1539 None 42 Human Functional pEC50 = 8.2 8.2 2 6
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/acs.jmedchem.7b01481
213056 1539 None 42 Human Functional pEC50 = 8.2 8.2 2 6
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/acs.jmedchem.7b01481
CHEMBL8759 1539 None 42 Human Functional pEC50 = 8.2 8.2 2 6
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/acs.jmedchem.7b01481
1393 1539 None 42 Human Functional pEC50 = 8.2 8.2 2 6
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/acs.jmedchem.5b01124
1396 1539 None 42 Human Functional pEC50 = 8.2 8.2 2 6
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/acs.jmedchem.5b01124
213056 1539 None 42 Human Functional pEC50 = 8.2 8.2 2 6
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/acs.jmedchem.5b01124
CHEMBL8759 1539 None 42 Human Functional pEC50 = 8.2 8.2 2 6
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/acs.jmedchem.5b01124
156817932 192183 None 0 Human Functional pEC50 = 8.1 8.1 - 1
Positive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP AssayPositive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP Assay
ChEMBL 465 4 0 5 4.1 O=C(c1cnc2c(cnn2CC2CC2)c1C(F)(F)F)N1CCN(c2ccc(F)cc2F)CC1 10.1021/acs.jmedchem.2c00593
CHEMBL5202739 192183 None 0 Human Functional pEC50 = 8.1 8.1 - 1
Positive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP AssayPositive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP Assay
ChEMBL 465 4 0 5 4.1 O=C(c1cnc2c(cnn2CC2CC2)c1C(F)(F)F)N1CCN(c2ccc(F)cc2F)CC1 10.1021/acs.jmedchem.2c00593
60096224 156636 None 0 Human Functional pEC50 = 8.1 8.1 -43 2
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 320 4 5 5 -0.4 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2O)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4068189 156636 None 0 Human Functional pEC50 = 8.1 8.1 -43 2
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 320 4 5 5 -0.4 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2O)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
71461395 83941 None 1 Human Functional pEC50 = 8.1 8.1 - 1
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 432 5 0 5 5.0 COc1c(F)ccc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm300912k
CHEMBL2206445 83941 None 1 Human Functional pEC50 = 8.1 8.1 - 1
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 432 5 0 5 5.0 COc1c(F)ccc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm300912k
23725156 61979 None 0 Rat Functional pEC50 = 8.1 8.1 - 1
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 357 3 0 3 4.7 Cn1c(CN2CCC(c3ccc(Cl)cc3F)CC2)nc2ccccc21 10.1021/jm101414h
CHEMBL1774107 61979 None 0 Rat Functional pEC50 = 8.1 8.1 - 1
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 357 3 0 3 4.7 Cn1c(CN2CCC(c3ccc(Cl)cc3F)CC2)nc2ccccc21 10.1021/jm101414h
49801370 157127 None 0 Human Functional pEC50 = 8.1 8.1 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 406 5 1 4 5.6 FC(F)(F)c1c(-c2ccc(NC3CC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
CHEMBL4073628 157127 None 0 Human Functional pEC50 = 8.1 8.1 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 406 5 1 4 5.6 FC(F)(F)c1c(-c2ccc(NC3CC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
90098428 123472 None 0 Human Functional pEC50 = 8.1 8.1 60 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 352 4 4 6 0.4 N[C@@]1(C(=O)O)C[C@H](Sc2nnc(C(F)(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616856 123472 None 0 Human Functional pEC50 = 8.1 8.1 60 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 352 4 4 6 0.4 N[C@@]1(C(=O)O)C[C@H](Sc2nnc(C(F)(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
25173616 184600 None 0 Human Functional pEC50 = 8.1 8.1 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 317 5 0 3 4.4 CC1CN(Cc2ccc(OC(C)C3CCCCC3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL484731 184600 None 0 Human Functional pEC50 = 8.1 8.1 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 317 5 0 3 4.4 CC1CN(Cc2ccc(OC(C)C3CCCCC3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
156010124 177136 None 0 Human Functional pEC50 = 8.1 8.1 - 1
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 396 5 0 5 4.7 COc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1 10.1021/acs.jmedchem.0c01058
CHEMBL4632373 177136 None 0 Human Functional pEC50 = 8.1 8.1 - 1
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 396 5 0 5 4.7 COc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1 10.1021/acs.jmedchem.0c01058
156010124 177136 None 0 Human Functional pEC50 = 8.1 8.1 - 1
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 396 5 0 5 4.7 COc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1 10.1021/acs.jmedchem.0c01058
CHEMBL4632373 177136 None 0 Human Functional pEC50 = 8.1 8.1 - 1
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 396 5 0 5 4.7 COc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1 10.1021/acs.jmedchem.0c01058
44591773 184366 None 0 Human Functional pEC50 = 7.2 7.2 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 303 3 0 2 4.0 C[C@@H]1CN(Cc2ccc(-c3ccc(F)cc3F)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL483751 184366 None 0 Human Functional pEC50 = 7.2 7.2 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 303 3 0 2 4.0 C[C@@H]1CN(Cc2ccc(-c3ccc(F)cc3F)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
162662443 182117 None 0 Human Functional pEC50 = 7.2 7.2 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 369 6 0 4 4.0 O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(Cl)cc1 10.1016/j.ejmech.2019.111881
CHEMBL4780663 182117 None 0 Human Functional pEC50 = 7.2 7.2 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 369 6 0 4 4.0 O=C1c2nc3ccccc3n2CCN1CCCCOc1ccc(Cl)cc1 10.1016/j.ejmech.2019.111881
162675793 183521 None 0 Human Functional pEC50 = 7.2 7.2 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 375 5 0 4 4.6 Clc1ccc(OCCCN2CCn3c(nc4ccccc43)C2)cc1Cl 10.1016/j.ejmech.2019.111881
CHEMBL4798495 183521 None 0 Human Functional pEC50 = 7.2 7.2 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 375 5 0 4 4.6 Clc1ccc(OCCCN2CCn3c(nc4ccccc43)C2)cc1Cl 10.1016/j.ejmech.2019.111881
155546950 173763 None 0 Human Functional pEC50 = 7.2 7.2 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 320 3 0 4 4.2 Clc1ccc(-c2ccc(Cn3nnc4ccccc43)cn2)cc1 10.1021/acs.jmedchem.8b00161
CHEMBL4534604 173763 None 0 Human Functional pEC50 = 7.2 7.2 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 320 3 0 4 4.2 Clc1ccc(-c2ccc(Cn3nnc4ccccc43)cn2)cc1 10.1021/acs.jmedchem.8b00161
155565811 175724 None 1 Human Functional pEC50 = 7.2 7.2 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 269 2 0 3 2.7 Fc1cc(Br)c2nnn(CC3CC3)c2c1 10.1021/acs.jmedchem.8b00161
CHEMBL4580525 175724 None 1 Human Functional pEC50 = 7.2 7.2 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 269 2 0 3 2.7 Fc1cc(Br)c2nnn(CC3CC3)c2c1 10.1021/acs.jmedchem.8b00161
146036861 176153 None 6 Human Functional pEC50 = 7.2 7.2 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 251 2 0 3 2.6 Brc1cccc2c1nnn2CC1CC1 10.1021/acs.jmedchem.8b00161
CHEMBL4590535 176153 None 6 Human Functional pEC50 = 7.2 7.2 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 251 2 0 3 2.6 Brc1cccc2c1nnn2CC1CC1 10.1021/acs.jmedchem.8b00161
155549028 173901 None 0 Human Functional pEC50 = 7.2 7.2 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 321 3 0 3 4.4 Fc1ccc(-c2ccc(Cn3nnc4ccccc43)cc2)c(F)c1 10.1021/acs.jmedchem.8b00161
CHEMBL4538026 173901 None 0 Human Functional pEC50 = 7.2 7.2 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 321 3 0 3 4.4 Fc1ccc(-c2ccc(Cn3nnc4ccccc43)cc2)c(F)c1 10.1021/acs.jmedchem.8b00161
71460259 80831 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 434 4 1 5 5.2 N#Cc1c(-c2ccc(NC3CCOCC3)c(Cl)c2)ccn2c(CC(F)(F)F)cnc12 10.1021/jm201561r
CHEMBL2152108 80831 None 0 Human Functional pEC50 = 6.2 6.2 - 1
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 434 4 1 5 5.2 N#Cc1c(-c2ccc(NC3CCOCC3)c(Cl)c2)ccn2c(CC(F)(F)F)cnc12 10.1021/jm201561r
44155535 8509 None 0 Human Functional pEC50 = 5.2 5.2 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 265 6 0 2 4.1 CCCCCCC1CN(c2ccccc2F)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1094133 8509 None 0 Human Functional pEC50 = 5.2 5.2 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 265 6 0 2 4.1 CCCCCCC1CN(c2ccccc2F)C(=O)O1 10.1016/j.bmcl.2010.03.089
134130007 142278 None 0 Human Functional pEC50 = 6.1 6.1 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 391 6 0 6 4.4 Clc1c(OCc2cccc(-c3cncnc3)c2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
CHEMBL3884042 142278 None 0 Human Functional pEC50 = 6.1 6.1 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assayPositive allosteric modulation of human mGlu2 receptor expressed in HEK293 cells coexpressing rat glutamate transporter assessed as inhibition of forskolin-stimulated cAMP production measured after 30 mins in presence of orthosteric antagonist LY341495 by FLIPR assay
ChEMBL 391 6 0 6 4.4 Clc1c(OCc2cccc(-c3cncnc3)c2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
44428731 143234 None 0 Rat Functional pEC50 = 4.1 4.1 - 1
Agonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAgonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level
ChEMBL 199 4 3 5 0.2 CCCc1c(C(N)C(=O)O)cnn1O 10.1016/j.bmc.2007.02.047
CHEMBL389585 143234 None 0 Rat Functional pEC50 = 4.1 4.1 - 1
Agonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAgonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level
ChEMBL 199 4 3 5 0.2 CCCc1c(C(N)C(=O)O)cnn1O 10.1016/j.bmc.2007.02.047
68107827 192593 None 0 Human Functional pEC50 = 5.1 5.1 - 1
Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay
ChEMBL 467 5 0 5 4.8 Fc1cc(Cl)ccc1N1CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1 10.1021/acs.jmedchem.2c00593
CHEMBL5208947 192593 None 0 Human Functional pEC50 = 5.1 5.1 - 1
Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay
ChEMBL 467 5 0 5 4.8 Fc1cc(Cl)ccc1N1CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1 10.1021/acs.jmedchem.2c00593
155535327 172118 None 0 Human Functional pEC50 = 6.1 6.1 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 281 3 0 4 2.6 COc1cc(Br)c2nnn(CC3CC3)c2c1 10.1021/acs.jmedchem.8b00161
CHEMBL4471540 172118 None 0 Human Functional pEC50 = 6.1 6.1 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 281 3 0 4 2.6 COc1cc(Br)c2nnn(CC3CC3)c2c1 10.1021/acs.jmedchem.8b00161
71136654 123475 None 0 Human Functional pEC50 = 7.1 7.1 3 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 326 5 4 6 0.5 CC(C)c1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
CHEMBL3616859 123475 None 0 Human Functional pEC50 = 7.1 7.1 3 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as inhibition of forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 326 5 4 6 0.5 CC(C)c1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
57459636 82664 None 0 Human Functional pEC50 = 7.1 7.1 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 357 4 0 5 3.9 N#Cc1c(N2CCC(c3ccccc3)CC2)ccn2c(CC3CC3)nnc12 10.1021/jm3010724
CHEMBL2179309 82664 None 0 Human Functional pEC50 = 7.1 7.1 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 357 4 0 5 3.9 N#Cc1c(N2CCC(c3ccccc3)CC2)ccn2c(CC3CC3)nnc12 10.1021/jm3010724
66786816 158448 None 0 Human Functional pEC50 = 7.1 7.1 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 426 6 0 6 5.5 CCOCc1nnc2c(Cl)c(-c3ccc(Oc4ccc(C)nc4C)c(F)c3)ccn12 10.1021/acs.jmedchem.7b00669
CHEMBL4089612 158448 None 0 Human Functional pEC50 = 7.1 7.1 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 426 6 0 6 5.5 CCOCc1nnc2c(Cl)c(-c3ccc(Oc4ccc(C)nc4C)c(F)c3)ccn12 10.1021/acs.jmedchem.7b00669
162675603 183402 None 0 Human Functional pEC50 = 6.1 6.1 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 389 6 0 4 4.8 FC(F)(F)Oc1ccc(CCCCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
CHEMBL4796990 183402 None 0 Human Functional pEC50 = 6.1 6.1 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 389 6 0 4 4.8 FC(F)(F)Oc1ccc(CCCCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
54580322 61994 None 0 Rat Functional pEC50 = 6.1 6.1 - 1
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 402 3 0 4 5.0 Cn1c(CN2CC[C@@H](c3ccc(C(F)(F)F)cc3)C(C)(C)C2)nc2ncccc21 10.1021/jm101414h
CHEMBL1774226 61994 None 0 Rat Functional pEC50 = 6.1 6.1 - 1
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 402 3 0 4 5.0 Cn1c(CN2CC[C@@H](c3ccc(C(F)(F)F)cc3)C(C)(C)C2)nc2ncccc21 10.1021/jm101414h
25173691 189116 None 0 Human Functional pEC50 = 7.1 7.1 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 317 5 0 3 4.4 CC(Oc1ccc(CN2CCCOC2=O)cc1)C1CCCCC1 10.1016/j.bmcl.2009.03.032
CHEMBL508821 189116 None 0 Human Functional pEC50 = 7.1 7.1 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 317 5 0 3 4.4 CC(Oc1ccc(CN2CCCOC2=O)cc1)C1CCCCC1 10.1016/j.bmcl.2009.03.032
162643509 181775 None 0 Human Functional pEC50 = 5.1 5.1 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 295 3 0 3 3.2 Fc1ccccc1CCN1CCn2c(nc3ccccc32)C1 10.1016/j.ejmech.2019.111881
CHEMBL4776355 181775 None 0 Human Functional pEC50 = 5.1 5.1 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 295 3 0 3 3.2 Fc1ccccc1CCN1CCn2c(nc3ccccc32)C1 10.1016/j.ejmech.2019.111881
11951986 124386 None 0 Human Functional pEC50 = 6.1 6.1 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 445 12 1 6 5.4 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC1CC1 10.1016/j.bmcl.2005.06.017
CHEMBL363531 124386 None 0 Human Functional pEC50 = 6.1 6.1 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 445 12 1 6 5.4 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC1CC1 10.1016/j.bmcl.2005.06.017
44591792 193479 None 0 Human Functional pEC50 = 5.1 5.1 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 268 3 0 3 3.1 C[C@@H]1CN(Cc2ccc(-c3cccnc3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL525075 193479 None 0 Human Functional pEC50 = 5.1 5.1 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 268 3 0 3 3.1 C[C@@H]1CN(Cc2ccc(-c3cccnc3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
168298153 192848 None 0 Human Functional pEC50 = 6.1 6.1 - 1
Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding
ChEMBL 421 6 0 4 5.8 FC(F)(F)c1c(-c2ccc(OCC3CC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.2c00969
CHEMBL5220484 192848 None 0 Human Functional pEC50 = 6.1 6.1 - 1
Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding
ChEMBL 421 6 0 4 5.8 FC(F)(F)c1c(-c2ccc(OCC3CC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.2c00969
25173778 185019 None 0 Human Functional pEC50 = 7.1 7.1 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 301 3 0 2 4.3 C[C@@H]1CN(Cc2ccc(-c3ccc(Cl)cc3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL485329 185019 None 0 Human Functional pEC50 = 7.1 7.1 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 301 3 0 2 4.3 C[C@@H]1CN(Cc2ccc(-c3ccc(Cl)cc3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
51357936 61997 None 0 Human Functional pEC50 = 7.1 7.1 -3 2
Positive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 418 4 0 5 4.6 COc1cc(C(F)(F)F)ccc1[C@@H]1CCN(Cc2nc3ncccc3n2C)C[C@@H]1C 10.1021/jm101414h
CHEMBL1774231 61997 None 0 Human Functional pEC50 = 7.1 7.1 -3 2
Positive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of human mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 418 4 0 5 4.6 COc1cc(C(F)(F)F)ccc1[C@@H]1CCN(Cc2nc3ncccc3n2C)C[C@@H]1C 10.1021/jm101414h
44155747 8699 None 0 Human Functional pEC50 = 6.1 6.1 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 272 6 0 3 3.9 CCCCCCC1CN(c2ccc(C#N)cc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1095746 8699 None 0 Human Functional pEC50 = 6.1 6.1 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 272 6 0 3 3.9 CCCCCCC1CN(c2ccc(C#N)cc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
11951991 133991 None 0 Human Functional pEC50 = 6.1 6.1 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 447 12 1 6 5.7 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)C 10.1016/j.bmcl.2005.06.017
CHEMBL371578 133991 None 0 Human Functional pEC50 = 6.1 6.1 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 447 12 1 6 5.7 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)C 10.1016/j.bmcl.2005.06.017
66786131 157258 None 0 Human Functional pEC50 = 7.1 7.1 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 402 5 0 5 5.6 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4075417 157258 None 0 Human Functional pEC50 = 7.1 7.1 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 402 5 0 5 5.6 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
11510036 66249 None 0 Human Functional pEC50 = 6.1 6.1 - 1
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 421 9 1 5 6.2 Cc1c(OCc2ccc(CSc3ccncc3)cc2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
CHEMBL184531 66249 None 0 Human Functional pEC50 = 6.1 6.1 - 1
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 421 9 1 5 6.2 Cc1c(OCc2ccc(CSc3ccncc3)cc2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
11952169 67551 None 0 Human Functional pEC50 = 6.1 6.1 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 459 10 1 6 5.8 CCCc1c(OC/C=C/COc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
CHEMBL189623 67551 None 0 Human Functional pEC50 = 6.1 6.1 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 459 10 1 6 5.8 CCCc1c(OC/C=C/COc2ccc(-c3nn[nH]n3)cc2)ccc2c1ccn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
24815976 202215 None 0 Rat Functional pEC50 = 7.1 7.1 5 2
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 373 3 0 3 5.0 Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2ccccc21 10.1021/jm101414h
CHEMBL593745 202215 None 0 Rat Functional pEC50 = 7.1 7.1 5 2
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 373 3 0 3 5.0 Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2ccccc21 10.1021/jm101414h
46887418 9001 None 0 Human Functional pEC50 = 6.1 6.1 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 337 4 0 3 4.1 O=C1OC(COc2ccc(C(F)(F)F)cc2)CN1c1ccccc1 10.1016/j.bmcl.2010.03.089
CHEMBL1098406 9001 None 0 Human Functional pEC50 = 6.1 6.1 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 337 4 0 3 4.1 O=C1OC(COc2ccc(C(F)(F)F)cc2)CN1c1ccccc1 10.1016/j.bmcl.2010.03.089
22368592 8754 None 0 Human Functional pEC50 = 5.1 5.1 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 263 6 1 3 3.7 CCCCCCC1CN(c2ccc(O)cc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1096318 8754 None 0 Human Functional pEC50 = 5.1 5.1 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 263 6 1 3 3.7 CCCCCCC1CN(c2ccc(O)cc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
51354014 61998 None 0 Rat Functional pEC50 = 6.1 6.1 - 1
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 418 4 0 5 4.6 COc1cc(C(F)(F)F)ccc1[C@H]1CCN(Cc2nc3ncccc3n2C)C[C@H]1C 10.1021/jm101414h
CHEMBL1774232 61998 None 0 Rat Functional pEC50 = 6.1 6.1 - 1
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 418 4 0 5 4.6 COc1cc(C(F)(F)F)ccc1[C@H]1CCN(Cc2nc3ncccc3n2C)C[C@H]1C 10.1021/jm101414h
11952347 67455 None 0 Human Functional pEC50 = 6.1 6.1 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 463 11 1 7 5.8 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c(CC(C)(C)C)noc12 10.1016/j.bmcl.2005.06.017
CHEMBL188977 67455 None 0 Human Functional pEC50 = 6.1 6.1 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 463 11 1 7 5.8 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c(CC(C)(C)C)noc12 10.1016/j.bmcl.2005.06.017
155518831 170462 None 0 Human Functional pEC50 = 7.1 7.1 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 353 3 0 3 5.5 Clc1ccc(-c2ccc(Cn3nnc4ccccc43)cc2)c(Cl)c1 10.1021/acs.jmedchem.8b00161
CHEMBL4447550 170462 None 0 Human Functional pEC50 = 7.1 7.1 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 353 3 0 3 5.5 Clc1ccc(-c2ccc(Cn3nnc4ccccc43)cc2)c(Cl)c1 10.1021/acs.jmedchem.8b00161
CHEMBL5093066 217895 None 0 Human Functional pEC50 = 7.1 7.1 - 1
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL None None None Cn1c(CN2CCN(c3ncc(C(F)(F)F)cc3Cl)CC2)nc2ncccc21 10.1021/acs.jmedchem.1c00563
156019582 178116 None 0 Human Functional pEC50 = 7.1 7.1 2 2
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 382 4 1 5 4.4 Oc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1 10.1021/acs.jmedchem.0c01058
CHEMBL4646555 178116 None 0 Human Functional pEC50 = 7.1 7.1 2 2
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 382 4 1 5 4.4 Oc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1 10.1021/acs.jmedchem.0c01058
59234231 2143 None 4 Human Functional pEC50 = 7.1 7.1 -1 2
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.7b00669
6330 2143 None 4 Human Functional pEC50 = 7.1 7.1 -1 2
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.7b00669
6331 2143 None 4 Human Functional pEC50 = 7.1 7.1 -1 2
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.7b00669
CHEMBL3337510 2143 None 4 Human Functional pEC50 = 7.1 7.1 -1 2
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.7b00669
156019582 178116 None 0 Human Functional pEC50 = 7.1 7.1 2 2
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 382 4 1 5 4.4 Oc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1 10.1021/acs.jmedchem.0c01058
CHEMBL4646555 178116 None 0 Human Functional pEC50 = 7.1 7.1 2 2
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 382 4 1 5 4.4 Oc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1 10.1021/acs.jmedchem.0c01058
67060124 166873 None 0 Rat Functional pEC50 = 7.1 7.1 - 1
Positive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis
ChEMBL 388 4 0 5 3.8 O=c1ccn2c(n1)O[C@H](COc1ccc(-c3cccc(C(F)(F)F)c3)cc1)C2 10.1016/j.bmcl.2018.08.022
CHEMBL4283963 166873 None 0 Rat Functional pEC50 = 7.1 7.1 - 1
Positive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysisPositive allosteric modulation of recombinant rat Gi-coupled mGluR2 expressed in HEK293 Flp-in-T-REx cells with Galpha16 assessed as increase in glutamate-induced forskolin-mediated cAMP accumulation after 5 mins by fluorescence analysis
ChEMBL 388 4 0 5 3.8 O=c1ccn2c(n1)O[C@H](COc1ccc(-c3cccc(C(F)(F)F)c3)cc1)C2 10.1016/j.bmcl.2018.08.022
46887272 8693 None 1 Human Functional pEC50 = 6.1 6.1 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 233 5 0 2 3.6 CCCCCC1CN(c2ccccc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1095702 8693 None 1 Human Functional pEC50 = 6.1 6.1 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 233 5 0 2 3.6 CCCCCC1CN(c2ccccc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
44155540 8729 None 0 Human Functional pEC50 = 6.1 6.1 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 265 6 0 2 4.1 CCCCCCC1CN(c2ccc(F)cc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
CHEMBL1095970 8729 None 0 Human Functional pEC50 = 6.1 6.1 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 265 6 0 2 4.1 CCCCCCC1CN(c2ccc(F)cc2)C(=O)O1 10.1016/j.bmcl.2010.03.089
53322148 57747 None 0 Human Functional pEC50 = 6.1 6.1 - 1
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 342 6 0 4 4.1 CCCn1ccc2cc(OCCc3cccnc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669386 57747 None 0 Human Functional pEC50 = 6.1 6.1 - 1
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 342 6 0 4 4.1 CCCn1ccc2cc(OCCc3cccnc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
53326075 57750 None 0 Human Functional pEC50 = 6.1 6.1 - 1
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 383 4 0 5 4.0 CCCn1ccc2cc(-c3ccc(N4CCOCC4)nc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669389 57750 None 0 Human Functional pEC50 = 6.1 6.1 - 1
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 383 4 0 5 4.0 CCCn1ccc2cc(-c3ccc(N4CCOCC4)nc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
53322149 57752 None 0 Human Functional pEC50 = 6.1 6.1 - 1
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 328 4 0 4 4.1 CCCn1ccc2cc(-c3ccc(OC)nc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669390 57752 None 0 Human Functional pEC50 = 6.1 6.1 - 1
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 328 4 0 4 4.1 CCCn1ccc2cc(-c3ccc(OC)nc3)cc(Cl)c2c1=O 10.1016/j.bmcl.2010.12.048
53324152 57763 None 0 Human Functional pEC50 = 5.1 5.1 - 1
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 264 3 0 3 3.5 CCCn1ccc2cc(-c3cccnc3)ccc2c1=O 10.1016/j.bmcl.2010.12.048
CHEMBL1669402 57763 None 0 Human Functional pEC50 = 5.1 5.1 - 1
Agonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assayAgonist activity at human mGluR2 expressed in CHO cells at by [S35]GTPgammaS binding assay
ChEMBL 264 3 0 3 3.5 CCCn1ccc2cc(-c3cccnc3)ccc2c1=O 10.1016/j.bmcl.2010.12.048
10176324 114891 None 1 Rat Functional pEC50 = 8.1 8.1 4 4
Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells
ChEMBL 173 3 3 3 -0.6 C[C@H]1[C@H](C(=O)O)[C@H]1[C@H](N)C(=O)O 10.1021/jm030967o
CHEMBL334160 114891 None 1 Rat Functional pEC50 = 8.1 8.1 4 4
Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells
ChEMBL 173 3 3 3 -0.6 C[C@H]1[C@H](C(=O)O)[C@H]1[C@H](N)C(=O)O 10.1021/jm030967o
57459488 83937 None 0 Human Functional pEC50 = 8.1 8.1 - 1
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 414 5 0 5 4.9 COc1ccc(F)cc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm300912k
CHEMBL2206441 83937 None 0 Human Functional pEC50 = 8.1 8.1 - 1
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 414 5 0 5 4.9 COc1ccc(F)cc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm300912k
68107827 192593 None 0 Human Functional pEC50 = 8.1 8.1 - 1
Positive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP AssayPositive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP Assay
ChEMBL 467 5 0 5 4.8 Fc1cc(Cl)ccc1N1CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1 10.1021/acs.jmedchem.2c00593
CHEMBL5208947 192593 None 0 Human Functional pEC50 = 8.1 8.1 - 1
Positive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP AssayPositive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP Assay
ChEMBL 467 5 0 5 4.8 Fc1cc(Cl)ccc1N1CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1 10.1021/acs.jmedchem.2c00593
60096178 156973 None 0 Human Functional pEC50 = 8.1 8.1 -10 2
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 338 4 4 4 0.6 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2cccc(Cl)c2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4071962 156973 None 0 Human Functional pEC50 = 8.1 8.1 -10 2
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 338 4 4 4 0.6 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2cccc(Cl)c2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
156018381 178027 None 0 Human Functional pEC50 = 8.1 8.1 - 1
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 440 8 0 6 4.7 COCCOc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1 10.1021/acs.jmedchem.0c01058
CHEMBL4645305 178027 None 0 Human Functional pEC50 = 8.1 8.1 - 1
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 440 8 0 6 4.7 COCCOc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1 10.1021/acs.jmedchem.0c01058
70209638 157701 None 0 Human Functional pEC50 = 8.1 8.1 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 456 5 0 5 6.3 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4080973 157701 None 0 Human Functional pEC50 = 8.1 8.1 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 456 5 0 5 6.3 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
156018381 178027 None 0 Human Functional pEC50 = 8.1 8.1 - 1
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 440 8 0 6 4.7 COCCOc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1 10.1021/acs.jmedchem.0c01058
CHEMBL4645305 178027 None 0 Human Functional pEC50 = 8.1 8.1 - 1
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 440 8 0 6 4.7 COCCOc1ccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)cc1 10.1021/acs.jmedchem.0c01058
146036869 175841 None 8 Human Functional pEC50 = 7.1 7.1 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 287 2 0 3 3.2 Brc1cccc2c1nnn2Cc1ccccc1 10.1021/acs.jmedchem.8b00161
CHEMBL4583006 175841 None 8 Human Functional pEC50 = 7.1 7.1 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 287 2 0 3 3.2 Brc1cccc2c1nnn2Cc1ccccc1 10.1021/acs.jmedchem.8b00161
162657401 181212 None 3 Human Functional pEC50 = 6.1 6.1 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 355 3 0 3 3.9 Brc1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
CHEMBL4760211 181212 None 3 Human Functional pEC50 = 6.1 6.1 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 355 3 0 3 3.9 Brc1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1 10.1016/j.ejmech.2019.111881
162657401 181212 None 3 Human Functional pEC50 = 6.1 6.1 - 1
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL 355 3 0 3 3.9 Brc1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1 10.1021/acs.jmedchem.1c00563
CHEMBL4760211 181212 None 3 Human Functional pEC50 = 6.1 6.1 - 1
Positive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysisPositive allosteric modulator activity at human mGlu2 receptor expressed in rat Chem-1 cells assessed as cytosolic Ca2+ ion concentration measured after 30 mins by fluorometric analysis
ChEMBL 355 3 0 3 3.9 Brc1ccc(CCN2CCn3c(nc4ccccc43)C2)cc1 10.1021/acs.jmedchem.1c00563
118714747 114633 None 0 Human Functional pEC50 = 7.1 7.1 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 351 4 0 4 3.7 N#Cc1c(N2CCC(c3ccccc3F)CC2)ccn(CC2CC2)c1=O 10.1021/jm500496m
CHEMBL3337513 114633 None 0 Human Functional pEC50 = 7.1 7.1 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 351 4 0 4 3.7 N#Cc1c(N2CCC(c3ccccc3F)CC2)ccn(CC2CC2)c1=O 10.1021/jm500496m
51354020 62002 None 0 Rat Functional pEC50 = 6.1 6.1 -23 2
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 422 4 0 5 4.6 C[C@@H]1CN(Cc2nc3ncccc3n2C)CC[C@@H]1c1ccc(OC(F)(F)F)cc1F 10.1021/jm101414h
CHEMBL1774236 62002 None 0 Rat Functional pEC50 = 6.1 6.1 -23 2
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 422 4 0 5 4.6 C[C@@H]1CN(Cc2nc3ncccc3n2C)CC[C@@H]1c1ccc(OC(F)(F)F)cc1F 10.1021/jm101414h
11495483 66688 None 0 Human Functional pEC50 = 6.1 6.1 - 1
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 421 9 1 5 6.2 Cc1c(OCc2cccc(CSc3ccncc3)c2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
CHEMBL185392 66688 None 0 Human Functional pEC50 = 6.1 6.1 - 1
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 421 9 1 5 6.2 Cc1c(OCc2cccc(CSc3ccncc3)c2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
49822116 147080 None 14 Human Functional pEC50 = 7.1 7.1 - 1
Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay
ChEMBL 451 5 0 5 4.3 Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.2c00593
CHEMBL3926416 147080 None 14 Human Functional pEC50 = 7.1 7.1 - 1
Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay
ChEMBL 451 5 0 5 4.3 Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.2c00593
46830123 1073 None 0 Human Functional pEC50 = 7.1 7.1 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 350 4 0 4 4.3 N#Cc1cccc(c1)N1C[C@H](OC1=O)COc1ccc(cc1)C(C)(C)C 10.1016/j.bmcl.2010.03.089
6321 1073 None 0 Human Functional pEC50 = 7.1 7.1 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 350 4 0 4 4.3 N#Cc1cccc(c1)N1C[C@H](OC1=O)COc1ccc(cc1)C(C)(C)C 10.1016/j.bmcl.2010.03.089
CHEMBL1094763 1073 None 0 Human Functional pEC50 = 7.1 7.1 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 350 4 0 4 4.3 N#Cc1cccc(c1)N1C[C@H](OC1=O)COc1ccc(cc1)C(C)(C)C 10.1016/j.bmcl.2010.03.089
44450470 96139 None 1 Rat Functional pEC50 = 4.1 4.1 -1 2
Activity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulationActivity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulation
ChEMBL 160 2 3 4 -0.9 N[C@H](C(=O)O)[C@H]1CC(O)=NO1 10.1021/jm701394a
CHEMBL260122 96139 None 1 Rat Functional pEC50 = 4.1 4.1 -1 2
Activity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulationActivity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulation
ChEMBL 160 2 3 4 -0.9 N[C@H](C(=O)O)[C@H]1CC(O)=NO1 10.1021/jm701394a
70685765 74629 None 0 Human Functional pEC50 = 6.1 6.1 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 357 5 0 5 4.3 Cc1cc(Oc2ccc(-c3ccn(CC4CC4)c(=O)c3C#N)cc2)ccn1 10.1021/jm2016864
CHEMBL2029808 74629 None 0 Human Functional pEC50 = 6.1 6.1 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 357 5 0 5 4.3 Cc1cc(Oc2ccc(-c3ccn(CC4CC4)c(=O)c3C#N)cc2)ccn1 10.1021/jm2016864
156817932 192183 None 0 Human Functional pEC50 = 7.1 7.1 - 1
Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay
ChEMBL 465 4 0 5 4.1 O=C(c1cnc2c(cnn2CC2CC2)c1C(F)(F)F)N1CCN(c2ccc(F)cc2F)CC1 10.1021/acs.jmedchem.2c00593
CHEMBL5202739 192183 None 0 Human Functional pEC50 = 7.1 7.1 - 1
Agonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP AssayAgonist activity at mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells by luciferase based GloSensor cAMP Assay
ChEMBL 465 4 0 5 4.1 O=C(c1cnc2c(cnn2CC2CC2)c1C(F)(F)F)N1CCN(c2ccc(F)cc2F)CC1 10.1021/acs.jmedchem.2c00593
25173697 172789 None 0 Human Functional pEC50 = 7.1 7.1 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 285 3 0 2 3.8 C[C@@H]1CN(Cc2ccc(-c3ccc(F)cc3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
CHEMBL450076 172789 None 0 Human Functional pEC50 = 7.1 7.1 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 285 3 0 2 3.8 C[C@@H]1CN(Cc2ccc(-c3ccc(F)cc3)cc2)C(=O)O1 10.1016/j.bmcl.2009.03.032
46887417 8946 None 0 Human Functional pEC50 = 6.1 6.1 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 303 4 0 3 3.7 O=C1OC(COc2cccc(Cl)c2)CN1c1ccccc1 10.1016/j.bmcl.2010.03.089
CHEMBL1097984 8946 None 0 Human Functional pEC50 = 6.1 6.1 - 1
Allosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assayAllosteric modulation of human mGluR2 expressed in CHO dhfr cells co-expressing G-protein Galpha16 assessed as potentiation of glutamate-induced calcium flux by FLIPR assay
ChEMBL 303 4 0 3 3.7 O=C1OC(COc2cccc(Cl)c2)CN1c1ccccc1 10.1016/j.bmcl.2010.03.089
44450470 96139 None 1 Rat Functional pEC50 = 4.1 4.1 -1 2
Activity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulationActivity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulation
ChEMBL 160 2 3 4 -0.9 N[C@H](C(=O)O)[C@H]1CC(O)=NO1 10.1021/jm701394a
CHEMBL260122 96139 None 1 Rat Functional pEC50 = 4.1 4.1 -1 2
Activity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulationActivity at rat cloned mGluR2 expressed in CHO cells assessed as effect on cAMP accumulation
ChEMBL 160 2 3 4 -0.9 N[C@H](C(=O)O)[C@H]1CC(O)=NO1 10.1021/jm701394a
58081135 80843 None 0 Human Functional pEC50 = 7.1 7.1 - 1
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 383 2 1 2 5.9 FC(F)(F)Cc1cnc2c(Cl)c(-c3cc(Cl)c4[nH]ccc4c3)ccn12 10.1021/jm201561r
CHEMBL2152121 80843 None 0 Human Functional pEC50 = 7.1 7.1 - 1
Agonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysisAgonist activity at human mGlu 2 expressed in CHO cells assessed as [35S]GTPgammaS binding by liquid scintillation analysis
ChEMBL 383 2 1 2 5.9 FC(F)(F)Cc1cnc2c(Cl)c(-c3cc(Cl)c4[nH]ccc4c3)ccn12 10.1021/jm201561r
1310 2315 None 61 Human Functional pEC50 = 5.1 5.1 -389 17
Agonistic activity at mGlu2 receptor expressed in CHO cellsAgonistic activity at mGlu2 receptor expressed in CHO cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm9602569
1369 2315 None 61 Human Functional pEC50 = 5.1 5.1 -389 17
Agonistic activity at mGlu2 receptor expressed in CHO cellsAgonistic activity at mGlu2 receptor expressed in CHO cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm9602569
33032 2315 None 61 Human Functional pEC50 = 5.1 5.1 -389 17
Agonistic activity at mGlu2 receptor expressed in CHO cellsAgonistic activity at mGlu2 receptor expressed in CHO cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm9602569
44272391 2315 None 61 Human Functional pEC50 = 5.1 5.1 -389 17
Agonistic activity at mGlu2 receptor expressed in CHO cellsAgonistic activity at mGlu2 receptor expressed in CHO cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm9602569
88747398 2315 None 61 Human Functional pEC50 = 5.1 5.1 -389 17
Agonistic activity at mGlu2 receptor expressed in CHO cellsAgonistic activity at mGlu2 receptor expressed in CHO cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm9602569
CHEMBL575060 2315 None 61 Human Functional pEC50 = 5.1 5.1 -389 17
Agonistic activity at mGlu2 receptor expressed in CHO cellsAgonistic activity at mGlu2 receptor expressed in CHO cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm9602569
DB00142 2315 None 61 Human Functional pEC50 = 5.1 5.1 -389 17
Agonistic activity at mGlu2 receptor expressed in CHO cellsAgonistic activity at mGlu2 receptor expressed in CHO cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm9602569
46226952 202307 None 0 Human Functional pEC50 = 6.1 6.1 - 1
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 387 3 0 7 2.4 N#Cc1c(N2CCN(c3ncccn3)CC2)ccn2c(CC(F)(F)F)cnc12 10.1016/j.bmcl.2009.11.008
CHEMBL594386 202307 None 0 Human Functional pEC50 = 6.1 6.1 - 1
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 387 3 0 7 2.4 N#Cc1c(N2CCN(c3ncccn3)CC2)ccn2c(CC(F)(F)F)cnc12 10.1016/j.bmcl.2009.11.008
66612837 74606 None 0 Human Functional pEC50 = 5.1 5.1 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 266 4 0 3 3.4 CC(C)CCn1ccc(-c2ccccc2)c(C#N)c1=O 10.1021/jm2016864
CHEMBL2029786 74606 None 0 Human Functional pEC50 = 5.1 5.1 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 266 4 0 3 3.4 CC(C)CCn1ccc(-c2ccccc2)c(C#N)c1=O 10.1021/jm2016864
66612837 74606 None 0 Human Functional pEC50 = 5.1 5.1 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 266 4 0 3 3.4 CC(C)CCn1ccc(-c2ccccc2)c(C#N)c1=O 10.1021/jm500496m
CHEMBL2029786 74606 None 0 Human Functional pEC50 = 5.1 5.1 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 266 4 0 3 3.4 CC(C)CCn1ccc(-c2ccccc2)c(C#N)c1=O 10.1021/jm500496m
155553087 174208 None 0 Human Functional pEC50 = 7.1 7.1 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 356 3 0 4 4.5 Fc1ccc2nnn(Cc3ccc(-c4ccc(Cl)cc4F)nc3)c2c1 10.1021/acs.jmedchem.8b00161
CHEMBL4545027 174208 None 0 Human Functional pEC50 = 7.1 7.1 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 356 3 0 4 4.5 Fc1ccc2nnn(Cc3ccc(-c4ccc(Cl)cc4F)nc3)c2c1 10.1021/acs.jmedchem.8b00161
51356569 61974 None 2 Rat Functional pEC50 = 7.1 7.1 10 3
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 335 4 0 4 4.0 COc1ccccc1C1CCN(Cc2nc3ccccc3n2C)CC1 10.1021/jm101414h
CHEMBL1774101 61974 None 2 Rat Functional pEC50 = 7.1 7.1 10 3
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 335 4 0 4 4.0 COc1ccccc1C1CCN(Cc2nc3ccccc3n2C)CC1 10.1021/jm101414h
168299005 192863 None 0 Human Functional pEC50 = 7.1 7.1 - 1
Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding
ChEMBL 372 7 0 6 3.8 CCCCn1cnc2c(-c3ccc(OCC4CC4)c(Cl)c3)cnn2c1=O 10.1021/acs.jmedchem.2c00969
CHEMBL5221091 192863 None 0 Human Functional pEC50 = 7.1 7.1 - 1
Positive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS bindingPositive allosteric modulator activity at mGluR2 receptor (unknown origin) assessed as glutamate-induced [35S]GTPgammaS binding
ChEMBL 372 7 0 6 3.8 CCCCn1cnc2c(-c3ccc(OCC4CC4)c(Cl)c3)cnn2c1=O 10.1021/acs.jmedchem.2c00969
66785182 157270 None 0 Human Functional pEC50 = 7.1 7.1 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 434 6 0 5 6.2 Fc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1Oc1ccnc(C2CC2)c1 10.1021/acs.jmedchem.7b00669
CHEMBL4075593 157270 None 0 Human Functional pEC50 = 7.1 7.1 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 434 6 0 5 6.2 Fc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1Oc1ccnc(C2CC2)c1 10.1021/acs.jmedchem.7b00669
59599545 147247 None 0 Human Functional pEC50 = 7.1 7.1 3 2
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 437 7 2 8 4.2 CC(=O)c1ccc(OCc2cccc(Oc3cc(-c4nn[nH]n4)ccn3)c2)c(Cl)c1O 10.1016/j.bmcl.2016.11.049
CHEMBL3927834 147247 None 0 Human Functional pEC50 = 7.1 7.1 3 2
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in hamster AV12 cells expressing EAAT1 assessed as potentiation of glutamate-induced intracellular calcium level measured after 24 to 48 hrs by FLIPR assay
ChEMBL 437 7 2 8 4.2 CC(=O)c1ccc(OCc2cccc(Oc3cc(-c4nn[nH]n4)ccn3)c2)c(Cl)c1O 10.1016/j.bmcl.2016.11.049
71136655 123468 None 0 Human Functional pEC50 = 7.1 7.1 12 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 326 5 4 6 0.5 CC(C)c1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
CHEMBL3616852 123468 None 0 Human Functional pEC50 = 7.1 7.1 12 2
Agonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assayAgonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as stimulation of Ca2+ mobilization after 1 hr by FLIPR assay
ChEMBL 326 5 4 6 0.5 CC(C)c1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
51356569 61974 None 2 Human Functional pEC50 = 6.1 6.1 -10 3
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 335 4 0 4 4.0 COc1ccccc1C1CCN(Cc2nc3ccccc3n2C)CC1 10.1016/j.ejmech.2019.111881
CHEMBL1774101 61974 None 2 Human Functional pEC50 = 6.1 6.1 -10 3
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 335 4 0 4 4.0 COc1ccccc1C1CCN(Cc2nc3ccccc3n2C)CC1 10.1016/j.ejmech.2019.111881
118714736 114622 None 0 Human Functional pEC50 = 6.1 6.1 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 321 4 0 4 3.3 CC(C)CCn1ccc(N2CCc3ccccc3C2)c(C#N)c1=O 10.1021/jm500496m
CHEMBL3337501 114622 None 0 Human Functional pEC50 = 6.1 6.1 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 321 4 0 4 3.3 CC(C)CCn1ccc(N2CCc3ccccc3C2)c(C#N)c1=O 10.1021/jm500496m
11951447 67505 None 0 Human Functional pEC50 = 6.1 6.1 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 495 9 1 6 7.2 CCCc1c(OCc2ccc(Oc3ccc(-c4nn[nH]n4)cc3)cc2)ccc2c1ccn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
CHEMBL189290 67505 None 0 Human Functional pEC50 = 6.1 6.1 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 495 9 1 6 7.2 CCCc1c(OCc2ccc(Oc3ccc(-c4nn[nH]n4)cc3)cc2)ccc2c1ccn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
44591712 184418 None 0 Human Functional pEC50 = 7.1 7.1 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 318 5 0 4 3.8 CC(Oc1ccc(CN2C[C@@H](C)OC2=O)cn1)C1CCCCC1 10.1016/j.bmcl.2009.03.032
CHEMBL484178 184418 None 0 Human Functional pEC50 = 7.1 7.1 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 318 5 0 4 3.8 CC(Oc1ccc(CN2C[C@@H](C)OC2=O)cn1)C1CCCCC1 10.1016/j.bmcl.2009.03.032
118714749 114635 None 0 Human Functional pEC50 = 7.1 7.1 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 351 4 0 4 3.7 N#Cc1c(N2CCC(c3ccc(F)cc3)CC2)ccn(CC2CC2)c1=O 10.1021/jm500496m
CHEMBL3337515 114635 None 0 Human Functional pEC50 = 7.1 7.1 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 351 4 0 4 3.7 N#Cc1c(N2CCC(c3ccc(F)cc3)CC2)ccn(CC2CC2)c1=O 10.1021/jm500496m
44392645 65265 None 0 Human Functional pEC50 = 6.1 6.1 - 1
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 407 8 1 5 6.1 Cc1c(OCc2cccc(Sc3ccncc3)c2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
CHEMBL182715 65265 None 0 Human Functional pEC50 = 6.1 6.1 - 1
Binding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assayBinding affinity towards human metabotropic glutamate receptor 2 determined by [35S]GTP gamma S binding assay
ChEMBL 407 8 1 5 6.1 Cc1c(OCc2cccc(Sc3ccncc3)c2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.09.028
54584258 61972 None 0 Rat Functional pEC50 = 6.1 6.1 - 1
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 456 5 0 6 3.3 COc1ccccc1N1CCN(Cc2c(Br)c(=O)n(-c3ccccc3)n2C)CC1 10.1021/jm101414h
CHEMBL1774099 61972 None 0 Rat Functional pEC50 = 6.1 6.1 - 1
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 456 5 0 6 3.3 COc1ccccc1N1CCN(Cc2c(Br)c(=O)n(-c3ccccc3)n2C)CC1 10.1021/jm101414h
137634033 156732 None 0 Human Functional pEC50 = 6.1 6.1 -1 2
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 332 6 4 4 0.2 N[C@@]1(C(=O)O)C[C@H](NC(=O)CCc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4069251 156732 None 0 Human Functional pEC50 = 6.1 6.1 -1 2
Agonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in HEK cells assessed as inhibition of forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 332 6 4 4 0.2 N[C@@]1(C(=O)O)C[C@H](NC(=O)CCc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
51357937 61999 None 0 Rat Functional pEC50 = 8.1 8.1 -2 2
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 406 3 0 4 4.8 C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(C(F)(F)F)cc1F 10.1021/jm101414h
CHEMBL1774233 61999 None 0 Rat Functional pEC50 = 8.1 8.1 -2 2
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 406 3 0 4 4.8 C[C@H]1CN(Cc2nc3ncccc3n2C)CC[C@H]1c1ccc(C(F)(F)F)cc1F 10.1021/jm101414h
156018305 177939 None 0 Human Functional pEC50 = 8.1 8.1 89 2
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 440 8 0 6 4.7 COCCOc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4643961 177939 None 0 Human Functional pEC50 = 8.1 8.1 89 2
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 440 8 0 6 4.7 COCCOc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/acs.jmedchem.0c01058
156018305 177939 None 0 Human Functional pEC50 = 8.0 8.0 89 2
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 440 8 0 6 4.7 COCCOc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4643961 177939 None 0 Human Functional pEC50 = 8.0 8.0 89 2
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 440 8 0 6 4.7 COCCOc1ccccc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/acs.jmedchem.0c01058
69093344 83942 None 0 Human Functional pEC50 = 8.0 8.0 - 1
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 432 5 0 5 5.0 COc1ccc(F)c(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm300912k
CHEMBL2206446 83942 None 0 Human Functional pEC50 = 8.0 8.0 - 1
Agonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation countingAgonist activity at human mGLuR2 expressed in CHO cell membrane assessed as [32S]GTPgammaS after 30 mins by scintillation counting
ChEMBL 432 5 0 5 5.0 COc1ccc(F)c(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm300912k
66786493 159773 None 0 Human Functional pEC50 = 8.0 8.0 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 464 5 2 5 5.7 O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4104081 159773 None 0 Human Functional pEC50 = 8.0 8.0 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 464 5 2 5 5.7 O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
156020355 178133 None 0 Human Functional pEC50 = 8 8.0 104 2
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 396 5 0 5 4.7 COc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1 10.1021/acs.jmedchem.0c01058
CHEMBL4646835 178133 None 0 Human Functional pEC50 = 8 8.0 104 2
Positive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assayPositive modulator activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr in presence of EC20 glutamate by Fluo-4 dye based fluorescence assay
ChEMBL 396 5 0 5 4.7 COc1cccc(C2CCN(c3ccn4c(CC5CC5)nnc4c3Cl)CC2)c1 10.1021/acs.jmedchem.0c01058
6604805 205145 None 1 Rat Functional pEC50 = 7.1 7.1 - 1
Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells
ChEMBL 195 3 3 3 -0.6 N[C@H](C(=O)O)[C@@H]1[C@@H](C(=O)O)C1(F)F 10.1021/jm030967o
CHEMBL61605 205145 None 1 Rat Functional pEC50 = 7.1 7.1 - 1
Metabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cellsMetabotropic glutamate receptor 2 agonist activity against forskolin stimulated c-AMP formation in rat non neuronal cells
ChEMBL 195 3 3 3 -0.6 N[C@H](C(=O)O)[C@@H]1[C@@H](C(=O)O)C1(F)F 10.1021/jm030967o
162659759 181417 None 0 Human Functional pEC50 = 7.1 7.1 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 359 5 0 4 4.3 Fc1ccc(SCCCN2CCn3c(nc4ccccc43)C2)cc1F 10.1016/j.ejmech.2019.111881
CHEMBL4762556 181417 None 0 Human Functional pEC50 = 7.1 7.1 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 359 5 0 4 4.3 Fc1ccc(SCCCN2CCn3c(nc4ccccc43)C2)cc1F 10.1016/j.ejmech.2019.111881
162662067 181515 None 0 Human Functional pEC50 = 7.1 7.1 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 349 6 0 4 3.7 Cc1ccccc1OCCCCN1CCn2c(nc3ccccc32)C1=O 10.1016/j.ejmech.2019.111881
CHEMBL4763686 181515 None 0 Human Functional pEC50 = 7.1 7.1 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 349 6 0 4 3.7 Cc1ccccc1OCCCCN1CCn2c(nc3ccccc32)C1=O 10.1016/j.ejmech.2019.111881
162662384 182158 None 0 Human Functional pEC50 = 7.1 7.1 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 389 5 0 4 4.3 O=C1c2nc3ccccc3n2CCN1CCCOc1ccc(Cl)c(Cl)c1 10.1016/j.ejmech.2019.111881
CHEMBL4781222 182158 None 0 Human Functional pEC50 = 7.1 7.1 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 389 5 0 4 4.3 O=C1c2nc3ccccc3n2CCN1CCCOc1ccc(Cl)c(Cl)c1 10.1016/j.ejmech.2019.111881
155518472 170408 None 0 Human Functional pEC50 = 7.1 7.1 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 207 2 0 3 2.5 Clc1cccc2c1nnn2CC1CC1 10.1021/acs.jmedchem.8b00161
CHEMBL4446625 170408 None 0 Human Functional pEC50 = 7.1 7.1 - 1
Positive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assayPositive allosteric modulation of human mGluR2 expressed in human Chem1 cells assessed as increase in glutamate-induced intracellular calcium influx preincubated for 30 mins followed by glutamate addition by calcium-5 dye based fluorometric assay
ChEMBL 207 2 0 3 2.5 Clc1cccc2c1nnn2CC1CC1 10.1021/acs.jmedchem.8b00161
156017237 177866 None 0 Human Functional pEC50 = 6.1 6.1 1 2
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 853 21 0 11 8.5 COc1c(OCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4642761 177866 None 0 Human Functional pEC50 = 6.1 6.1 1 2
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 853 21 0 11 8.5 COc1c(OCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
156017237 177866 None 0 Human Functional pEC50 = 6.0 6.0 1 2
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 853 21 0 11 8.5 COc1c(OCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
CHEMBL4642761 177866 None 0 Human Functional pEC50 = 6.0 6.0 1 2
Agonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assayAgonist activity at human mGlu2 receptor expressed in HEK293 cells co-expressing Gqo5 assessed as increase in intracellular Ca2+ mobilization incubated for 1 hr by Fluo-4 dye based fluorescence assay
ChEMBL 853 21 0 11 8.5 COc1c(OCCOCCOCCOc2ccc(C3CCN(c4ccn5c(CC6CC6)nnc5c4Cl)CC3)cc2)cccc1C(=O)C1CCN(CCc2ccc(F)cc2)CC1 10.1021/acs.jmedchem.0c01058
156817945 190593 None 0 Human Functional pEC50 = 6.0 6.0 - 1
Positive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP AssayPositive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP Assay
ChEMBL 451 5 0 5 4.3 Fc1ccc(N2CCN(Cc3cc(C(F)(F)F)cn4c(CC5CC5)nnc34)CC2)c(F)c1 10.1021/acs.jmedchem.2c00593
CHEMBL5179002 190593 None 0 Human Functional pEC50 = 6.0 6.0 - 1
Positive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP AssayPositive allosteric modulation of mGlu2 receptor (unknown origin) expressed in human Flp-In-T-REx-293 cells in presence of L-glutamate by luciferase based GloSensor cAMP Assay
ChEMBL 451 5 0 5 4.3 Fc1ccc(N2CCN(Cc3cc(C(F)(F)F)cn4c(CC5CC5)nnc34)CC2)c(F)c1 10.1021/acs.jmedchem.2c00593
3954 664 None 44 Human Functional pEC50 = 7.0 7.0 6 3
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 454 6 1 3 6.8 Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1 10.1021/acs.jmedchem.7b00669
9868580 664 None 44 Human Functional pEC50 = 7.0 7.0 6 3
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 454 6 1 3 6.8 Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1 10.1021/acs.jmedchem.7b00669
CHEMBL593013 664 None 44 Human Functional pEC50 = 7.0 7.0 6 3
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 454 6 1 3 6.8 Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1 10.1021/acs.jmedchem.7b00669
66784262 158323 None 0 Human Functional pEC50 = 7.0 7.0 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 392 5 1 4 5.3 CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1F 10.1021/acs.jmedchem.7b00669
CHEMBL4088239 158323 None 0 Human Functional pEC50 = 7.0 7.0 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 392 5 1 4 5.3 CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1F 10.1021/acs.jmedchem.7b00669
70694132 74637 None 0 Human Functional pEC50 = 6.0 6.0 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 393 6 0 5 5.3 CCCCn1ccc(-c2ccc(Oc3ccnc(C)c3)cc2Cl)c(C#N)c1=O 10.1021/jm2016864
CHEMBL2029816 74637 None 0 Human Functional pEC50 = 6.0 6.0 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation countingPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting
ChEMBL 393 6 0 5 5.3 CCCCn1ccc(-c2ccc(Oc3ccnc(C)c3)cc2Cl)c(C#N)c1=O 10.1021/jm2016864
11655609 165996 None 0 Human Functional pEC50 = 6.0 6.0 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 expressed in HEK293 cells done for 1 hr at 30 degree CEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 expressed in HEK293 cells done for 1 hr at 30 degree C
ChEMBL 463 11 1 8 4.8 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1nnn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
CHEMBL424998 165996 None 0 Human Functional pEC50 = 6.0 6.0 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 expressed in HEK293 cells done for 1 hr at 30 degree CEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 expressed in HEK293 cells done for 1 hr at 30 degree C
ChEMBL 463 11 1 8 4.8 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1nnn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
1395 2528 None 14 Rat Functional pEC50 = 7.0 7.0 -7 4
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 217 2 3 4 -1.2 O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O 10.1021/jm000346k
9837317 2528 None 14 Rat Functional pEC50 = 7.0 7.0 -7 4
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 217 2 3 4 -1.2 O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O 10.1021/jm000346k
CHEMBL121053 2528 None 14 Rat Functional pEC50 = 7.0 7.0 -7 4
Agonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formationAgonist activity against Metabotropic glutamate receptor 2 expressed in CHO cells was evaluated by measuring forskolin-induced cyclic AMP formation
ChEMBL 217 2 3 4 -1.2 O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O 10.1021/jm000346k
57459512 82673 None 0 Human Functional pEC50 = 6.0 6.0 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 367 4 0 5 3.7 Clc1c(N2CCN(c3ccccc3)CC2)ccn2c(CC3CC3)nnc12 10.1021/jm3010724
CHEMBL2179318 82673 None 0 Human Functional pEC50 = 6.0 6.0 - 1
Positive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assayPositive allosteric modulator activity at human mGlu2R expressed in CHO cells incubated for 30 mins by [35S]GTPgammaS binding assay
ChEMBL 367 4 0 5 3.7 Clc1c(N2CCN(c3ccccc3)CC2)ccn2c(CC3CC3)nnc12 10.1021/jm3010724
118714742 114629 None 0 Human Functional pEC50 = 7.0 7.0 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 335 5 0 4 3.9 CCCCn1ccc(N2CCC(c3ccccc3)CC2)c(C#N)c1=O 10.1021/jm500496m
CHEMBL3337508 114629 None 0 Human Functional pEC50 = 7.0 7.0 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 335 5 0 4 3.9 CCCCn1ccc(N2CCC(c3ccccc3)CC2)c(C#N)c1=O 10.1021/jm500496m
71117214 151196 None 0 Human Functional pEC50 = 6.0 6.0 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 446 4 0 8 2.1 Cn1cnc(S(=O)(=O)N2CCCC(c3ccc4c(n3)n(C)c(=O)n4CC(C)(C)C)C2)c1 nan
CHEMBL3959189 151196 None 0 Human Functional pEC50 = 6.0 6.0 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 446 4 0 8 2.1 Cn1cnc(S(=O)(=O)N2CCCC(c3ccc4c(n3)n(C)c(=O)n4CC(C)(C)C)C2)c1 nan
44591770 192427 None 0 Human Functional pEC50 = 7.0 7.0 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 311 5 0 3 4.1 CCOc1ccc(-c2ccc(CN3C[C@@H](C)OC3=O)cc2)cc1 10.1016/j.bmcl.2009.03.032
CHEMBL520639 192427 None 0 Human Functional pEC50 = 7.0 7.0 - 1
Agonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamateAgonist activity at mGluR2 expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 311 5 0 3 4.1 CCOc1ccc(-c2ccc(CN3C[C@@H](C)OC3=O)cc2)cc1 10.1016/j.bmcl.2009.03.032
68109333 159486 None 0 Human Functional pEC50 = 7.0 7.0 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 459 4 1 5 5.5 O[C@H]1CC[C@@H](Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4100691 159486 None 0 Human Functional pEC50 = 7.0 7.0 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting methodPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes assessed as increase in glutamate-induced [35S]GTPgammaS binding preincubated for 30 mins followed by [35S]GTPgammaS addition measured after 30 mins by Topcount scintillation counting method
ChEMBL 459 4 1 5 5.5 O[C@H]1CC[C@@H](Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
162649465 180171 None 0 Human Functional pEC50 = 6.0 6.0 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 391 5 0 3 5.0 Fc1cc(C(F)(F)F)ccc1CCCCN1CCn2c(nc3ccccc32)C1 10.1016/j.ejmech.2019.111881
CHEMBL4747874 180171 None 0 Human Functional pEC50 = 6.0 6.0 - 1
Positive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assayPositive allosteric modulation of human mGlu2 receptor stably expressed in human Chem-1 cells assessed as potentiation of glutamate-induced intracellular calcium level preincubated for 30 mins followed by glutamate addition by fluorescence assay
ChEMBL 391 5 0 3 5.0 Fc1cc(C(F)(F)F)ccc1CCCCN1CCn2c(nc3ccccc32)C1 10.1016/j.ejmech.2019.111881
46226930 204374 None 0 Human Functional pEC50 = 6.0 6.0 - 1
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 345 4 0 5 3.5 CCCc1cnc2c(C#N)c(N3CCN(c4ccccc4)CC3)ccn12 10.1016/j.bmcl.2009.11.008
CHEMBL607518 204374 None 0 Human Functional pEC50 = 6.0 6.0 - 1
Allosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assayAllosteric modulation of human mGluR2 expressed in CHO cells by [35S]GTPgammaS binding assay
ChEMBL 345 4 0 5 3.5 CCCc1cnc2c(C#N)c(N3CCN(c4ccccc4)CC3)ccn12 10.1016/j.bmcl.2009.11.008
118714754 114640 None 0 Human Functional pEC50 = 7.0 7.0 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 363 5 0 5 3.5 COc1ccc(C2CCN(c3ccn(CC4CC4)c(=O)c3C#N)CC2)cc1 10.1021/jm500496m
CHEMBL3337520 114640 None 0 Human Functional pEC50 = 7.0 7.0 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 minsPositive allosteric modulation of human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins
ChEMBL 363 5 0 5 3.5 COc1ccc(C2CCN(c3ccn(CC4CC4)c(=O)c3C#N)CC2)cc1 10.1021/jm500496m
11950553 67316 None 0 Human Functional pEC50 = 6.0 6.0 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 462 11 1 7 5.5 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1cnn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
CHEMBL188286 67316 None 0 Human Functional pEC50 = 6.0 6.0 - 1
Effective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hrEffective concentration for stimulation of [35S]GTP-gamma-S, binding to human metabotropic glutamate receptor 2 incubated at 30 degree C for 1 hr
ChEMBL 462 11 1 7 5.5 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc2c1cnn2CC(C)(C)C 10.1016/j.bmcl.2005.06.017
71117402 150519 None 0 Human Functional pEC50 = 6.0 6.0 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 532 5 1 6 5.8 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3CCC(C)(C)C(NC(=O)c4ccc(OC(F)(F)F)cc4)C3)nc21 nan
CHEMBL3953950 150519 None 0 Human Functional pEC50 = 6.0 6.0 - 1
Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).Fluorescence Laser Imaging Plate Reader (FLIPR) Based Assay: The compounds of the present invention may be tested in a fluorescence laser imaging plate reader (FLIPR) based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr-cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with dose responses of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity. The potentiation response is monitored after a subsequent addition of an EC20 concentration of glutamate (900 nM).
ChEMBL 532 5 1 6 5.8 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3CCC(C)(C)C(NC(=O)c4ccc(OC(F)(F)F)cc4)C3)nc21 nan
51354017 62000 None 0 Rat Functional pEC50 = 6 6.0 - 1
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 406 3 0 4 4.8 C[C@@H]1CN(Cc2nc3ncccc3n2C)CC[C@@H]1c1ccc(C(F)(F)F)cc1F 10.1021/jm101414h
CHEMBL1774234 62000 None 0 Rat Functional pEC50 = 6 6.0 - 1
Positive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assayPositive allosteric modulation of rat mGluR2 expressed in HEK293 cells co-expressing Galpha15 G protein assessed as increase in glutamate-induced intracellular calcium release by FLIPR assay
ChEMBL 406 3 0 4 4.8 C[C@@H]1CN(Cc2nc3ncccc3n2C)CC[C@@H]1c1ccc(C(F)(F)F)cc1F 10.1021/jm101414h
131636309 160139 None 0 Human Functional pIC50 = 9.0 9.0 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 445 4 0 5 5.6 CCOc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)(F)F nan
CHEMBL4108184 160139 None 0 Human Functional pIC50 = 9.0 9.0 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 445 4 0 5 5.6 CCOc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)(F)F nan
131636462 160263 None 0 Human Functional pIC50 = 8.8 8.8 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 409 5 0 5 4.8 CCOc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)cc1C nan
CHEMBL4109246 160263 None 0 Human Functional pIC50 = 8.8 8.8 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 409 5 0 5 4.8 CCOc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)cc1C nan
131636310 160640 None 0 Human Functional pIC50 = 8.8 8.8 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 431 4 0 5 5.3 CCOc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)(F)F nan
CHEMBL4112479 160640 None 0 Human Functional pIC50 = 8.8 8.8 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 431 4 0 5 5.3 CCOc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)(F)F nan
131636389 160200 None 0 Human Functional pIC50 = 8.7 8.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 441 5 0 5 5.3 Cc1cc(-c2nc(-c3ccc(OC4CC4)c(Cl)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
CHEMBL4108743 160200 None 0 Human Functional pIC50 = 8.7 8.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 441 5 0 5 5.3 Cc1cc(-c2nc(-c3ccc(OC4CC4)c(Cl)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
131636463 160404 None 0 Human Functional pIC50 = 8.7 8.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 423 5 0 5 5.2 Cc1cc(-c2nc(-c3ccc(OC(C)C)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
CHEMBL4110543 160404 None 0 Human Functional pIC50 = 8.7 8.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 423 5 0 5 5.2 Cc1cc(-c2nc(-c3ccc(OC(C)C)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
78319942 160274 None 0 Human Functional pIC50 = 8.7 8.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 3 0 5 5.1 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4109319 160274 None 0 Human Functional pIC50 = 8.7 8.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 3 0 5 5.1 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCO[C@H](C)C3)ccn1 nan
131636453 160664 None 0 Human Functional pIC50 = 8.7 8.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 431 5 0 5 5.3 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(CF)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4112624 160664 None 0 Human Functional pIC50 = 8.7 8.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 431 5 0 5 5.3 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(CF)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
11484819 56322 None 0 Human Functional pIC50 = 8 8.0 -2 2
Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 347 2 1 3 4.9 O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(Cl)cc2N1 10.1016/j.bmcl.2010.09.125
CHEMBL1629863 56322 None 0 Human Functional pIC50 = 8 8.0 -2 2
Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 347 2 1 3 4.9 O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(Cl)cc2N1 10.1016/j.bmcl.2010.09.125
44450479 96316 None 0 Rat Functional pIC50 = 8 8.0 - 1
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 398 3 1 4 4.9 CCc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2008.02.076
CHEMBL261050 96316 None 0 Rat Functional pIC50 = 8 8.0 - 1
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 398 3 1 4 4.9 CCc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2008.02.076
9909080 155372 None 0 Rat Functional pIC50 = 8 8.0 - 1
Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 402 2 1 4 4.7 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C#Cc3ccccc3)cc2N1 10.1016/j.bmcl.2007.12.005
CHEMBL402886 155372 None 0 Rat Functional pIC50 = 8 8.0 - 1
Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 402 2 1 4 4.7 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C#Cc3ccccc3)cc2N1 10.1016/j.bmcl.2007.12.005
22317744 56303 None 0 Rat Functional pIC50 = 8 8.0 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 425 3 1 4 5.5 COc1ccc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cn1 10.1016/j.bmcl.2010.09.125
CHEMBL1629844 56303 None 0 Rat Functional pIC50 = 8 8.0 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 425 3 1 4 5.5 COc1ccc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cn1 10.1016/j.bmcl.2010.09.125
22317767 56306 None 0 Rat Functional pIC50 = 8 8.0 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 437 3 1 3 6.7 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(C(C)C)nc3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1629847 56306 None 0 Rat Functional pIC50 = 8 8.0 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 437 3 1 3 6.7 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(C(C)C)nc3)c1)=N2 10.1016/j.bmcl.2010.09.125
11235624 56321 None 0 Rat Functional pIC50 = 8 8.0 -1 3
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 425 4 1 4 5.6 CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncc3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1629862 56321 None 0 Rat Functional pIC50 = 8 8.0 -1 3
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 425 4 1 4 5.6 CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncc3)c1)=N2 10.1016/j.bmcl.2010.09.125
22317431 56429 None 0 Rat Functional pIC50 = 8 8.0 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 437 3 1 3 6.7 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C(C)C)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631864 56429 None 0 Rat Functional pIC50 = 8 8.0 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 437 3 1 3 6.7 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C(C)C)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
78324632 160347 None 0 Human Functional pIC50 = 8 8.0 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 397 3 0 5 4.9 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1Cl nan
CHEMBL4110016 160347 None 0 Human Functional pIC50 = 8 8.0 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 397 3 0 5 4.9 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1Cl nan
78320556 160751 None 0 Human Functional pIC50 = 8 8.0 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 415 4 0 5 4.8 COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)cc1Cl nan
CHEMBL4113304 160751 None 0 Human Functional pIC50 = 8 8.0 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 415 4 0 5 4.8 COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)cc1Cl nan
131636370 159972 None 0 Human Functional pIC50 = 8.0 8.0 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 3 0 5 5.2 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4106787 159972 None 0 Human Functional pIC50 = 8.0 8.0 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 3 0 5 5.2 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
131636447 160837 None 0 Human Functional pIC50 = 8.0 8.0 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 5 0 5 5.3 Cc1cc(-c2nc(-c3ccc(C)c(OCC4CC4)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4113943 160837 None 0 Human Functional pIC50 = 8.0 8.0 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 5 0 5 5.3 Cc1cc(-c2nc(-c3ccc(C)c(OCC4CC4)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
131636434 151462 None 0 Human Functional pIC50 = 8.0 8.0 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 391 5 0 5 4.8 CCOc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1CC nan
CHEMBL3961419 151462 None 0 Human Functional pIC50 = 8.0 8.0 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 391 5 0 5 4.8 CCOc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1CC nan
131636342 142980 None 0 Human Functional pIC50 = 8.0 8.0 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 3 0 5 4.7 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCOCC3)ccn1 nan
CHEMBL3893630 142980 None 0 Human Functional pIC50 = 8.0 8.0 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 3 0 5 4.7 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCOCC3)ccn1 nan
76318479 106159 None 0 Human Functional pIC50 = 7 7.0 - 1
Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis
ChEMBL 446 6 1 5 5.1 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(OCCCF)c(C(F)(F)F)cc2N1 10.1039/C3MD00110E
CHEMBL3133886 106159 None 0 Human Functional pIC50 = 7 7.0 - 1
Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis
ChEMBL 446 6 1 5 5.1 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(OCCCF)c(C(F)(F)F)cc2N1 10.1039/C3MD00110E
131636402 160518 None 0 Human Functional pIC50 = 7 7.0 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 451 4 1 6 4.4 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](C)C3)cc(CO)n1 nan
CHEMBL4111387 160518 None 0 Human Functional pIC50 = 7 7.0 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 451 4 1 6 4.4 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](C)C3)cc(CO)n1 nan
10778385 78770 None 0 Human Functional pIC50 = 6 6.0 -1 2
Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2
ChEMBL 269 6 3 4 1.2 NC(CCc1ccsc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970497w
CHEMBL2112581 78770 None 0 Human Functional pIC50 = 6 6.0 -1 2
Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2
ChEMBL 269 6 3 4 1.2 NC(CCc1ccsc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970497w
10826383 78773 None 0 Human Functional pIC50 = 6 6.0 -1 2
Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2
ChEMBL 277 7 3 3 1.5 NC(CCCc1ccccc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970497w
CHEMBL2112584 78773 None 0 Human Functional pIC50 = 6 6.0 -1 2
Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2
ChEMBL 277 7 3 3 1.5 NC(CCCc1ccccc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970497w
44348769 16788 None 0 Human Functional pIC50 = 6 6.0 -3 2
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 279 6 4 4 0.8 N[C@@](CCc1cccc(O)c1)(C(=O)O)C1C[C@@H]1C(=O)O 10.1021/jm970498o
CHEMBL124483 16788 None 0 Human Functional pIC50 = 6 6.0 -3 2
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 279 6 4 4 0.8 N[C@@](CCc1cccc(O)c1)(C(=O)O)C1C[C@@H]1C(=O)O 10.1021/jm970498o
49858118 1110 None 0 Human Functional pIC50 = 6 6.0 10 2
Negative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assayNegative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assay
ChEMBL 324 3 2 5 2.7 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)OC 10.1021/jm101069m
6224 1110 None 0 Human Functional pIC50 = 6 6.0 10 2
Negative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assayNegative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assay
ChEMBL 324 3 2 5 2.7 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)OC 10.1021/jm101069m
CHEMBL1630807 1110 None 0 Human Functional pIC50 = 6 6.0 10 2
Negative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assayNegative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assay
ChEMBL 324 3 2 5 2.7 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)OC 10.1021/jm101069m
11269030 56320 None 0 Rat Functional pIC50 = 7 7.0 -1 3
Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 381 2 1 3 5.2 O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(C(F)(F)F)cc2N1 10.1016/j.bmcl.2010.09.125
CHEMBL1629861 56320 None 0 Rat Functional pIC50 = 7 7.0 -1 3
Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 381 2 1 3 5.2 O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(C(F)(F)F)cc2N1 10.1016/j.bmcl.2010.09.125
155550334 174401 None 0 Rat Functional pIC50 = 7.0 7.0 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 449 5 1 6 3.8 NC(=O)c1cc(-c2ccc(F)cc2F)n2nc(COc3ccnc(C(F)(F)F)c3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4550009 174401 None 0 Rat Functional pIC50 = 7.0 7.0 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 449 5 1 6 3.8 NC(=O)c1cc(-c2ccc(F)cc2F)n2nc(COc3ccnc(C(F)(F)F)c3)cc2n1 10.1021/acs.jmedchem.8b01266
155550334 174401 None 0 Rat Functional pIC50 = 7.0 7.0 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 449 5 1 6 3.8 NC(=O)c1cc(-c2ccc(F)cc2F)n2nc(COc3ccnc(C(F)(F)F)c3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4550009 174401 None 0 Rat Functional pIC50 = 7.0 7.0 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 449 5 1 6 3.8 NC(=O)c1cc(-c2ccc(F)cc2F)n2nc(COc3ccnc(C(F)(F)F)c3)cc2n1 10.1021/acs.jmedchem.8b01266
131636325 160782 None 0 Human Functional pIC50 = 7.0 7.0 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 451 5 0 6 4.7 Cc1cc(-c2nc(-c3ccc(F)c(OCC4(C)COC4)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4113523 160782 None 0 Human Functional pIC50 = 7.0 7.0 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 451 5 0 6 4.7 Cc1cc(-c2nc(-c3ccc(F)c(OCC4(C)COC4)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
155559601 174959 None 0 Rat Functional pIC50 = 6.0 6.0 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 405 4 1 4 4.4 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCC(F)(F)CC3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4563183 174959 None 0 Rat Functional pIC50 = 6.0 6.0 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 405 4 1 4 4.4 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCC(F)(F)CC3)cc2n1 10.1021/acs.jmedchem.8b01266
155566989 175981 None 0 Rat Functional pIC50 = 6.0 6.0 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 361 5 1 5 2.8 NC(=O)c1cc(-c2ccc(F)cc2)n2nc(CCc3ccncc3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4586203 175981 None 0 Rat Functional pIC50 = 6.0 6.0 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 361 5 1 5 2.8 NC(=O)c1cc(-c2ccc(F)cc2)n2nc(CCc3ccncc3)cc2n1 10.1021/acs.jmedchem.8b01266
155559601 174959 None 0 Rat Functional pIC50 = 6.0 6.0 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 405 4 1 4 4.4 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCC(F)(F)CC3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4563183 174959 None 0 Rat Functional pIC50 = 6.0 6.0 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 405 4 1 4 4.4 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCC(F)(F)CC3)cc2n1 10.1021/acs.jmedchem.8b01266
155566989 175981 None 0 Rat Functional pIC50 = 6.0 6.0 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 361 5 1 5 2.8 NC(=O)c1cc(-c2ccc(F)cc2)n2nc(CCc3ccncc3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4586203 175981 None 0 Rat Functional pIC50 = 6.0 6.0 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 361 5 1 5 2.8 NC(=O)c1cc(-c2ccc(F)cc2)n2nc(CCc3ccncc3)cc2n1 10.1021/acs.jmedchem.8b01266
172452146 195796 None 0 Human Functional pIC50 = 7.0 7.0 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 377 5 1 6 1.9 CCn1cc(-c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)cn1 10.1021/acsmedchemlett.3c00210
CHEMBL5410897 195796 None 0 Human Functional pIC50 = 7.0 7.0 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 377 5 1 6 1.9 CCn1cc(-c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)cn1 10.1021/acsmedchemlett.3c00210
131636415 159979 None 0 Human Functional pIC50 = 7.0 7.0 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 463 7 1 7 3.9 COc1cc(-c2nc(-c3cc(C)nc(CO)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)F nan
CHEMBL4106864 159979 None 0 Human Functional pIC50 = 7.0 7.0 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 463 7 1 7 3.9 COc1cc(-c2nc(-c3cc(C)nc(CO)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)F nan
9845873 160893 None 0 Rat Functional pIC50 = 8.0 8.0 - 1
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 436 2 2 5 4.6 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL411440 160893 None 0 Rat Functional pIC50 = 8.0 8.0 - 1
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 436 2 2 5 4.6 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2008.02.076
9845873 160893 None 0 Rat Functional pIC50 = 8.0 8.0 - 1
Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 436 2 2 5 4.6 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2007.12.005
CHEMBL411440 160893 None 0 Rat Functional pIC50 = 8.0 8.0 - 1
Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 436 2 2 5 4.6 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2007.12.005
22224657 96225 None 0 Rat Functional pIC50 = 8.0 8.0 2 2
Antagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK currentAntagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK current
ChEMBL 396 3 1 4 5.1 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccccc3F)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL260636 96225 None 0 Rat Functional pIC50 = 8.0 8.0 2 2
Antagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK currentAntagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK current
ChEMBL 396 3 1 4 5.1 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccccc3F)cc2N1 10.1016/j.bmcl.2008.02.076
9952648 96361 None 0 Rat Functional pIC50 = 8.0 8.0 1 2
Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 397 3 1 5 4.5 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1 10.1016/j.bmcl.2010.09.125
CHEMBL261288 96361 None 0 Rat Functional pIC50 = 8.0 8.0 1 2
Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 397 3 1 5 4.5 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1 10.1016/j.bmcl.2010.09.125
11474913 56423 None 0 Rat Functional pIC50 = 8.0 8.0 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 395 2 1 3 5.5 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncc3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631858 56423 None 0 Rat Functional pIC50 = 8.0 8.0 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 395 2 1 3 5.5 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncc3)c1)=N2 10.1016/j.bmcl.2010.09.125
9845873 160893 None 0 Rat Functional pIC50 = 8.0 8.0 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 436 2 2 5 4.6 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2010.09.125
CHEMBL411440 160893 None 0 Rat Functional pIC50 = 8.0 8.0 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 436 2 2 5 4.6 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2010.09.125
89554734 160255 None 0 Human Functional pIC50 = 8.0 8.0 676 2
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 419 4 1 6 2.5 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCO[C@@H](C(F)(F)F)C4)ccc23)cn1 10.1021/acsmedchemlett.3c00210
CHEMBL4109210 160255 None 0 Human Functional pIC50 = 8.0 8.0 676 2
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 419 4 1 6 2.5 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCO[C@@H](C(F)(F)F)C4)ccc23)cn1 10.1021/acsmedchemlett.3c00210
172462270 196707 None 0 Human Functional pIC50 = 8.0 8.0 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 428 5 1 6 3.6 CC(c1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1)c1cnn(CC(F)(F)F)c1 10.1021/acsmedchemlett.3c00210
CHEMBL5430371 196707 None 0 Human Functional pIC50 = 8.0 8.0 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 428 5 1 6 3.6 CC(c1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1)c1cnn(CC(F)(F)F)c1 10.1021/acsmedchemlett.3c00210
90354590 145769 None 0 Human Functional pIC50 = 7.9 7.9 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 443 5 0 5 5.5 Cc1cc(-c2nc(-c3ccc(OCc4ccccc4)c(F)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3916087 145769 None 0 Human Functional pIC50 = 7.9 7.9 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 443 5 0 5 5.5 Cc1cc(-c2nc(-c3ccc(OCc4ccccc4)c(F)c3)n3c2CCOCC3)cc(C)n1 nan
90354676 160493 None 0 Human Functional pIC50 = 7.9 7.9 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 415 4 0 5 4.8 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1Cl nan
CHEMBL4111258 160493 None 0 Human Functional pIC50 = 7.9 7.9 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 415 4 0 5 4.8 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1Cl nan
131636304 160705 None 0 Human Functional pIC50 = 7.9 7.9 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 411 4 0 5 5.2 CC[C@@H]1Cn2c(-c3ccc(Cl)c(OC)c3)nc(-c3cc(C)nc(C)c3)c2CCO1 nan
CHEMBL4112952 160705 None 0 Human Functional pIC50 = 7.9 7.9 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 411 4 0 5 5.2 CC[C@@H]1Cn2c(-c3ccc(Cl)c(OC)c3)nc(-c3cc(C)nc(C)c3)c2CCO1 nan
131636458 160605 None 0 Human Functional pIC50 = 7.9 7.9 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 429 5 0 5 5.2 Cc1cc(-c2nc(-c3ccc(OCCF)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4112214 160605 None 0 Human Functional pIC50 = 7.9 7.9 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 429 5 0 5 5.2 Cc1cc(-c2nc(-c3ccc(OCCF)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
10515174 78762 None 0 Human Functional pIC50 = 6.0 6.0 1 2
Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2
ChEMBL 255 5 3 3 1.5 NC(CC1CCCCC1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970497w
CHEMBL2112574 78762 None 0 Human Functional pIC50 = 6.0 6.0 1 2
Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2
ChEMBL 255 5 3 3 1.5 NC(CC1CCCCC1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970497w
44272296 66213 None 0 Rat Functional pIC50 = 5.0 5.0 - 1
Antagonistic activity against Metabotropic glutamate receptor 2 was determinedAntagonistic activity against Metabotropic glutamate receptor 2 was determined
ChEMBL 245 4 4 3 0.4 C[C@H](Nc1ccc(P(=O)(O)O)cc1)C(=O)O 10.1016/S0960-894X(97)00177-7
CHEMBL18439 66213 None 0 Rat Functional pIC50 = 5.0 5.0 - 1
Antagonistic activity against Metabotropic glutamate receptor 2 was determinedAntagonistic activity against Metabotropic glutamate receptor 2 was determined
ChEMBL 245 4 4 3 0.4 C[C@H](Nc1ccc(P(=O)(O)O)cc1)C(=O)O 10.1016/S0960-894X(97)00177-7
90643971 112064 None 0 Rat Functional pIC50 = 6.0 6.0 -1 2
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 386 2 0 5 4.6 Cn1c(=O)c2ccc(-c3cccnc3)cc2n2nc(-c3ccc(Cl)cc3)cc12 10.1016/j.bmcl.2014.04.051
CHEMBL3288667 112064 None 0 Rat Functional pIC50 = 6.0 6.0 -1 2
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 386 2 0 5 4.6 Cn1c(=O)c2ccc(-c3cccnc3)cc2n2nc(-c3ccc(Cl)cc3)cc12 10.1016/j.bmcl.2014.04.051
134138062 147588 None 0 Human Functional pIC50 = 6.0 6.0 -1 2
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 374 5 4 5 0.9 N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1OCc1ccc(Cl)c(Cl)c1 10.1016/j.bmcl.2016.10.067
CHEMBL3930511 147588 None 0 Human Functional pIC50 = 6.0 6.0 -1 2
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 374 5 4 5 0.9 N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1OCc1ccc(Cl)c(Cl)c1 10.1016/j.bmcl.2016.10.067
162658781 183797 None 0 Human Functional pIC50 = 6.9 6.9 1 2
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 323 5 4 5 0.5 N[C@@]1(C(=O)O)[C@H](CSc2ccccc2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4759209 183797 None 0 Human Functional pIC50 = 6.9 6.9 1 2
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 323 5 4 5 0.5 N[C@@]1(C(=O)O)[C@H](CSc2ccccc2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4803105 183797 None 0 Human Functional pIC50 = 6.9 6.9 1 2
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 323 5 4 5 0.5 N[C@@]1(C(=O)O)[C@H](CSc2ccccc2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
18548766 95916 None 0 Rat Functional pIC50 = 6.9 6.9 - 1
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 405 2 1 5 4.4 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2cc(Cl)c(C(F)(F)F)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL259053 95916 None 0 Rat Functional pIC50 = 6.9 6.9 - 1
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 405 2 1 5 4.4 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2cc(Cl)c(C(F)(F)F)cc2N1 10.1016/j.bmcl.2008.02.076
131636289 160823 None 0 Human Functional pIC50 = 6.9 6.9 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 367 3 0 5 4.0 COc1ccc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)cc1F nan
CHEMBL4113819 160823 None 0 Human Functional pIC50 = 6.9 6.9 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 367 3 0 5 4.0 COc1ccc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)cc1F nan
22224854 95437 None 0 Rat Functional pIC50 = 7.9 7.9 - 1
Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 421 2 1 5 4.3 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2007.12.005
CHEMBL256812 95437 None 0 Rat Functional pIC50 = 7.9 7.9 - 1
Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 421 2 1 5 4.3 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2007.12.005
89554852 148226 None 0 Human Functional pIC50 = 7.9 7.9 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 432 4 2 4 3.5 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(C(F)(F)F)C3)cc2n1 10.1021/acsmedchemlett.3c00210
CHEMBL3935453 148226 None 0 Human Functional pIC50 = 7.9 7.9 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 432 4 2 4 3.5 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(C(F)(F)F)C3)cc2n1 10.1021/acsmedchemlett.3c00210
123400501 196643 None 0 Human Functional pIC50 = 7.9 7.9 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 419 4 1 6 2.5 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)cn1 10.1021/acsmedchemlett.3c00210
CHEMBL5428785 196643 None 0 Human Functional pIC50 = 7.9 7.9 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 419 4 1 6 2.5 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)cn1 10.1021/acsmedchemlett.3c00210
131636351 150585 None 0 Human Functional pIC50 = 7.9 7.9 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 415 5 0 6 4.4 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1OC(F)F nan
CHEMBL3954434 150585 None 0 Human Functional pIC50 = 7.9 7.9 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 415 5 0 6 4.4 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1OC(F)F nan
90354488 161030 None 0 Human Functional pIC50 = 7.9 7.9 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 377 3 0 5 4.5 COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1C nan
CHEMBL4115442 161030 None 0 Human Functional pIC50 = 7.9 7.9 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 377 3 0 5 4.5 COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1C nan
131636294 160117 None 0 Human Functional pIC50 = 7.9 7.9 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 387 2 0 4 5.2 Cc1cc(-c2nc(-c3ccc(Cl)c(Cl)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4108019 160117 None 0 Human Functional pIC50 = 7.9 7.9 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 387 2 0 4 5.2 Cc1cc(-c2nc(-c3ccc(Cl)c(Cl)c3)n3c2CCO[C@H](C)C3)ccn1 nan
67705089 152344 None 0 Human Functional pIC50 = 7.9 7.9 1 2
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 458 7 4 7 1.9 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@@H](Sc2nc[nH]n2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1016/j.bmcl.2016.10.067
CHEMBL3969063 152344 None 0 Human Functional pIC50 = 7.9 7.9 1 2
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 458 7 4 7 1.9 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@@H](Sc2nc[nH]n2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1016/j.bmcl.2016.10.067
90367533 160177 None 0 Human Functional pIC50 = 7.9 7.9 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 395 4 0 5 4.7 COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](C)OCC3)ccc1C nan
CHEMBL4108547 160177 None 0 Human Functional pIC50 = 7.9 7.9 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 395 4 0 5 4.7 COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](C)OCC3)ccc1C nan
131636379 160838 None 0 Human Functional pIC50 = 7.9 7.9 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 3 0 5 5.2 Cc1cc(-c2nc(-c3ccc(F)c(OC(F)(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4113948 160838 None 0 Human Functional pIC50 = 7.9 7.9 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 3 0 5 5.2 Cc1cc(-c2nc(-c3ccc(F)c(OC(F)(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
137635882 155984 None 0 Human Functional pIC50 = 4.9 4.9 1 2
Antagonist activity at human mGlu2 receptor expressed in HEK cells assessed as reversal of DCG-4 inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in HEK cells assessed as reversal of DCG-4 inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 310 4 4 4 0.2 N[C@@]1(C(=O)O)C[C@H](NC(=O)C2CCCCC2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4060567 155984 None 0 Human Functional pIC50 = 4.9 4.9 1 2
Antagonist activity at human mGlu2 receptor expressed in HEK cells assessed as reversal of DCG-4 inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in HEK cells assessed as reversal of DCG-4 inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 310 4 4 4 0.2 N[C@@]1(C(=O)O)C[C@H](NC(=O)C2CCCCC2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
172463814 196849 None 0 Human Functional pIC50 = 6.9 6.9 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 418 4 2 6 2.1 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCNC(C(F)(F)F)C4)ccc23)cn1 10.1021/acsmedchemlett.3c00210
CHEMBL5433302 196849 None 0 Human Functional pIC50 = 6.9 6.9 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 418 4 2 6 2.1 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCNC(C(F)(F)F)C4)ccc23)cn1 10.1021/acsmedchemlett.3c00210
71565668 150507 None 0 Human Functional pIC50 = 6.9 6.9 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 365 4 1 4 3.1 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCOC3=O)cc2n1 10.1021/acsmedchemlett.3c00210
CHEMBL3953821 150507 None 0 Human Functional pIC50 = 6.9 6.9 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 365 4 1 4 3.1 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCOC3=O)cc2n1 10.1021/acsmedchemlett.3c00210
162644419 183728 None 0 Human Functional pIC50 = 7.9 7.9 186 2
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 323 5 4 5 0.5 N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2[C@H](O)[C@@H]1CSc1ccccc1 10.1021/acs.jmedchem.6b01119
CHEMBL4778355 183728 None 0 Human Functional pIC50 = 7.9 7.9 186 2
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 323 5 4 5 0.5 N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2[C@H](O)[C@@H]1CSc1ccccc1 10.1021/acs.jmedchem.6b01119
CHEMBL4802356 183728 None 0 Human Functional pIC50 = 7.9 7.9 186 2
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 323 5 4 5 0.5 N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2[C@H](O)[C@@H]1CSc1ccccc1 10.1021/acs.jmedchem.6b01119
22448689 97608 None 0 Rat Functional pIC50 = 7.9 7.9 - 1
Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 457 4 1 6 4.6 N#CCOc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2007.12.005
CHEMBL270616 97608 None 0 Rat Functional pIC50 = 7.9 7.9 - 1
Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 457 4 1 6 4.6 N#CCOc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2007.12.005
11281280 56424 None 0 Rat Functional pIC50 = 7.9 7.9 1 3
Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 409 2 1 3 5.8 Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
CHEMBL1631859 56424 None 0 Rat Functional pIC50 = 7.9 7.9 1 3
Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 409 2 1 3 5.8 Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
172448441 195875 None 0 Human Functional pIC50 = 7.9 7.9 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 360 4 1 4 3.5 Cn1cc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 10.1021/acsmedchemlett.3c00210
CHEMBL5412433 195875 None 0 Human Functional pIC50 = 7.9 7.9 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 360 4 1 4 3.5 Cn1cc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 10.1021/acsmedchemlett.3c00210
90354550 160036 None 0 Human Functional pIC50 = 7.9 7.9 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 5 0 5 5.1 Cc1cc(-c2nc(-c3ccc(F)c(OCC4CC4)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4107291 160036 None 0 Human Functional pIC50 = 7.9 7.9 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 5 0 5 5.1 Cc1cc(-c2nc(-c3ccc(F)c(OCC4CC4)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
131636419 148195 None 0 Human Functional pIC50 = 7.9 7.9 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 4 0 5 5.2 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCOCC3)cc(CF)n1 nan
CHEMBL3935209 148195 None 0 Human Functional pIC50 = 7.9 7.9 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 4 0 5 5.2 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCOCC3)cc(CF)n1 nan
131636316 159986 None 0 Human Functional pIC50 = 7.9 7.9 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 419 3 0 4 5.7 Cc1cc(-c2nc(-c3ccc(Cl)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(CF)n1 nan
CHEMBL4106929 159986 None 0 Human Functional pIC50 = 7.9 7.9 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 419 3 0 4 5.7 Cc1cc(-c2nc(-c3ccc(Cl)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(CF)n1 nan
78324633 160675 None 0 Human Functional pIC50 = 7.9 7.9 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 3 0 5 4.9 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)(F)F nan
CHEMBL4112706 160675 None 0 Human Functional pIC50 = 7.9 7.9 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 3 0 5 4.9 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)(F)F nan
131636296 160948 None 0 Human Functional pIC50 = 7.9 7.9 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 451 3 0 5 5.7 Cc1cc(-c2nc(-c3ccc(Cl)c(OC(F)(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4114910 160948 None 0 Human Functional pIC50 = 7.9 7.9 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 451 3 0 5 5.7 Cc1cc(-c2nc(-c3ccc(Cl)c(OC(F)(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
90354846 160102 None 0 Human Functional pIC50 = 7.9 7.9 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 401 4 0 5 4.5 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1Cl nan
CHEMBL4107888 160102 None 0 Human Functional pIC50 = 7.9 7.9 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 401 4 0 5 4.5 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1Cl nan
131636366 160334 None 0 Human Functional pIC50 = 7.9 7.9 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 419 2 0 4 5.3 Cc1cc(-c2nc(-c3ccc(F)c(C(F)(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4109916 160334 None 0 Human Functional pIC50 = 7.9 7.9 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 419 2 0 4 5.3 Cc1cc(-c2nc(-c3ccc(F)c(C(F)(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
131636405 160223 None 0 Human Functional pIC50 = 7.9 7.9 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 4 0 5 4.9 Cc1cc(-c2nc(-c3ccc(F)c(OC(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4108937 160223 None 0 Human Functional pIC50 = 7.9 7.9 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 4 0 5 4.9 Cc1cc(-c2nc(-c3ccc(F)c(OC(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
90354352 144813 None 0 Human Functional pIC50 = 7.9 7.9 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 451 4 0 5 5.4 Cc1cc(-c2nc(-c3ccc(Cl)c(OCC(F)(F)F)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3908808 144813 None 0 Human Functional pIC50 = 7.9 7.9 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 451 4 0 5 5.4 Cc1cc(-c2nc(-c3ccc(Cl)c(OCC(F)(F)F)c3)n3c2CCOCC3)cc(C)n1 nan
76318478 106156 None 0 Human Functional pIC50 = 6.9 6.9 - 1
Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis
ChEMBL 504 3 1 4 5.6 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3cccc(I)c3)cc2N1 10.1039/C3MD00110E
CHEMBL3133883 106156 None 0 Human Functional pIC50 = 6.9 6.9 - 1
Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis
ChEMBL 504 3 1 4 5.6 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3cccc(I)c3)cc2N1 10.1039/C3MD00110E
44328753 210213 None 0 Rat Functional pIC50 = 5.9 5.9 -45 6
Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated
ChEMBL 409 8 3 4 4.2 CCCC[C@@H]1[C@H](C(=O)O)[C@H]1C(N)(CC1c2ccccc2Oc2ccccc21)C(=O)O 10.1016/s0960-894x(98)00510-1
CHEMBL95868 210213 None 0 Rat Functional pIC50 = 5.9 5.9 -45 6
Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated
ChEMBL 409 8 3 4 4.2 CCCC[C@@H]1[C@H](C(=O)O)[C@H]1C(N)(CC1c2ccccc2Oc2ccccc21)C(=O)O 10.1016/s0960-894x(98)00510-1
76336598 106157 None 0 Human Functional pIC50 = 6.9 6.9 - 1
Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis
ChEMBL 504 3 1 4 5.6 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccc(I)cc3)cc2N1 10.1039/C3MD00110E
CHEMBL3133884 106157 None 0 Human Functional pIC50 = 6.9 6.9 - 1
Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis
ChEMBL 504 3 1 4 5.6 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccc(I)cc3)cc2N1 10.1039/C3MD00110E
44329033 210439 None 0 Rat Functional pIC50 = 5.9 5.9 -34 5
Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated
ChEMBL 409 7 3 4 4.1 CC(C)C[C@@H]1[C@H](C(=O)O)[C@H]1C(N)(CC1c2ccccc2Oc2ccccc21)C(=O)O 10.1016/s0960-894x(98)00510-1
CHEMBL97200 210439 None 0 Rat Functional pIC50 = 5.9 5.9 -34 5
Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated
ChEMBL 409 7 3 4 4.1 CC(C)C[C@@H]1[C@H](C(=O)O)[C@H]1C(N)(CC1c2ccccc2Oc2ccccc21)C(=O)O 10.1016/s0960-894x(98)00510-1
90643959 112056 None 0 Rat Functional pIC50 = 5.9 5.9 -1 2
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 460 4 1 7 3.2 COc1cccc(-c2cc3n(C)c(=O)c4ccc(-c5cccc(S(N)(=O)=O)c5)cc4n3n2)c1 10.1016/j.bmcl.2014.04.051
CHEMBL3288646 112056 None 0 Rat Functional pIC50 = 5.9 5.9 -1 2
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 460 4 1 7 3.2 COc1cccc(-c2cc3n(C)c(=O)c4ccc(-c5cccc(S(N)(=O)=O)c5)cc4n3n2)c1 10.1016/j.bmcl.2014.04.051
11158623 3351 None 11 Human Functional pIC50 = 7.9 7.9 -7 4
Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 10.1016/j.bmcl.2010.09.125
6226 3351 None 11 Human Functional pIC50 = 7.9 7.9 -7 4
Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 10.1016/j.bmcl.2010.09.125
CHEMBL1629855 3351 None 11 Human Functional pIC50 = 7.9 7.9 -7 4
Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 10.1016/j.bmcl.2010.09.125
10115228 96226 None 0 Rat Functional pIC50 = 7.9 7.9 - 1
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 456 5 1 6 4.8 CC(C)CN(C)c1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
CHEMBL260642 96226 None 0 Rat Functional pIC50 = 7.9 7.9 - 1
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 456 5 1 6 4.8 CC(C)CN(C)c1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
53324715 56435 None 0 Rat Functional pIC50 = 7.9 7.9 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 453 3 2 4 5.8 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C(C)(C)O)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631870 56435 None 0 Rat Functional pIC50 = 7.9 7.9 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 453 3 2 4 5.8 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C(C)(C)O)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
131636423 160128 None 0 Human Functional pIC50 = 7.9 7.9 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 471 5 0 5 5.3 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](CF)C3)cc(CF)n1 nan
CHEMBL4108112 160128 None 0 Human Functional pIC50 = 7.9 7.9 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 471 5 0 5 5.3 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](CF)C3)cc(CF)n1 nan
122580887 160600 None 0 Human Functional pIC50 = 7.9 7.9 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 401 2 0 4 5.5 Cc1cc(-c2nc(-c3ccc(Cl)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4112158 160600 None 0 Human Functional pIC50 = 7.9 7.9 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 401 2 0 4 5.5 Cc1cc(-c2nc(-c3ccc(Cl)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
131636280 159960 None 0 Human Functional pIC50 = 7.9 7.9 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 3 0 5 4.8 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4106725 159960 None 0 Human Functional pIC50 = 7.9 7.9 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 3 0 5 4.8 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCO[C@H](C)C3)ccn1 nan
131636375 161010 None 0 Human Functional pIC50 = 7.8 7.8 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 2 0 4 5.6 Cc1cc(-c2nc(-c3ccc(Cl)c(C(F)(F)F)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4115306 161010 None 0 Human Functional pIC50 = 7.8 7.8 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 2 0 4 5.6 Cc1cc(-c2nc(-c3ccc(Cl)c(C(F)(F)F)c3)n3c2CCO[C@H](C)C3)ccn1 nan
10710505 78769 None 0 Human Functional pIC50 = 5.9 5.9 -1 2
Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2
ChEMBL 316 6 3 4 1.6 Cn1cc(CCC(N)(C(=O)O)[C@H]2C[C@@H]2C(=O)O)c2ccccc21 10.1021/jm970497w
CHEMBL2112580 78769 None 0 Human Functional pIC50 = 5.9 5.9 -1 2
Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2
ChEMBL 316 6 3 4 1.6 Cn1cc(CCC(N)(C(=O)O)[C@H]2C[C@@H]2C(=O)O)c2ccccc21 10.1021/jm970497w
155526616 171238 None 0 Rat Functional pIC50 = 5.9 5.9 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 371 5 1 5 3.0 CN(Cc1cc2nc(C(N)=O)cc(-c3ccc(F)cc3)c2s1)C1COC1 10.1021/acs.jmedchem.8b01266
CHEMBL4458387 171238 None 0 Rat Functional pIC50 = 5.9 5.9 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 371 5 1 5 3.0 CN(Cc1cc2nc(C(N)=O)cc(-c3ccc(F)cc3)c2s1)C1COC1 10.1021/acs.jmedchem.8b01266
155530126 171571 None 0 Rat Functional pIC50 = 5.9 5.9 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 401 5 1 6 3.0 COc1ccc(-c2cc(C(N)=O)nc3cc(CN4CCOCC4)sc23)c(F)c1 10.1021/acs.jmedchem.8b01266
CHEMBL4463498 171571 None 0 Rat Functional pIC50 = 5.9 5.9 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 401 5 1 6 3.0 COc1ccc(-c2cc(C(N)=O)nc3cc(CN4CCOCC4)sc23)c(F)c1 10.1021/acs.jmedchem.8b01266
155526616 171238 None 0 Rat Functional pIC50 = 5.9 5.9 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 371 5 1 5 3.0 CN(Cc1cc2nc(C(N)=O)cc(-c3ccc(F)cc3)c2s1)C1COC1 10.1021/acs.jmedchem.8b01266
CHEMBL4458387 171238 None 0 Rat Functional pIC50 = 5.9 5.9 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 371 5 1 5 3.0 CN(Cc1cc2nc(C(N)=O)cc(-c3ccc(F)cc3)c2s1)C1COC1 10.1021/acs.jmedchem.8b01266
155530126 171571 None 0 Rat Functional pIC50 = 5.9 5.9 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 401 5 1 6 3.0 COc1ccc(-c2cc(C(N)=O)nc3cc(CN4CCOCC4)sc23)c(F)c1 10.1021/acs.jmedchem.8b01266
CHEMBL4463498 171571 None 0 Rat Functional pIC50 = 5.9 5.9 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 401 5 1 6 3.0 COc1ccc(-c2cc(C(N)=O)nc3cc(CN4CCOCC4)sc23)c(F)c1 10.1021/acs.jmedchem.8b01266
162654849 183776 None 0 Human Functional pIC50 = 5.8 5.8 -1 2
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 341 5 4 5 0.6 N[C@@]1(C(=O)O)[C@H](CSc2ccccc2F)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4755204 183776 None 0 Human Functional pIC50 = 5.8 5.8 -1 2
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 341 5 4 5 0.6 N[C@@]1(C(=O)O)[C@H](CSc2ccccc2F)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4802906 183776 None 0 Human Functional pIC50 = 5.8 5.8 -1 2
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 341 5 4 5 0.6 N[C@@]1(C(=O)O)[C@H](CSc2ccccc2F)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
155550549 175212 None 0 Rat Functional pIC50 = 6.8 6.8 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 461 6 1 7 3.6 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccnc(C(F)(F)F)c4)nn23)c(F)c1 10.1021/acs.jmedchem.8b01266
CHEMBL4569114 175212 None 0 Rat Functional pIC50 = 6.8 6.8 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 461 6 1 7 3.6 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccnc(C(F)(F)F)c4)nn23)c(F)c1 10.1021/acs.jmedchem.8b01266
155550549 175212 None 0 Rat Functional pIC50 = 6.8 6.8 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 461 6 1 7 3.6 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccnc(C(F)(F)F)c4)nn23)c(F)c1 10.1021/acs.jmedchem.8b01266
CHEMBL4569114 175212 None 0 Rat Functional pIC50 = 6.8 6.8 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 461 6 1 7 3.6 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccnc(C(F)(F)F)c4)nn23)c(F)c1 10.1021/acs.jmedchem.8b01266
134139744 146047 None 0 Human Functional pIC50 = 6.8 6.8 -1 2
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 375 5 4 5 1.0 N[C@@]1(C(=O)O)[C@H](OCc2cccc(Cl)c2Cl)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1016/j.bmcl.2016.10.067
CHEMBL3918170 146047 None 0 Human Functional pIC50 = 6.8 6.8 -1 2
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 375 5 4 5 1.0 N[C@@]1(C(=O)O)[C@H](OCc2cccc(Cl)c2Cl)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1016/j.bmcl.2016.10.067
11442010 56325 None 0 Human Functional pIC50 = 7.8 7.8 -5 3
Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 439 4 1 4 5.9 CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1629866 56325 None 0 Human Functional pIC50 = 7.8 7.8 -5 3
Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 439 4 1 4 5.9 CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
18548908 96317 None 0 Rat Functional pIC50 = 7.8 7.8 - 1
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 404 2 1 4 5.0 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(Cl)c(C(F)(F)F)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL261051 96317 None 0 Rat Functional pIC50 = 7.8 7.8 - 1
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 404 2 1 4 5.0 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(Cl)c(C(F)(F)F)cc2N1 10.1016/j.bmcl.2008.02.076
9891158 155676 None 0 Rat Functional pIC50 = 7.8 7.8 - 1
Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 476 6 1 6 4.8 COCCOc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2007.12.005
CHEMBL404463 155676 None 0 Rat Functional pIC50 = 7.8 7.8 - 1
Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 476 6 1 6 4.8 COCCOc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2007.12.005
22317918 56316 None 0 Rat Functional pIC50 = 7.8 7.8 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 439 3 2 4 5.3 Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(CO)n1 10.1016/j.bmcl.2010.09.125
CHEMBL1629858 56316 None 0 Rat Functional pIC50 = 7.8 7.8 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 439 3 2 4 5.3 Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(CO)n1 10.1016/j.bmcl.2010.09.125
172441694 195335 None 0 Human Functional pIC50 = 7.8 7.8 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 374 5 1 4 3.7 Cn1ccc(CCc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)n1 10.1021/acsmedchemlett.3c00210
CHEMBL5401453 195335 None 0 Human Functional pIC50 = 7.8 7.8 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 374 5 1 4 3.7 Cn1ccc(CCc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)n1 10.1021/acsmedchemlett.3c00210
172450613 195950 None 0 Human Functional pIC50 = 7.8 7.8 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 376 5 2 5 4.0 Cc1cc(NCc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)no1 10.1021/acsmedchemlett.3c00210
CHEMBL5414037 195950 None 0 Human Functional pIC50 = 7.8 7.8 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 376 5 2 5 4.0 Cc1cc(NCc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)no1 10.1021/acsmedchemlett.3c00210
131636418 160681 None 0 Human Functional pIC50 = 7.8 7.8 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 4 0 4 5.7 Cc1cc(-c2nc(-c3ccc(C(F)F)c(Cl)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
CHEMBL4112763 160681 None 0 Human Functional pIC50 = 7.8 7.8 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 4 0 4 5.7 Cc1cc(-c2nc(-c3ccc(C(F)F)c(Cl)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
131636410 160922 None 0 Human Functional pIC50 = 7.8 7.8 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 449 5 0 5 5.8 COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)F nan
CHEMBL4114609 160922 None 0 Human Functional pIC50 = 7.8 7.8 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 449 5 0 5 5.8 COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)F nan
131636388 160453 None 0 Human Functional pIC50 = 7.8 7.8 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 439 4 0 5 4.9 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](CF)C3)ccn1 nan
CHEMBL4110884 160453 None 0 Human Functional pIC50 = 7.8 7.8 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 439 4 0 5 4.9 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](CF)C3)ccn1 nan
131636353 161020 None 0 Human Functional pIC50 = 7.8 7.8 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 2 0 4 5.9 Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4115388 161020 None 0 Human Functional pIC50 = 7.8 7.8 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 2 0 4 5.9 Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
131636385 160886 None 0 Human Functional pIC50 = 7.8 7.8 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 447 6 0 6 4.8 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)F nan
CHEMBL4114364 160886 None 0 Human Functional pIC50 = 7.8 7.8 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 447 6 0 6 4.8 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)F nan
49858117 1089 None 4 Human Functional pIC50 = 5.8 5.8 5 2
Negative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assayNegative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assay
ChEMBL 308 2 2 4 3.0 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)C 10.1021/jm101069m
6223 1089 None 4 Human Functional pIC50 = 5.8 5.8 5 2
Negative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assayNegative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assay
ChEMBL 308 2 2 4 3.0 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)C 10.1021/jm101069m
CHEMBL1630806 1089 None 4 Human Functional pIC50 = 5.8 5.8 5 2
Negative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assayNegative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assay
ChEMBL 308 2 2 4 3.0 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)C 10.1021/jm101069m
155566841 175964 None 0 Rat Functional pIC50 = 5.8 5.8 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 382 5 1 6 3.5 Cn1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)n1 10.1021/acs.jmedchem.8b01266
CHEMBL4585786 175964 None 0 Rat Functional pIC50 = 5.8 5.8 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 382 5 1 6 3.5 Cn1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)n1 10.1021/acs.jmedchem.8b01266
155566841 175964 None 0 Rat Functional pIC50 = 5.8 5.8 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 382 5 1 6 3.5 Cn1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)n1 10.1021/acs.jmedchem.8b01266
CHEMBL4585786 175964 None 0 Rat Functional pIC50 = 5.8 5.8 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 382 5 1 6 3.5 Cn1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)n1 10.1021/acs.jmedchem.8b01266
71681826 90095 None 0 Human Functional pIC50 = 4.8 4.8 -1 3
Antagonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as reversal of DCG-4-inhibited, forskolin-stimulated cAMP production after 1 hr by fluorescence assayAntagonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as reversal of DCG-4-inhibited, forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 293 4 3 4 1.3 N[C@@]1(C(=O)O)C[C@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL2381651 90095 None 0 Human Functional pIC50 = 4.8 4.8 -1 3
Antagonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as reversal of DCG-4-inhibited, forskolin-stimulated cAMP production after 1 hr by fluorescence assayAntagonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as reversal of DCG-4-inhibited, forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 293 4 3 4 1.3 N[C@@]1(C(=O)O)C[C@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
90643958 112055 None 0 Rat Functional pIC50 = 5.8 5.8 -6 2
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 370 2 0 5 4.1 Cn1c(=O)c2ccc(-c3cccnc3)cc2n2nc(-c3cccc(F)c3)cc12 10.1016/j.bmcl.2014.04.051
CHEMBL3288644 112055 None 0 Rat Functional pIC50 = 5.8 5.8 -6 2
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 370 2 0 5 4.1 Cn1c(=O)c2ccc(-c3cccnc3)cc2n2nc(-c3cccc(F)c3)cc12 10.1016/j.bmcl.2014.04.051
22224970 155582 None 0 Rat Functional pIC50 = 7.8 7.8 - 1
Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 420 2 1 4 4.9 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C#Cc3ccccc3F)cc2N1 10.1016/j.bmcl.2007.12.005
CHEMBL404080 155582 None 0 Rat Functional pIC50 = 7.8 7.8 - 1
Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 420 2 1 4 4.9 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C#Cc3ccccc3F)cc2N1 10.1016/j.bmcl.2007.12.005
22317715 56313 None 0 Rat Functional pIC50 = 7.8 7.8 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 396 2 1 4 4.9 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cnccn3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1629854 56313 None 0 Rat Functional pIC50 = 7.8 7.8 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 396 2 1 4 4.9 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cnccn3)c1)=N2 10.1016/j.bmcl.2010.09.125
53326017 56437 None 0 Rat Functional pIC50 = 7.8 7.8 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 425 3 1 4 5.5 COc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
CHEMBL1631872 56437 None 0 Rat Functional pIC50 = 7.8 7.8 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 425 3 1 4 5.5 COc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
131636403 159989 None 0 Human Functional pIC50 = 7.8 7.8 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 4 0 5 4.9 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(F)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4106954 159989 None 0 Human Functional pIC50 = 7.8 7.8 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 4 0 5 4.9 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(F)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
131636317 160669 None 0 Human Functional pIC50 = 7.8 7.8 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 433 5 0 5 5.0 COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](CF)OCC3)ccc1Cl nan
CHEMBL4112663 160669 None 0 Human Functional pIC50 = 7.8 7.8 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 433 5 0 5 5.0 COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](CF)OCC3)ccc1Cl nan
69669747 183759 None 14 Human Functional pIC50 = 7.8 7.8 -2 4
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 359 5 4 5 0.8 N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)c(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4751065 183759 None 14 Human Functional pIC50 = 7.8 7.8 -2 4
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 359 5 4 5 0.8 N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)c(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4802733 183759 None 14 Human Functional pIC50 = 7.8 7.8 -2 4
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 359 5 4 5 0.8 N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)c(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
90354858 159958 None 0 Human Functional pIC50 = 7.8 7.8 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 431 5 0 5 5.1 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)F nan
CHEMBL4106716 159958 None 0 Human Functional pIC50 = 7.8 7.8 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 431 5 0 5 5.1 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)F nan
67705326 153337 None 0 Human Functional pIC50 = 7.8 7.8 2 2
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 457 7 4 6 2.5 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@@H](Sc2ncc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1016/j.bmcl.2016.10.067
CHEMBL3977508 153337 None 0 Human Functional pIC50 = 7.8 7.8 2 2
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 457 7 4 6 2.5 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@@H](Sc2ncc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1016/j.bmcl.2016.10.067
131636349 145320 None 0 Human Functional pIC50 = 7.8 7.8 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 3 0 4 5.4 Cc1cc(-c2nc(-c3ccc(Cl)c(C(F)F)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3912677 145320 None 0 Human Functional pIC50 = 7.8 7.8 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 3 0 4 5.4 Cc1cc(-c2nc(-c3ccc(Cl)c(C(F)F)c3)n3c2CCOCC3)cc(C)n1 nan
131636444 159971 None 0 Human Functional pIC50 = 7.8 7.8 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 377 4 0 5 4.6 CCOc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C nan
CHEMBL4106785 159971 None 0 Human Functional pIC50 = 7.8 7.8 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 377 4 0 5 4.6 CCOc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C nan
131636315 160623 None 0 Human Functional pIC50 = 7.8 7.8 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 399 3 0 4 5.3 Cc1cc(-c2nc(-c3ccc(Cl)c(C)c3)n3c2CCO[C@H](C)C3)cc(CF)n1 nan
CHEMBL4112341 160623 None 0 Human Functional pIC50 = 7.8 7.8 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 399 3 0 4 5.3 Cc1cc(-c2nc(-c3ccc(Cl)c(C)c3)n3c2CCO[C@H](C)C3)cc(CF)n1 nan
22317185 56307 None 0 Rat Functional pIC50 = 6.8 6.8 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 410 2 2 4 5.1 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(N)nc3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1629848 56307 None 0 Rat Functional pIC50 = 6.8 6.8 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 410 2 2 4 5.1 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(N)nc3)c1)=N2 10.1016/j.bmcl.2010.09.125
44345358 113413 None 0 Human Functional pIC50 = 5.8 5.8 1 2
Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2
ChEMBL 215 5 3 3 0.5 CC(C)C[C@](N)(C(=O)O)C1C[C@@H]1C(=O)O 10.1021/jm970497w
CHEMBL331753 113413 None 0 Human Functional pIC50 = 5.8 5.8 1 2
Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2
ChEMBL 215 5 3 3 0.5 CC(C)C[C@](N)(C(=O)O)C1C[C@@H]1C(=O)O 10.1021/jm970497w
123331489 195921 None 0 Human Functional pIC50 = 6.8 6.8 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 365 4 1 6 2.0 CC1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)CCO1 10.1021/acsmedchemlett.3c00210
CHEMBL5413435 195921 None 0 Human Functional pIC50 = 6.8 6.8 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 365 4 1 6 2.0 CC1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)CCO1 10.1021/acsmedchemlett.3c00210
10456810 107935 None 0 Rat Functional pIC50 = 5.8 5.8 -13 5
Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated
ChEMBL 457 8 3 4 4.7 NC(CC1c2ccccc2Oc2ccccc21)(C(=O)O)[C@H]1[C@H](CCc2ccccc2)[C@@H]1C(=O)O 10.1016/s0960-894x(98)00510-1
CHEMBL319279 107935 None 0 Rat Functional pIC50 = 5.8 5.8 -13 5
Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated
ChEMBL 457 8 3 4 4.7 NC(CC1c2ccccc2Oc2ccccc21)(C(=O)O)[C@H]1[C@H](CCc2ccccc2)[C@@H]1C(=O)O 10.1016/s0960-894x(98)00510-1
134132133 144877 None 0 Human Functional pIC50 = 6.8 6.8 -1 2
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 375 5 4 5 1.0 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1016/j.bmcl.2016.10.067
CHEMBL3909237 144877 None 0 Human Functional pIC50 = 6.8 6.8 -1 2
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 375 5 4 5 1.0 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1016/j.bmcl.2016.10.067
44450391 168938 None 0 Rat Functional pIC50 = 7.8 7.8 - 1
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 414 3 1 4 5.3 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3cc(F)ccc3F)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL437835 168938 None 0 Rat Functional pIC50 = 7.8 7.8 - 1
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 414 3 1 4 5.3 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3cc(F)ccc3F)cc2N1 10.1016/j.bmcl.2008.02.076
9820321 155098 None 0 Rat Functional pIC50 = 7.8 7.8 - 1
Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 361 1 1 3 4.4 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.12.005
CHEMBL401446 155098 None 0 Rat Functional pIC50 = 7.8 7.8 - 1
Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 361 1 1 3 4.4 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.12.005
135544097 155755 None 0 Rat Functional pIC50 = 7.8 7.8 269 2
Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 437 2 2 6 4.0 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2007.12.005
CHEMBL404886 155755 None 0 Rat Functional pIC50 = 7.8 7.8 269 2
Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 437 2 2 6 4.0 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2007.12.005
9820321 155098 None 0 Rat Functional pIC50 = 7.8 7.8 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 361 1 1 3 4.4 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2010.09.125
CHEMBL401446 155098 None 0 Rat Functional pIC50 = 7.8 7.8 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 361 1 1 3 4.4 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2010.09.125
67633340 183827 None 0 Human Functional pIC50 = 7.8 7.8 1 2
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 355 5 4 5 0.9 Cc1cc(SC[C@@H]2[C@@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)ccc1F 10.1021/acs.jmedchem.6b01119
CHEMBL4780402 183827 None 0 Human Functional pIC50 = 7.8 7.8 1 2
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 355 5 4 5 0.9 Cc1cc(SC[C@@H]2[C@@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)ccc1F 10.1021/acs.jmedchem.6b01119
CHEMBL4803381 183827 None 0 Human Functional pIC50 = 7.8 7.8 1 2
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 355 5 4 5 0.9 Cc1cc(SC[C@@H]2[C@@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)ccc1F 10.1021/acs.jmedchem.6b01119
131636443 159940 None 0 Human Functional pIC50 = 7.8 7.8 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 431 6 0 5 5.5 CCc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1OCC1CC1 nan
CHEMBL4106566 159940 None 0 Human Functional pIC50 = 7.8 7.8 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 431 6 0 5 5.5 CCc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1OCC1CC1 nan
131636400 160095 None 0 Human Functional pIC50 = 7.8 7.8 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 413 4 0 5 5.1 COc1ccc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](C)OCC3)cc1C nan
CHEMBL4107829 160095 None 0 Human Functional pIC50 = 7.8 7.8 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 413 4 0 5 5.1 COc1ccc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](C)OCC3)cc1C nan
131636337 152764 None 0 Human Functional pIC50 = 7.8 7.8 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 437 3 0 5 5.4 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(Cl)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3972702 152764 None 0 Human Functional pIC50 = 7.8 7.8 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 437 3 0 5 5.4 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(Cl)c3)n3c2CCOCC3)cc(C)n1 nan
131636401 160489 None 0 Human Functional pIC50 = 7.8 7.8 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 447 4 1 6 4.6 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(CO)n1 nan
CHEMBL4111225 160489 None 0 Human Functional pIC50 = 7.8 7.8 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 447 4 1 6 4.6 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(CO)n1 nan
11503055 2400 None 2 Human Functional pIC50 = 4.8 4.8 -31 2
Negative allosteric modulation of human mGlu2 receptor assessed as Ca2+ flux by FLIPR assayNegative allosteric modulation of human mGlu2 receptor assessed as Ca2+ flux by FLIPR assay
ChEMBL 400 4 1 4 3.9 Clc1ccc(c(c1)Cl)CN[C@H]1CCN(C1)c1ncc(cn1)Br 10.1021/jm400439t
9694 2400 None 2 Human Functional pIC50 = 4.8 4.8 -31 2
Negative allosteric modulation of human mGlu2 receptor assessed as Ca2+ flux by FLIPR assayNegative allosteric modulation of human mGlu2 receptor assessed as Ca2+ flux by FLIPR assay
ChEMBL 400 4 1 4 3.9 Clc1ccc(c(c1)Cl)CN[C@H]1CCN(C1)c1ncc(cn1)Br 10.1021/jm400439t
CHEMBL2204436 2400 None 2 Human Functional pIC50 = 4.8 4.8 -31 2
Negative allosteric modulation of human mGlu2 receptor assessed as Ca2+ flux by FLIPR assayNegative allosteric modulation of human mGlu2 receptor assessed as Ca2+ flux by FLIPR assay
ChEMBL 400 4 1 4 3.9 Clc1ccc(c(c1)Cl)CN[C@H]1CCN(C1)c1ncc(cn1)Br 10.1021/jm400439t
155538435 172470 None 0 Rat Functional pIC50 = 5.8 5.8 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 447 5 1 5 5.2 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3ccnc(C(F)(F)F)c3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4476138 172470 None 0 Rat Functional pIC50 = 5.8 5.8 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 447 5 1 5 5.2 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3ccnc(C(F)(F)F)c3)cc2n1 10.1021/acs.jmedchem.8b01266
155539352 172938 None 0 Rat Functional pIC50 = 5.8 5.8 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 369 4 1 4 4.2 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCCCC3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4514334 172938 None 0 Rat Functional pIC50 = 5.8 5.8 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 369 4 1 4 4.2 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCCCC3)cc2n1 10.1021/acs.jmedchem.8b01266
155562175 175928 None 0 Rat Functional pIC50 = 5.8 5.8 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 361 5 1 5 2.8 NC(=O)c1cc(-c2ccc(F)cc2)n2nc(CCc3cccnc3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4584801 175928 None 0 Rat Functional pIC50 = 5.8 5.8 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 361 5 1 5 2.8 NC(=O)c1cc(-c2ccc(F)cc2)n2nc(CCc3cccnc3)cc2n1 10.1021/acs.jmedchem.8b01266
155539352 172938 None 0 Rat Functional pIC50 = 5.8 5.8 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 369 4 1 4 4.2 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCCCC3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4514334 172938 None 0 Rat Functional pIC50 = 5.8 5.8 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 369 4 1 4 4.2 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCCCC3)cc2n1 10.1021/acs.jmedchem.8b01266
155562175 175928 None 0 Rat Functional pIC50 = 5.8 5.8 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 361 5 1 5 2.8 NC(=O)c1cc(-c2ccc(F)cc2)n2nc(CCc3cccnc3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4584801 175928 None 0 Rat Functional pIC50 = 5.8 5.8 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 361 5 1 5 2.8 NC(=O)c1cc(-c2ccc(F)cc2)n2nc(CCc3cccnc3)cc2n1 10.1021/acs.jmedchem.8b01266
155538435 172470 None 0 Rat Functional pIC50 = 5.8 5.8 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 447 5 1 5 5.2 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3ccnc(C(F)(F)F)c3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4476138 172470 None 0 Rat Functional pIC50 = 5.8 5.8 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 447 5 1 5 5.2 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3ccnc(C(F)(F)F)c3)cc2n1 10.1021/acs.jmedchem.8b01266
11298568 69397 None 1 Human Functional pIC50 = 5.8 5.8 5 2
Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor
ChEMBL 199 2 3 3 -0.2 C[C@@H]1C[C@H]2[C@H](C(=O)O)[C@H]2[C@]1(N)C(=O)O 10.1021/jm040222y
CHEMBL192977 69397 None 1 Human Functional pIC50 = 5.8 5.8 5 2
Evaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptorEvaluation of the functional effect on cAMP responses in RGT cells expressing human mGlu2 receptor
ChEMBL 199 2 3 3 -0.2 C[C@@H]1C[C@H]2[C@H](C(=O)O)[C@H]2[C@]1(N)C(=O)O 10.1021/jm040222y
90643974 112066 None 0 Rat Functional pIC50 = 5.8 5.8 -3 2
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 352 2 0 5 3.9 Cn1c(=O)c2ccc(-c3ccncc3)cc2n2nc(-c3ccccc3)cc12 10.1016/j.bmcl.2014.04.051
CHEMBL3288675 112066 None 0 Rat Functional pIC50 = 5.8 5.8 -3 2
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 352 2 0 5 3.9 Cn1c(=O)c2ccc(-c3ccncc3)cc2n2nc(-c3ccccc3)cc12 10.1016/j.bmcl.2014.04.051
90643963 112058 None 0 Rat Functional pIC50 = 5.8 5.8 -3 2
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 366 2 0 5 4.2 Cc1cccc(-c2cc3n(C)c(=O)c4ccc(-c5cccnc5)cc4n3n2)c1 10.1016/j.bmcl.2014.04.051
CHEMBL3288653 112058 None 0 Rat Functional pIC50 = 5.8 5.8 -3 2
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 366 2 0 5 4.2 Cc1cccc(-c2cc3n(C)c(=O)c4ccc(-c5cccnc5)cc4n3n2)c1 10.1016/j.bmcl.2014.04.051
22224670 96320 None 0 Rat Functional pIC50 = 7.8 7.8 - 1
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 415 3 1 5 4.7 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3cc(F)ccc3F)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL261081 96320 None 0 Rat Functional pIC50 = 7.8 7.8 - 1
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 415 3 1 5 4.7 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3cc(F)ccc3F)cc2N1 10.1016/j.bmcl.2008.02.076
53316736 56300 None 0 Rat Functional pIC50 = 7.8 7.8 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 423 3 1 3 6.1 CCc1ccc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cn1 10.1016/j.bmcl.2010.09.125
CHEMBL1629715 56300 None 0 Rat Functional pIC50 = 7.8 7.8 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 423 3 1 3 6.1 CCc1ccc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cn1 10.1016/j.bmcl.2010.09.125
22317847 56426 None 0 Rat Functional pIC50 = 7.8 7.8 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 420 2 1 4 5.4 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C#N)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631861 56426 None 0 Rat Functional pIC50 = 7.8 7.8 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 420 2 1 4 5.4 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C#N)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
11212447 56433 None 0 Rat Functional pIC50 = 7.8 7.8 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 425 3 2 4 5.0 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(CO)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631868 56433 None 0 Rat Functional pIC50 = 7.8 7.8 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 425 3 2 4 5.0 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(CO)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
172471485 197144 None 0 Human Functional pIC50 = 7.8 7.8 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 380 4 1 5 2.2 CC1CCN(c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)CC1 10.1021/acsmedchemlett.3c00210
CHEMBL5439830 197144 None 0 Human Functional pIC50 = 7.8 7.8 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 380 4 1 5 2.2 CC1CCN(c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)CC1 10.1021/acsmedchemlett.3c00210
131636450 160732 None 0 Human Functional pIC50 = 7.8 7.8 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 447 4 1 6 4.6 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(CO)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4113175 160732 None 0 Human Functional pIC50 = 7.8 7.8 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 447 4 1 6 4.6 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(CO)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
131636373 159952 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 4 0 5 4.6 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(F)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4106692 159952 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 4 0 5 4.6 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(F)c3)n3c2CCO[C@H](C)C3)ccn1 nan
131636397 160077 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 465 5 0 6 5.0 COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)cc1OC(F)(F)F nan
CHEMBL4107640 160077 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 465 5 0 6 5.0 COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)cc1OC(F)(F)F nan
131636360 150336 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 3 0 4 5.4 Cc1cc(-c2nc(-c3ccc(C(F)F)c(Cl)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3952383 150336 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 3 0 4 5.4 Cc1cc(-c2nc(-c3ccc(C(F)F)c(Cl)c3)n3c2CCOCC3)cc(C)n1 nan
131636427 160775 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 453 4 0 5 5.4 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](C)C3)cc(CF)n1 nan
CHEMBL4113474 160775 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 453 4 0 5 5.4 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](C)C3)cc(CF)n1 nan
67707808 148730 None 0 Human Functional pIC50 = 7.7 7.7 1 2
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 432 6 4 6 1.3 COC(=O)N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1OCc1ccc(Cl)c(Cl)c1 10.1016/j.bmcl.2016.10.067
CHEMBL3939492 148730 None 0 Human Functional pIC50 = 7.7 7.7 1 2
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 432 6 4 6 1.3 COC(=O)N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1OCc1ccc(Cl)c(Cl)c1 10.1016/j.bmcl.2016.10.067
131636372 160304 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 415 5 0 6 4.5 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1OC(F)F nan
CHEMBL4109618 160304 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 415 5 0 6 4.5 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1OC(F)F nan
131636299 160364 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 395 4 0 5 4.5 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1C nan
CHEMBL4110209 160364 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 395 4 0 5 4.5 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1C nan
10492773 16792 None 0 Human Functional pIC50 = 6.8 6.8 -2 2
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 277 6 3 3 1.4 Cc1cccc(CC[C@](N)(C(=O)O)[C@H]2C[C@@H]2C(=O)O)c1 10.1021/jm970498o
CHEMBL124501 16792 None 0 Human Functional pIC50 = 6.8 6.8 -2 2
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 277 6 3 3 1.4 Cc1cccc(CC[C@](N)(C(=O)O)[C@H]2C[C@@H]2C(=O)O)c1 10.1021/jm970498o
44348993 114649 None 0 Human Functional pIC50 = 6.8 6.8 1 2
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 297 6 3 3 1.8 N[C@@](CCc1cccc(Cl)c1)(C(=O)O)C1C[C@@H]1C(=O)O 10.1021/jm970498o
CHEMBL333771 114649 None 0 Human Functional pIC50 = 6.8 6.8 1 2
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 297 6 3 3 1.8 N[C@@](CCc1cccc(Cl)c1)(C(=O)O)C1C[C@@H]1C(=O)O 10.1021/jm970498o
44348706 116946 None 0 Human Functional pIC50 = 6.8 6.8 1 2
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 281 6 3 3 1.3 N[C@@](CCc1ccc(F)cc1)(C(=O)O)C1C[C@@H]1C(=O)O 10.1021/jm970498o
CHEMBL338282 116946 None 0 Human Functional pIC50 = 6.8 6.8 1 2
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 281 6 3 3 1.3 N[C@@](CCc1ccc(F)cc1)(C(=O)O)C1C[C@@H]1C(=O)O 10.1021/jm970498o
10828532 78796 None 0 Human Functional pIC50 = 5.8 5.8 -22 2
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 307 7 4 4 0.8 NC(CCc1cccc(C(=O)O)c1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970498o
CHEMBL2112634 78796 None 0 Human Functional pIC50 = 5.8 5.8 -22 2
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 307 7 4 4 0.8 NC(CCc1cccc(C(=O)O)c1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970498o
10359073 155064 None 0 Human Functional pIC50 = 4.8 4.8 -1 2
Tested for agonist activity in non-neuronal cells (RGT) expressing human Metabotropic glutamate receptor 2 by measuring ACPD (3 uM) induced inhibition of forskolin (15 uM)-stimulated cAMP formationTested for agonist activity in non-neuronal cells (RGT) expressing human Metabotropic glutamate receptor 2 by measuring ACPD (3 uM) induced inhibition of forskolin (15 uM)-stimulated cAMP formation
ChEMBL 327 8 3 3 2.7 N[C@@H](C[C@H](CC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O 10.1016/s0960-894x(98)00091-2
CHEMBL40123 155064 None 0 Human Functional pIC50 = 4.8 4.8 -1 2
Tested for agonist activity in non-neuronal cells (RGT) expressing human Metabotropic glutamate receptor 2 by measuring ACPD (3 uM) induced inhibition of forskolin (15 uM)-stimulated cAMP formationTested for agonist activity in non-neuronal cells (RGT) expressing human Metabotropic glutamate receptor 2 by measuring ACPD (3 uM) induced inhibition of forskolin (15 uM)-stimulated cAMP formation
ChEMBL 327 8 3 3 2.7 N[C@@H](C[C@H](CC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O 10.1016/s0960-894x(98)00091-2
18613455 96103 None 0 Rat Functional pIC50 = 6.7 6.7 - 1
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 414 3 1 6 3.8 CN(C)c1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
CHEMBL259924 96103 None 0 Rat Functional pIC50 = 6.7 6.7 - 1
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 414 3 1 6 3.8 CN(C)c1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
44329031 108330 None 0 Rat Functional pIC50 = 5.7 5.7 -15 7
Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated
ChEMBL 437 10 3 4 5.0 CCCCCC[C@@H]1[C@H](C(=O)O)[C@H]1C(N)(CC1c2ccccc2Oc2ccccc21)C(=O)O 10.1016/s0960-894x(98)00510-1
CHEMBL319732 108330 None 0 Rat Functional pIC50 = 5.7 5.7 -15 7
Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated
ChEMBL 437 10 3 4 5.0 CCCCCC[C@@H]1[C@H](C(=O)O)[C@H]1C(N)(CC1c2ccccc2Oc2ccccc21)C(=O)O 10.1016/s0960-894x(98)00510-1
18548739 160459 None 0 Rat Functional pIC50 = 7.7 7.7 - 1
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 384 2 1 4 4.7 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2008.02.076
CHEMBL411095 160459 None 0 Rat Functional pIC50 = 7.7 7.7 - 1
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 384 2 1 4 4.7 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2008.02.076
18548739 160459 None 0 Rat Functional pIC50 = 7.7 7.7 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 384 2 1 4 4.7 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL411095 160459 None 0 Rat Functional pIC50 = 7.7 7.7 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 384 2 1 4 4.7 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2010.09.125
172456225 196300 None 0 Human Functional pIC50 = 7.7 7.7 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 387 5 2 5 3.9 Cc1ncc(NCc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 10.1021/acsmedchemlett.3c00210
CHEMBL5420899 196300 None 0 Human Functional pIC50 = 7.7 7.7 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 387 5 2 5 3.9 Cc1ncc(NCc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 10.1021/acsmedchemlett.3c00210
131636333 154277 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 2 0 4 5.5 Cc1cc(-c2nc(-c3ccc(Cl)c(C(F)(F)F)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3985799 154277 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 2 0 4 5.5 Cc1cc(-c2nc(-c3ccc(Cl)c(C(F)(F)F)c3)n3c2CCOCC3)cc(C)n1 nan
131636339 160230 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 383 3 0 5 4.5 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1Cl nan
CHEMBL4108997 160230 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 383 3 0 5 4.5 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1Cl nan
131636378 160582 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 433 4 0 6 4.8 COc1ccc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)cc1OC(F)(F)F nan
CHEMBL4111987 160582 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 433 4 0 6 4.8 COc1ccc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)cc1OC(F)(F)F nan
131636395 160596 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 437 3 0 4 5.3 Cc1cc(-c2nc(-c3ccc(F)c(C(F)(F)F)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
CHEMBL4112129 160596 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 437 3 0 4 5.3 Cc1cc(-c2nc(-c3ccc(F)c(C(F)(F)F)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
131636373 159952 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 4 0 5 4.6 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(F)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4106692 159952 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 4 0 5 4.6 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(F)c3)n3c2CCO[C@H](C)C3)ccn1 nan
131636407 160197 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 433 3 0 4 5.5 Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
CHEMBL4108700 160197 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 433 3 0 4 5.5 Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
131636408 160854 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 419 3 0 4 5.2 Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)ccn1 nan
CHEMBL4114047 160854 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 419 3 0 4 5.2 Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)ccn1 nan
131636329 144725 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 363 3 0 5 4.1 COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)cc1C nan
CHEMBL3908089 144725 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 363 3 0 5 4.1 COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)cc1C nan
131636284 160598 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 367 2 0 4 4.8 Cc1cc(-c2nc(-c3ccc(Cl)c(C)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4112146 160598 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 367 2 0 4 4.8 Cc1cc(-c2nc(-c3ccc(Cl)c(C)c3)n3c2CCO[C@H](C)C3)ccn1 nan
90354963 160740 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 427 4 0 5 5.3 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(C)(F)F nan
CHEMBL4113235 160740 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 427 4 0 5 5.3 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(C)(F)F nan
131636406 160470 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 4 0 5 4.6 Cc1cc(-c2nc(-c3ccc(F)c(OC(F)F)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4111067 160470 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 4 0 5 4.6 Cc1cc(-c2nc(-c3ccc(F)c(OC(F)F)c3)n3c2CCO[C@H](C)C3)ccn1 nan
90355009 160343 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 433 4 1 6 4.3 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(CO)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4109993 160343 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 433 4 1 6 4.3 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(CO)c3)n3c2CCO[C@H](C)C3)ccn1 nan
86695984 149853 None 0 Human Functional pIC50 = 7.7 7.7 1 2
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 472 7 3 8 1.9 Cn1ncnc1S[C@@H]1[C@@H](OCc2ccc(Cl)c(Cl)c2)[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1016/j.bmcl.2016.10.067
CHEMBL3948272 149853 None 0 Human Functional pIC50 = 7.7 7.7 1 2
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 472 7 3 8 1.9 Cn1ncnc1S[C@@H]1[C@@H](OCc2ccc(Cl)c(Cl)c2)[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1016/j.bmcl.2016.10.067
53316798 56421 None 0 Rat Functional pIC50 = 6.7 6.7 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 384 2 1 4 4.6 Cn1nccc1-c1cccc(C2=Nc3ccc(C(F)(F)F)cc3NC(=O)C2)c1 10.1016/j.bmcl.2010.09.125
CHEMBL1631856 56421 None 0 Rat Functional pIC50 = 6.7 6.7 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 384 2 1 4 4.6 Cn1nccc1-c1cccc(C2=Nc3ccc(C(F)(F)F)cc3NC(=O)C2)c1 10.1016/j.bmcl.2010.09.125
44348846 117076 None 0 Human Functional pIC50 = 6.7 6.7 -1 2
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 341 7 3 5 0.5 CS(=O)(=O)c1cccc(CC[C@](N)(C(=O)O)C2C[C@@H]2C(=O)O)c1 10.1021/jm970498o
CHEMBL2111822 117076 None 0 Human Functional pIC50 = 6.7 6.7 -1 2
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 341 7 3 5 0.5 CS(=O)(=O)c1cccc(CC[C@](N)(C(=O)O)C2C[C@@H]2C(=O)O)c1 10.1021/jm970498o
CHEMBL338911 117076 None 0 Human Functional pIC50 = 6.7 6.7 -1 2
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 341 7 3 5 0.5 CS(=O)(=O)c1cccc(CC[C@](N)(C(=O)O)C2C[C@@H]2C(=O)O)c1 10.1021/jm970498o
90643954 112053 None 0 Rat Functional pIC50 = 5.7 5.7 -2 2
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 430 3 1 6 3.2 Cn1c(=O)c2ccc(-c3cccc(S(N)(=O)=O)c3)cc2n2nc(-c3ccccc3)cc12 10.1016/j.bmcl.2014.04.051
CHEMBL3288636 112053 None 0 Rat Functional pIC50 = 5.7 5.7 -2 2
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 430 3 1 6 3.2 Cn1c(=O)c2ccc(-c3cccc(S(N)(=O)=O)c3)cc2n2nc(-c3ccccc3)cc12 10.1016/j.bmcl.2014.04.051
155523578 171011 None 0 Rat Functional pIC50 = 5.7 5.7 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 409 6 1 6 4.2 COc1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)cn1 10.1021/acs.jmedchem.8b01266
CHEMBL4454867 171011 None 0 Rat Functional pIC50 = 5.7 5.7 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 409 6 1 6 4.2 COc1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)cn1 10.1021/acs.jmedchem.8b01266
155523578 171011 None 0 Rat Functional pIC50 = 5.7 5.7 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 409 6 1 6 4.2 COc1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)cn1 10.1021/acs.jmedchem.8b01266
CHEMBL4454867 171011 None 0 Rat Functional pIC50 = 5.7 5.7 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 409 6 1 6 4.2 COc1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)cn1 10.1021/acs.jmedchem.8b01266
11304010 56323 None 0 Rat Functional pIC50 = 8.7 8.7 2 3
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 395 2 1 3 5.8 Cc1cc(-c2cccc(C3=Nc4cc(Cl)c(Cl)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
CHEMBL1629864 56323 None 0 Rat Functional pIC50 = 8.7 8.7 2 3
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 395 2 1 3 5.8 Cc1cc(-c2cccc(C3=Nc4cc(Cl)c(Cl)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
122580902 160099 None 0 Human Functional pIC50 = 8.7 8.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 451 5 0 5 5.4 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(Cl)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
CHEMBL4107872 160099 None 0 Human Functional pIC50 = 8.7 8.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 451 5 0 5 5.4 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(Cl)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
131636451 160104 None 0 Human Functional pIC50 = 8.6 8.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 449 4 0 5 5.6 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(CF)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4107913 160104 None 0 Human Functional pIC50 = 8.6 8.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 449 4 0 5 5.6 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(CF)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
131636422 160136 None 0 Human Functional pIC50 = 8.6 8.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 467 5 0 5 5.3 COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)(F)F nan
CHEMBL4108163 160136 None 0 Human Functional pIC50 = 8.6 8.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 467 5 0 5 5.3 COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)(F)F nan
131636461 160218 None 0 Human Functional pIC50 = 8.6 8.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 405 4 0 5 5.3 Cc1cc(-c2nc(-c3ccc(OC(C)C)c(C)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4108918 160218 None 0 Human Functional pIC50 = 8.6 8.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 405 4 0 5 5.3 Cc1cc(-c2nc(-c3ccc(OC(C)C)c(C)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
78320558 160541 None 0 Human Functional pIC50 = 8.6 8.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 4 0 5 5.3 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(CF)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4111659 160541 None 0 Human Functional pIC50 = 8.6 8.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 4 0 5 5.3 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(CF)c3)n3c2CCO[C@H](C)C3)ccn1 nan
90354985 160773 None 0 Human Functional pIC50 = 8.6 8.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 425 4 0 5 5.6 Cc1cc(-c2nc(-c3ccc(OC(C)C)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4113466 160773 None 0 Human Functional pIC50 = 8.6 8.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 425 4 0 5 5.6 Cc1cc(-c2nc(-c3ccc(OC(C)C)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
78319944 160825 None 0 Human Functional pIC50 = 8.6 8.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 465 5 0 6 5.0 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)(F)F nan
CHEMBL4113834 160825 None 0 Human Functional pIC50 = 8.6 8.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 465 5 0 6 5.0 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)(F)F nan
78320252 160619 None 0 Human Functional pIC50 = 8.6 8.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 411 4 0 5 5.2 CCOc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1Cl nan
CHEMBL4112321 160619 None 0 Human Functional pIC50 = 8.6 8.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 411 4 0 5 5.2 CCOc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1Cl nan
90354835 160658 None 0 Human Functional pIC50 = 8.6 8.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 433 4 0 5 5.4 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4112598 160658 None 0 Human Functional pIC50 = 8.6 8.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 433 4 0 5 5.4 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
131636455 160498 None 0 Human Functional pIC50 = 8.5 8.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 5 0 5 5.0 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(CF)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4111276 160498 None 0 Human Functional pIC50 = 8.5 8.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 5 0 5 5.0 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(CF)c3)n3c2CCO[C@H](C)C3)ccn1 nan
131636460 160573 None 0 Human Functional pIC50 = 8.5 8.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 391 4 0 5 4.9 CCOc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1C nan
CHEMBL4111924 160573 None 0 Human Functional pIC50 = 8.5 8.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 391 4 0 5 4.9 CCOc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1C nan
1397 2529 None 15 Human Functional pIC50 = 7.7 7.7 1 8
Antagonist activity at mGLUR2 expressed in CHO cells assessed as inhibition of glutamate-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at mGLUR2 expressed in CHO cells assessed as inhibition of glutamate-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 377 5 3 4 2.1 OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1016/j.bmcl.2012.01.039
9886034 2529 None 15 Human Functional pIC50 = 7.7 7.7 1 8
Antagonist activity at mGLUR2 expressed in CHO cells assessed as inhibition of glutamate-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at mGLUR2 expressed in CHO cells assessed as inhibition of glutamate-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 377 5 3 4 2.1 OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1016/j.bmcl.2012.01.039
CHEMBL186453 2529 None 15 Human Functional pIC50 = 7.7 7.7 1 8
Antagonist activity at mGLUR2 expressed in CHO cells assessed as inhibition of glutamate-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at mGLUR2 expressed in CHO cells assessed as inhibition of glutamate-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 377 5 3 4 2.1 OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1016/j.bmcl.2012.01.039
22317728 56305 None 0 Rat Functional pIC50 = 7.7 7.7 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 435 3 1 3 6.4 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(C4CC4)nc3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1629846 56305 None 0 Rat Functional pIC50 = 7.7 7.7 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 435 3 1 3 6.4 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(C4CC4)nc3)c1)=N2 10.1016/j.bmcl.2010.09.125
71566598 142777 None 16 Human Functional pIC50 = 7.7 7.7 2 3
Negative allosteric modulation of human mGluR2 by GTPgammaS binding assayNegative allosteric modulation of human mGluR2 by GTPgammaS binding assay
ChEMBL 377 4 1 4 2.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1 10.1016/j.bmcl.2020.127066
CHEMBL3892073 142777 None 16 Human Functional pIC50 = 7.7 7.7 2 3
Negative allosteric modulation of human mGluR2 by GTPgammaS binding assayNegative allosteric modulation of human mGluR2 by GTPgammaS binding assay
ChEMBL 377 4 1 4 2.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1 10.1016/j.bmcl.2020.127066
67637138 183724 None 0 Human Functional pIC50 = 7.7 7.7 2 2
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 341 5 4 5 0.6 N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)cc2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4776989 183724 None 0 Human Functional pIC50 = 7.7 7.7 2 2
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 341 5 4 5 0.6 N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)cc2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4802329 183724 None 0 Human Functional pIC50 = 7.7 7.7 2 2
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 341 5 4 5 0.6 N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)cc2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
131636365 160089 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 401 2 0 4 5.2 Cc1cc(-c2nc(-c3ccc(C(F)(F)F)cc3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4107737 160089 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 401 2 0 4 5.2 Cc1cc(-c2nc(-c3ccc(C(F)(F)F)cc3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
131636282 160673 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 381 2 0 4 5.2 Cc1cc(-c2nc(-c3ccc(Cl)c(C)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4112692 160673 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 381 2 0 4 5.2 Cc1cc(-c2nc(-c3ccc(Cl)c(C)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
131636409 160555 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 467 6 0 5 5.7 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C(F)F)n1 nan
CHEMBL4111753 160555 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 467 6 0 5 5.7 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C(F)F)n1 nan
131636331 144988 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 3 0 5 4.8 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3910129 144988 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 3 0 5 4.8 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCOCC3)cc(C)n1 nan
131636297 160076 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 4 0 5 5.0 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
CHEMBL4107635 160076 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 4 0 5 5.0 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
122580890 160570 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 419 3 0 4 5.4 Cc1cc(-c2nc(-c3ccc(Cl)c(Cl)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
CHEMBL4111874 160570 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 419 3 0 4 5.4 Cc1cc(-c2nc(-c3ccc(Cl)c(Cl)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
10807972 35826 None 1 Human Functional pIC50 = 6.7 6.7 -12 4
Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2
ChEMBL 353 5 3 4 2.8 N[C@@](CC1c2ccccc2Oc2ccccc21)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970497w
CHEMBL144151 35826 None 1 Human Functional pIC50 = 6.7 6.7 -12 4
Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2
ChEMBL 353 5 3 4 2.8 N[C@@](CC1c2ccccc2Oc2ccccc21)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970497w
1378 2417 None 39 Rat Functional pIC50 = 6.7 6.7 -9 14
Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1016/s0960-894x(98)00510-1
1399 2417 None 39 Rat Functional pIC50 = 6.7 6.7 -9 14
Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1016/s0960-894x(98)00510-1
9819927 2417 None 39 Rat Functional pIC50 = 6.7 6.7 -9 14
Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1016/s0960-894x(98)00510-1
CHEMBL432038 2417 None 39 Rat Functional pIC50 = 6.7 6.7 -9 14
Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1016/s0960-894x(98)00510-1
10358265 102181 None 0 Human Functional pIC50 = 4.7 4.7 -2 2
In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.
ChEMBL 314 4 3 4 1.3 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2cccc3ccccc23)C1 10.1016/s0960-894x(98)00352-7
CHEMBL302411 102181 None 0 Human Functional pIC50 = 4.7 4.7 -2 2
In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.
ChEMBL 314 4 3 4 1.3 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2cccc3ccccc23)C1 10.1016/s0960-894x(98)00352-7
162663798 183825 None 0 Human Functional pIC50 = 5.7 5.7 1 2
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 323 5 4 5 0.5 N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2[C@@H](O)[C@@H]1CSc1ccccc1 10.1021/acs.jmedchem.6b01119
CHEMBL4779554 183825 None 0 Human Functional pIC50 = 5.7 5.7 1 2
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 323 5 4 5 0.5 N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2[C@@H](O)[C@@H]1CSc1ccccc1 10.1021/acs.jmedchem.6b01119
CHEMBL4803378 183825 None 0 Human Functional pIC50 = 5.7 5.7 1 2
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 323 5 4 5 0.5 N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2[C@@H](O)[C@@H]1CSc1ccccc1 10.1021/acs.jmedchem.6b01119
1378 2417 None 39 Human Functional pIC50 = 7.7 7.7 -2 14
Antagonist activity at human mGLUR2 expressed in RGT cells assessed as inhibition of (1S,3R)-1-aminocyclopentane-1,3-dicarboxylic acid-induced inhibition of forskolin stimulated cyclic-AMPAntagonist activity at human mGLUR2 expressed in RGT cells assessed as inhibition of (1S,3R)-1-aminocyclopentane-1,3-dicarboxylic acid-induced inhibition of forskolin stimulated cyclic-AMP
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1016/j.bmcl.2012.01.039
1399 2417 None 39 Human Functional pIC50 = 7.7 7.7 -2 14
Antagonist activity at human mGLUR2 expressed in RGT cells assessed as inhibition of (1S,3R)-1-aminocyclopentane-1,3-dicarboxylic acid-induced inhibition of forskolin stimulated cyclic-AMPAntagonist activity at human mGLUR2 expressed in RGT cells assessed as inhibition of (1S,3R)-1-aminocyclopentane-1,3-dicarboxylic acid-induced inhibition of forskolin stimulated cyclic-AMP
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1016/j.bmcl.2012.01.039
9819927 2417 None 39 Human Functional pIC50 = 7.7 7.7 -2 14
Antagonist activity at human mGLUR2 expressed in RGT cells assessed as inhibition of (1S,3R)-1-aminocyclopentane-1,3-dicarboxylic acid-induced inhibition of forskolin stimulated cyclic-AMPAntagonist activity at human mGLUR2 expressed in RGT cells assessed as inhibition of (1S,3R)-1-aminocyclopentane-1,3-dicarboxylic acid-induced inhibition of forskolin stimulated cyclic-AMP
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1016/j.bmcl.2012.01.039
CHEMBL432038 2417 None 39 Human Functional pIC50 = 7.7 7.7 -2 14
Antagonist activity at human mGLUR2 expressed in RGT cells assessed as inhibition of (1S,3R)-1-aminocyclopentane-1,3-dicarboxylic acid-induced inhibition of forskolin stimulated cyclic-AMPAntagonist activity at human mGLUR2 expressed in RGT cells assessed as inhibition of (1S,3R)-1-aminocyclopentane-1,3-dicarboxylic acid-induced inhibition of forskolin stimulated cyclic-AMP
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1016/j.bmcl.2012.01.039
131636435 148478 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 377 5 0 5 4.5 CCOc1cc(-c2nc(-c3ccnc(C)c3)c3n2CCOCC3)ccc1CC nan
CHEMBL3937514 148478 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 377 5 0 5 4.5 CCOc1cc(-c2nc(-c3ccnc(C)c3)c3n2CCOCC3)ccc1CC nan
131636361 160768 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 385 2 0 4 5.0 Cc1cc(-c2nc(-c3ccc(F)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4113439 160768 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 385 2 0 4 5.0 Cc1cc(-c2nc(-c3ccc(F)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
131636283 160878 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 377 3 0 5 4.5 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C nan
CHEMBL4114284 160878 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 377 3 0 5 4.5 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C nan
131636454 160059 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 429 5 1 6 4.3 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(CO)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4107497 160059 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 429 5 1 6 4.3 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(CO)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
131636290 160593 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 367 2 0 4 4.8 Cc1cc(-c2nc(-c3ccc(Cl)cc3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4112105 160593 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 367 2 0 4 4.8 Cc1cc(-c2nc(-c3ccc(Cl)cc3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
122580905 160160 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 385 2 0 4 5.0 Cc1cc(-c2nc(-c3ccc(Cl)c(F)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4108383 160160 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 385 2 0 4 5.0 Cc1cc(-c2nc(-c3ccc(Cl)c(F)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
131636285 161041 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 363 3 0 5 4.2 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C nan
CHEMBL4115529 161041 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 363 3 0 5 4.2 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C nan
134154496 152599 None 0 Human Functional pIC50 = 6.7 6.7 -1 2
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 341 5 4 5 0.3 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)cc2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1016/j.bmcl.2016.10.067
CHEMBL3971347 152599 None 0 Human Functional pIC50 = 6.7 6.7 -1 2
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 341 5 4 5 0.3 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)cc2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1016/j.bmcl.2016.10.067
134141510 147156 None 0 Human Functional pIC50 = 6.7 6.7 -2 2
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 339 5 4 5 0.1 Cc1cc(CO[C@@H]2[C@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)ccc1F 10.1016/j.bmcl.2016.10.067
CHEMBL3927108 147156 None 0 Human Functional pIC50 = 6.7 6.7 -2 2
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 339 5 4 5 0.1 Cc1cc(CO[C@@H]2[C@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)ccc1F 10.1016/j.bmcl.2016.10.067
44329029 163616 None 0 Rat Functional pIC50 = 5.7 5.7 2 6
Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated
ChEMBL 479 13 3 4 6.2 CCCCCCCCC[C@@H]1[C@H](C(=O)O)[C@H]1C(N)(CC1c2ccccc2Oc2ccccc21)C(=O)O 10.1016/s0960-894x(98)00510-1
CHEMBL420262 163616 None 0 Rat Functional pIC50 = 5.7 5.7 2 6
Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated
ChEMBL 479 13 3 4 6.2 CCCCCCCCC[C@@H]1[C@H](C(=O)O)[C@H]1C(N)(CC1c2ccccc2Oc2ccccc21)C(=O)O 10.1016/s0960-894x(98)00510-1
9952648 96361 None 0 Rat Functional pIC50 = 7.7 7.7 1 2
Antagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK currentAntagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK current
ChEMBL 397 3 1 5 4.5 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL261288 96361 None 0 Rat Functional pIC50 = 7.7 7.7 1 2
Antagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK currentAntagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK current
ChEMBL 397 3 1 5 4.5 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1 10.1016/j.bmcl.2008.02.076
172457959 196475 None 0 Human Functional pIC50 = 7.7 7.7 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 377 5 2 3 3.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CNCC(F)(F)F)cc2n1 10.1021/acsmedchemlett.3c00210
CHEMBL5424670 196475 None 0 Human Functional pIC50 = 7.7 7.7 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 377 5 2 3 3.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CNCC(F)(F)F)cc2n1 10.1021/acsmedchemlett.3c00210
118906265 146036 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 433 4 0 6 4.7 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1OC(F)(F)F nan
CHEMBL3918111 146036 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 433 4 0 6 4.7 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1OC(F)(F)F nan
131636314 160135 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 3 0 4 5.1 Cc1cc(-c2nc(-c3ccc(Cl)c(F)c3)n3c2CCO[C@H](C)C3)cc(CF)n1 nan
CHEMBL4108162 160135 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 3 0 4 5.1 Cc1cc(-c2nc(-c3ccc(Cl)c(F)c3)n3c2CCO[C@H](C)C3)cc(CF)n1 nan
131636448 160634 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 419 5 0 5 5.5 Cc1cc(-c2nc(-c3ccc(C)c(OCC(C)C)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4112439 160634 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 419 5 0 5 5.5 Cc1cc(-c2nc(-c3ccc(C)c(OCC(C)C)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
131636346 152589 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 3 0 5 4.8 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1C(F)(F)F nan
CHEMBL3971278 152589 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 3 0 5 4.8 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1C(F)(F)F nan
131636369 160911 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 3 0 4 5.8 Cc1cc(-c2nc(-c3ccc(C(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4114534 160911 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 3 0 4 5.8 Cc1cc(-c2nc(-c3ccc(C(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
131636276 145995 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 383 3 0 5 4.5 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1Cl nan
CHEMBL3917816 145995 None 0 Human Functional pIC50 = 7.7 7.7 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 383 3 0 5 4.5 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1Cl nan
90367528 144168 None 0 Human Functional pIC50 = 7.6 7.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 397 4 0 5 4.9 CCOc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1Cl nan
CHEMBL3903357 144168 None 0 Human Functional pIC50 = 7.6 7.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 397 4 0 5 4.9 CCOc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1Cl nan
44348911 16573 None 0 Human Functional pIC50 = 6.7 6.7 1 2
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 331 6 3 3 2.1 N[C@@](CCc1cccc(C(F)(F)F)c1)(C(=O)O)C1C[C@@H]1C(=O)O 10.1021/jm970498o
CHEMBL123847 16573 None 0 Human Functional pIC50 = 6.7 6.7 1 2
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 331 6 3 3 2.1 N[C@@](CCc1cccc(C(F)(F)F)c1)(C(=O)O)C1C[C@@H]1C(=O)O 10.1021/jm970498o
10688450 16611 None 0 Human Functional pIC50 = 6.7 6.7 -1 2
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 339 7 3 3 2.7 N[C@](CC(c1ccccc1)c1ccccc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970498o
CHEMBL124078 16611 None 0 Human Functional pIC50 = 6.7 6.7 -1 2
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 339 7 3 3 2.7 N[C@](CC(c1ccccc1)c1ccccc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970498o
155547618 173690 None 0 Rat Functional pIC50 = 6.7 6.7 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 441 5 1 6 3.4 NC(=O)c1cc(-c2ccc(F)cc2)n2nc(COc3ccnc(Br)c3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4533083 173690 None 0 Rat Functional pIC50 = 6.7 6.7 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 441 5 1 6 3.4 NC(=O)c1cc(-c2ccc(F)cc2)n2nc(COc3ccnc(Br)c3)cc2n1 10.1021/acs.jmedchem.8b01266
155547618 173690 None 0 Rat Functional pIC50 = 6.7 6.7 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 441 5 1 6 3.4 NC(=O)c1cc(-c2ccc(F)cc2)n2nc(COc3ccnc(Br)c3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4533083 173690 None 0 Rat Functional pIC50 = 6.7 6.7 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 441 5 1 6 3.4 NC(=O)c1cc(-c2ccc(F)cc2)n2nc(COc3ccnc(Br)c3)cc2n1 10.1021/acs.jmedchem.8b01266
134129940 142533 None 0 Human Functional pIC50 = 6.7 6.7 -1 2
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 359 5 4 5 0.5 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(F)c2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1016/j.bmcl.2016.10.067
CHEMBL3890112 142533 None 0 Human Functional pIC50 = 6.7 6.7 -1 2
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 359 5 4 5 0.5 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(F)c2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1016/j.bmcl.2016.10.067
162652146 180319 None 0 Human Functional pIC50 = 5.6 5.6 1 2
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 289 5 4 5 -0.2 CC(C)SC[C@@H]1[C@@H](O)[C@@H]2[C@@H]([C@H]2C(=O)O)[C@]1(N)C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4749728 180319 None 0 Human Functional pIC50 = 5.6 5.6 1 2
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 289 5 4 5 -0.2 CC(C)SC[C@@H]1[C@@H](O)[C@@H]2[C@@H]([C@H]2C(=O)O)[C@]1(N)C(=O)O 10.1021/acs.jmedchem.6b01119
1378 2417 None 39 Human Functional pIC50 = 7.6 7.6 -2 14
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/jm970498o
1399 2417 None 39 Human Functional pIC50 = 7.6 7.6 -2 14
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/jm970498o
9819927 2417 None 39 Human Functional pIC50 = 7.6 7.6 -2 14
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/jm970498o
CHEMBL432038 2417 None 39 Human Functional pIC50 = 7.6 7.6 -2 14
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/jm970498o
172449011 195944 None 0 Human Functional pIC50 = 7.6 7.6 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 393 5 1 6 2.6 CC(C)C1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)CCO1 10.1021/acsmedchemlett.3c00210
CHEMBL5413826 195944 None 0 Human Functional pIC50 = 7.6 7.6 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 393 5 1 6 2.6 CC(C)C1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)CCO1 10.1021/acsmedchemlett.3c00210
22224852 95917 None 0 Rat Functional pIC50 = 7.6 7.6 -2 2
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 396 3 1 4 5.1 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL259054 95917 None 0 Rat Functional pIC50 = 7.6 7.6 -2 2
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 396 3 1 4 5.1 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2008.02.076
9845873 160893 None 0 Rat Functional pIC50 = 7.6 7.6 - 1
Antagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK currentAntagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK current
ChEMBL 436 2 2 5 4.6 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL411440 160893 None 0 Rat Functional pIC50 = 7.6 7.6 - 1
Antagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK currentAntagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK current
ChEMBL 436 2 2 5 4.6 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2008.02.076
9845873 160893 None 0 Rat Functional pIC50 = 7.6 7.6 - 1
Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 436 2 2 5 4.6 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2010.09.125
CHEMBL411440 160893 None 0 Rat Functional pIC50 = 7.6 7.6 - 1
Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 436 2 2 5 4.6 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2010.09.125
71565884 143512 None 0 Human Functional pIC50 = 7.6 7.6 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 433 4 1 4 3.9 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1 10.1021/acsmedchemlett.3c00210
CHEMBL3898121 143512 None 0 Human Functional pIC50 = 7.6 7.6 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 433 4 1 4 3.9 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1 10.1021/acsmedchemlett.3c00210
131636382 160501 None 0 Human Functional pIC50 = 7.6 7.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 5 0 5 4.8 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)F nan
CHEMBL4111287 160501 None 0 Human Functional pIC50 = 7.6 7.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 5 0 5 4.8 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)F nan
131636396 160335 None 0 Human Functional pIC50 = 7.6 7.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 423 3 0 4 5.0 Cc1cc(-c2nc(-c3ccc(F)c(C(F)(F)F)c3)n3c2CCO[C@H](CF)C3)ccn1 nan
CHEMBL4109918 160335 None 0 Human Functional pIC50 = 7.6 7.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 423 3 0 4 5.0 Cc1cc(-c2nc(-c3ccc(F)c(C(F)(F)F)c3)n3c2CCO[C@H](CF)C3)ccn1 nan
131636301 160530 None 0 Human Functional pIC50 = 7.6 7.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 399 3 0 4 5.1 Cc1cc(-c2nc(-c3ccc(Cl)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
CHEMBL4111566 160530 None 0 Human Functional pIC50 = 7.6 7.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 399 3 0 4 5.1 Cc1cc(-c2nc(-c3ccc(Cl)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
10852666 78772 None 0 Human Functional pIC50 = 6.6 6.6 1 2
Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2
ChEMBL 313 6 3 3 2.3 NC(CCc1cccc2ccccc12)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970497w
CHEMBL2112583 78772 None 0 Human Functional pIC50 = 6.6 6.6 1 2
Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2
ChEMBL 313 6 3 3 2.3 NC(CCc1cccc2ccccc12)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970497w
10567792 78775 None 0 Human Functional pIC50 = 6.6 6.6 3 2
Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2
ChEMBL 321 6 3 3 2.5 NC(CCC12CC3CC(CC(C3)C1)C2)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970497w
CHEMBL2112586 78775 None 0 Human Functional pIC50 = 6.6 6.6 3 2
Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2
ChEMBL 321 6 3 3 2.5 NC(CCC12CC3CC(CC(C3)C1)C2)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970497w
90355016 160796 None 0 Human Functional pIC50 = 6.6 6.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 399 4 1 6 3.7 COc1cc(-c2nc(-c3ccnc(CO)c3)c3n2C[C@@H](C)OCC3)ccc1Cl nan
CHEMBL4113592 160796 None 0 Human Functional pIC50 = 6.6 6.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 399 4 1 6 3.7 COc1cc(-c2nc(-c3ccnc(CO)c3)c3n2C[C@@H](C)OCC3)ccc1Cl nan
86298614 112067 None 0 Rat Functional pIC50 = 6.6 6.6 -3 2
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 353 2 0 6 3.3 Cn1c(=O)c2ccc(-c3cncnc3)cc2n2nc(-c3ccccc3)cc12 10.1016/j.bmcl.2014.04.051
CHEMBL3288676 112067 None 0 Rat Functional pIC50 = 6.6 6.6 -3 2
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 353 2 0 6 3.3 Cn1c(=O)c2ccc(-c3cncnc3)cc2n2nc(-c3ccccc3)cc12 10.1016/j.bmcl.2014.04.051
86298614 112067 None 0 Rat Functional pIC50 = 6.6 6.6 -3 2
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 353 2 0 6 3.3 Cn1c(=O)c2ccc(-c3cncnc3)cc2n2nc(-c3ccccc3)cc12 10.1016/j.bmcl.2014.04.051
CHEMBL3288676 112067 None 0 Rat Functional pIC50 = 6.6 6.6 -3 2
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 353 2 0 6 3.3 Cn1c(=O)c2ccc(-c3cncnc3)cc2n2nc(-c3ccccc3)cc12 10.1016/j.bmcl.2014.04.051
11211597 56324 None 0 Human Functional pIC50 = 7.6 7.6 -1 3
Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 395 2 1 3 5.5 Cc1cc(-c2cccc(C3=Nc4ccc(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
CHEMBL1629865 56324 None 0 Human Functional pIC50 = 7.6 7.6 -1 3
Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 395 2 1 3 5.5 Cc1cc(-c2cccc(C3=Nc4ccc(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
131636336 148752 None 0 Human Functional pIC50 = 7.6 7.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 378 2 0 5 4.3 Cc1cc(-c2nc(-c3ccc(Cl)c(C#N)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3939714 148752 None 0 Human Functional pIC50 = 7.6 7.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 378 2 0 5 4.3 Cc1cc(-c2nc(-c3ccc(Cl)c(C#N)c3)n3c2CCOCC3)cc(C)n1 nan
131636311 152737 None 0 Human Functional pIC50 = 7.6 7.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 387 4 0 5 4.3 COc1cc(-c2nc(-c3ccnc(CF)c3)c3n2CCOCC3)ccc1Cl nan
CHEMBL3972441 152737 None 0 Human Functional pIC50 = 7.6 7.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 387 4 0 5 4.3 COc1cc(-c2nc(-c3ccnc(CF)c3)c3n2CCOCC3)ccc1Cl nan
131636326 160653 None 0 Human Functional pIC50 = 7.6 7.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 5 0 5 5.2 Cc1cc(-c2nc(-c3ccc(F)c(OCC4CCC4)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4112588 160653 None 0 Human Functional pIC50 = 7.6 7.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 5 0 5 5.2 Cc1cc(-c2nc(-c3ccc(F)c(OCC4CCC4)c3)n3c2CCO[C@H](C)C3)ccn1 nan
131636323 148149 None 0 Human Functional pIC50 = 7.6 7.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 5 0 5 5.1 Cc1cc(-c2nc(-c3ccc(F)c(OCC4CCC4)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3934756 148149 None 0 Human Functional pIC50 = 7.6 7.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 5 0 5 5.1 Cc1cc(-c2nc(-c3ccc(F)c(OCC4CCC4)c3)n3c2CCOCC3)cc(C)n1 nan
131636298 160222 None 0 Human Functional pIC50 = 7.6 7.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 4 0 5 4.7 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCO[C@H](CF)C3)ccn1 nan
CHEMBL4108936 160222 None 0 Human Functional pIC50 = 7.6 7.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 4 0 5 4.7 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCO[C@H](CF)C3)ccn1 nan
122580894 160787 None 0 Human Functional pIC50 = 7.6 7.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 3 0 4 5.8 Cc1cc(-c2nc(-c3ccc(Cl)c(C(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4113546 160787 None 0 Human Functional pIC50 = 7.6 7.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 3 0 4 5.8 Cc1cc(-c2nc(-c3ccc(Cl)c(C(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
155538978 172885 None 0 Rat Functional pIC50 = 5.6 5.6 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 383 5 1 6 2.9 COc1ccc(-c2cc(C(N)=O)nc3cc(CN4CCOCC4)sc23)cc1 10.1021/acs.jmedchem.8b01266
CHEMBL4513332 172885 None 0 Rat Functional pIC50 = 5.6 5.6 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 383 5 1 6 2.9 COc1ccc(-c2cc(C(N)=O)nc3cc(CN4CCOCC4)sc23)cc1 10.1021/acs.jmedchem.8b01266
155538978 172885 None 0 Rat Functional pIC50 = 5.6 5.6 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 383 5 1 6 2.9 COc1ccc(-c2cc(C(N)=O)nc3cc(CN4CCOCC4)sc23)cc1 10.1021/acs.jmedchem.8b01266
CHEMBL4513332 172885 None 0 Rat Functional pIC50 = 5.6 5.6 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 383 5 1 6 2.9 COc1ccc(-c2cc(C(N)=O)nc3cc(CN4CCOCC4)sc23)cc1 10.1021/acs.jmedchem.8b01266
155514808 170001 None 0 Rat Functional pIC50 = 5.6 5.6 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 409 6 1 6 4.2 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccc(F)nc4)sc23)cc1 10.1021/acs.jmedchem.8b01266
CHEMBL4440771 170001 None 0 Rat Functional pIC50 = 5.6 5.6 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 409 6 1 6 4.2 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccc(F)nc4)sc23)cc1 10.1021/acs.jmedchem.8b01266
155514808 170001 None 0 Rat Functional pIC50 = 5.6 5.6 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 409 6 1 6 4.2 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccc(F)nc4)sc23)cc1 10.1021/acs.jmedchem.8b01266
CHEMBL4440771 170001 None 0 Rat Functional pIC50 = 5.6 5.6 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 409 6 1 6 4.2 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccc(F)nc4)sc23)cc1 10.1021/acs.jmedchem.8b01266
11269030 56320 None 0 Rat Functional pIC50 = 7.6 7.6 -1 3
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 381 2 1 3 5.2 O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(C(F)(F)F)cc2N1 10.1016/j.bmcl.2010.09.125
CHEMBL1629861 56320 None 0 Rat Functional pIC50 = 7.6 7.6 -1 3
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 381 2 1 3 5.2 O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(C(F)(F)F)cc2N1 10.1016/j.bmcl.2010.09.125
131636328 148833 None 0 Human Functional pIC50 = 7.6 7.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 387 2 0 4 5.1 Cc1cc(-c2nc(-c3ccc(Cl)c(Cl)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3940380 148833 None 0 Human Functional pIC50 = 7.6 7.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 387 2 0 4 5.1 Cc1cc(-c2nc(-c3ccc(Cl)c(Cl)c3)n3c2CCOCC3)cc(C)n1 nan
131636354 160444 None 0 Human Functional pIC50 = 7.6 7.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 392 2 0 5 4.7 Cc1cc(-c2nc(-c3ccc(Cl)c(C#N)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4110789 160444 None 0 Human Functional pIC50 = 7.6 7.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 392 2 0 5 4.7 Cc1cc(-c2nc(-c3ccc(Cl)c(C#N)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
67705376 145427 None 0 Human Functional pIC50 = 7.6 7.6 -1 2
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 416 6 4 5 1.1 CC(=O)N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1OCc1ccc(Cl)c(Cl)c1 10.1016/j.bmcl.2016.10.067
CHEMBL3913414 145427 None 0 Human Functional pIC50 = 7.6 7.6 -1 2
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 416 6 4 5 1.1 CC(=O)N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1OCc1ccc(Cl)c(Cl)c1 10.1016/j.bmcl.2016.10.067
69669820 183746 None 0 Human Functional pIC50 = 7.6 7.6 -2 2
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 396 6 4 5 1.1 CC(=O)N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1CSc1ccc(F)c(C)c1 10.1021/acs.jmedchem.6b01119
CHEMBL4746125 183746 None 0 Human Functional pIC50 = 7.6 7.6 -2 2
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 396 6 4 5 1.1 CC(=O)N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1CSc1ccc(F)c(C)c1 10.1021/acs.jmedchem.6b01119
CHEMBL4802570 183746 None 0 Human Functional pIC50 = 7.6 7.6 -2 2
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 396 6 4 5 1.1 CC(=O)N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1CSc1ccc(F)c(C)c1 10.1021/acs.jmedchem.6b01119
131636374 160194 None 0 Human Functional pIC50 = 7.6 7.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 405 2 0 4 5.0 Cc1cc(-c2nc(-c3ccc(F)c(C(F)(F)F)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4108665 160194 None 0 Human Functional pIC50 = 7.6 7.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 405 2 0 4 5.0 Cc1cc(-c2nc(-c3ccc(F)c(C(F)(F)F)c3)n3c2CCO[C@H](C)C3)ccn1 nan
90354688 160633 None 0 Human Functional pIC50 = 7.6 7.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 413 5 0 5 4.7 Cc1cc(-c2nc(-c3ccc(F)c(OCCF)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4112422 160633 None 0 Human Functional pIC50 = 7.6 7.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 413 5 0 5 4.7 Cc1cc(-c2nc(-c3ccc(F)c(OCCF)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
1378 2417 None 39 Human Functional pIC50 = 7.6 7.6 -2 14
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/acs.jmedchem.6b01119
1399 2417 None 39 Human Functional pIC50 = 7.6 7.6 -2 14
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/acs.jmedchem.6b01119
9819927 2417 None 39 Human Functional pIC50 = 7.6 7.6 -2 14
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/acs.jmedchem.6b01119
CHEMBL432038 2417 None 39 Human Functional pIC50 = 7.6 7.6 -2 14
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/acs.jmedchem.6b01119
131636393 160166 None 0 Human Functional pIC50 = 7.6 7.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 3 0 4 4.9 Cc1cc(-c2nc(-c3ccc(F)c(Cl)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
CHEMBL4108446 160166 None 0 Human Functional pIC50 = 7.6 7.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 3 0 4 4.9 Cc1cc(-c2nc(-c3ccc(F)c(Cl)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
131636442 161045 None 0 Human Functional pIC50 = 7.6 7.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 6 0 5 5.2 CCc1ccc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)cc1OCC1CC1 nan
CHEMBL4115553 161045 None 0 Human Functional pIC50 = 7.6 7.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 6 0 5 5.2 CCc1ccc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)cc1OCC1CC1 nan
18613373 96227 None 0 Rat Functional pIC50 = 6.6 6.6 - 1
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 442 5 2 6 4.8 CC(C)CNc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
CHEMBL260643 96227 None 0 Rat Functional pIC50 = 6.6 6.6 - 1
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 442 5 2 6 4.8 CC(C)CNc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
22224657 96225 None 0 Rat Functional pIC50 = 7.6 7.6 2 2
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 396 3 1 4 5.1 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccccc3F)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL260636 96225 None 0 Rat Functional pIC50 = 7.6 7.6 2 2
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 396 3 1 4 5.1 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccccc3F)cc2N1 10.1016/j.bmcl.2008.02.076
9952648 96361 None 0 Rat Functional pIC50 = 7.6 7.6 1 2
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 397 3 1 5 4.5 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1 10.1016/j.bmcl.2010.09.125
CHEMBL261288 96361 None 0 Rat Functional pIC50 = 7.6 7.6 1 2
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 397 3 1 5 4.5 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1 10.1016/j.bmcl.2010.09.125
172470330 197122 None 0 Human Functional pIC50 = 7.6 7.6 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 360 4 1 4 3.7 Cc1cnn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)c1 10.1021/acsmedchemlett.3c00210
CHEMBL5439283 197122 None 0 Human Functional pIC50 = 7.6 7.6 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 360 4 1 4 3.7 Cc1cnn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)c1 10.1021/acsmedchemlett.3c00210
131636338 148070 None 0 Human Functional pIC50 = 7.6 7.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 401 2 0 4 5.1 Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(C)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3934173 148070 None 0 Human Functional pIC50 = 7.6 7.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 401 2 0 4 5.1 Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(C)c3)n3c2CCOCC3)cc(C)n1 nan
131636432 150378 None 0 Human Functional pIC50 = 7.6 7.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 4 0 5 5.2 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(CF)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3952745 150378 None 0 Human Functional pIC50 = 7.6 7.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 4 0 5 5.2 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(CF)c3)n3c2CCOCC3)cc(C)n1 nan
69669646 183785 None 0 Human Functional pIC50 = 7.6 7.6 2 2
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 351 5 4 5 1.1 Cc1ccc(SC[C@@H]2[C@@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)cc1C 10.1021/acs.jmedchem.6b01119
CHEMBL4757159 183785 None 0 Human Functional pIC50 = 7.6 7.6 2 2
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 351 5 4 5 1.1 Cc1ccc(SC[C@@H]2[C@@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)cc1C 10.1021/acs.jmedchem.6b01119
CHEMBL4802990 183785 None 0 Human Functional pIC50 = 7.6 7.6 2 2
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 351 5 4 5 1.1 Cc1ccc(SC[C@@H]2[C@@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)cc1C 10.1021/acs.jmedchem.6b01119
131636367 146725 None 0 Human Functional pIC50 = 7.6 7.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 459 5 0 6 5.2 Cc1cc(-c2nc(-c3ccc(OC4CC4)c(OC(F)(F)F)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3923457 146725 None 0 Human Functional pIC50 = 7.6 7.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 459 5 0 6 5.2 Cc1cc(-c2nc(-c3ccc(OC4CC4)c(OC(F)(F)F)c3)n3c2CCOCC3)cc(C)n1 nan
131636357 160799 None 0 Human Functional pIC50 = 7.6 7.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 419 2 0 4 5.3 Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(F)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4113614 160799 None 0 Human Functional pIC50 = 7.6 7.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 419 2 0 4 5.3 Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(F)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
90354626 159957 None 0 Human Functional pIC50 = 7.6 7.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 401 4 0 5 4.7 COc1cc(-c2nc(-c3ccnc(CF)c3)c3n2C[C@@H](C)OCC3)ccc1Cl nan
CHEMBL4106714 159957 None 0 Human Functional pIC50 = 7.6 7.6 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 401 4 0 5 4.7 COc1cc(-c2nc(-c3ccnc(CF)c3)c3n2C[C@@H](C)OCC3)ccc1Cl nan
131636286 159990 None 0 Human Functional pIC50 = 7.5 7.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 413 4 0 6 4.6 COc1cc(-c2nc(-c3ccc(Cl)c(OC)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4106958 159990 None 0 Human Functional pIC50 = 7.5 7.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 413 4 0 6 4.6 COc1cc(-c2nc(-c3ccc(Cl)c(OC)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
131636319 154151 None 0 Human Functional pIC50 = 7.5 7.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 4 0 5 4.9 Cc1cc(-c2nc(-c3ccc(F)c(OCC(F)(F)F)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3984622 154151 None 0 Human Functional pIC50 = 7.5 7.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 4 0 5 4.9 Cc1cc(-c2nc(-c3ccc(F)c(OCC(F)(F)F)c3)n3c2CCOCC3)cc(C)n1 nan
134144441 150482 None 0 Human Functional pIC50 = 6.6 6.6 -1 2
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 341 5 4 5 0.3 N[C@@]1(C(=O)O)[C@H](OCc2cccc(Cl)c2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1016/j.bmcl.2016.10.067
CHEMBL3953570 150482 None 0 Human Functional pIC50 = 6.6 6.6 -1 2
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 341 5 4 5 0.3 N[C@@]1(C(=O)O)[C@H](OCc2cccc(Cl)c2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1016/j.bmcl.2016.10.067
44329042 169186 None 0 Rat Functional pIC50 = 5.5 5.5 -38 5
Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated
ChEMBL 381 6 3 4 3.5 CC[C@@H]1[C@H](C(=O)O)[C@H]1C(N)(CC1c2ccccc2Oc2ccccc21)C(=O)O 10.1016/s0960-894x(98)00510-1
CHEMBL439775 169186 None 0 Rat Functional pIC50 = 5.5 5.5 -38 5
Antagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluatedAntagonistic activity against metabotropic glutamate receptor 2 (mGluR2) was evaluated
ChEMBL 381 6 3 4 3.5 CC[C@@H]1[C@H](C(=O)O)[C@H]1C(N)(CC1c2ccccc2Oc2ccccc21)C(=O)O 10.1016/s0960-894x(98)00510-1
155555318 174422 None 0 Rat Functional pIC50 = 6.5 6.5 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 407 6 1 7 2.9 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccnc(C)c4)nn23)c(F)c1 10.1021/acs.jmedchem.8b01266
CHEMBL4550517 174422 None 0 Rat Functional pIC50 = 6.5 6.5 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 407 6 1 7 2.9 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccnc(C)c4)nn23)c(F)c1 10.1021/acs.jmedchem.8b01266
155555318 174422 None 0 Rat Functional pIC50 = 6.5 6.5 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 407 6 1 7 2.9 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccnc(C)c4)nn23)c(F)c1 10.1021/acs.jmedchem.8b01266
CHEMBL4550517 174422 None 0 Rat Functional pIC50 = 6.5 6.5 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 407 6 1 7 2.9 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccnc(C)c4)nn23)c(F)c1 10.1021/acs.jmedchem.8b01266
131636300 160227 None 0 Human Functional pIC50 = 7.5 7.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 381 4 0 5 4.1 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1C nan
CHEMBL4108984 160227 None 0 Human Functional pIC50 = 7.5 7.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 381 4 0 5 4.1 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1C nan
131636399 160810 None 0 Human Functional pIC50 = 7.5 7.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 429 5 1 6 4.3 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(CO)n1 nan
CHEMBL4113737 160810 None 0 Human Functional pIC50 = 7.5 7.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 429 5 1 6 4.3 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(CO)n1 nan
131636312 160398 None 0 Human Functional pIC50 = 7.5 7.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 4 0 5 4.9 C[C@@H]1Cn2c(-c3ccc(OC(F)(F)F)cc3)nc(-c3ccnc(CF)c3)c2CCO1 nan
CHEMBL4110503 160398 None 0 Human Functional pIC50 = 7.5 7.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 4 0 5 4.9 C[C@@H]1Cn2c(-c3ccc(OC(F)(F)F)cc3)nc(-c3ccnc(CF)c3)c2CCO1 nan
22224852 95917 None 0 Rat Functional pIC50 = 6.5 6.5 -2 2
Antagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK currentAntagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK current
ChEMBL 396 3 1 4 5.1 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL259054 95917 None 0 Rat Functional pIC50 = 6.5 6.5 -2 2
Antagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK currentAntagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK current
ChEMBL 396 3 1 4 5.1 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2008.02.076
11158623 3351 None 11 Rat Functional pIC50 = 8.5 8.5 1 4
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 10.1016/j.bmcl.2010.09.125
6226 3351 None 11 Rat Functional pIC50 = 8.5 8.5 1 4
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 10.1016/j.bmcl.2010.09.125
CHEMBL1629855 3351 None 11 Rat Functional pIC50 = 8.5 8.5 1 4
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 10.1016/j.bmcl.2010.09.125
11484819 56322 None 0 Rat Functional pIC50 = 8.5 8.5 2 2
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 347 2 1 3 4.9 O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(Cl)cc2N1 10.1016/j.bmcl.2010.09.125
CHEMBL1629863 56322 None 0 Rat Functional pIC50 = 8.5 8.5 2 2
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 347 2 1 3 4.9 O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(Cl)cc2N1 10.1016/j.bmcl.2010.09.125
11406781 56441 None 0 Rat Functional pIC50 = 8.5 8.5 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 395 2 1 3 5.5 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cccnc3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631876 56441 None 0 Rat Functional pIC50 = 8.5 8.5 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 395 2 1 3 5.5 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cccnc3)c1)=N2 10.1016/j.bmcl.2010.09.125
131636376 160750 None 0 Human Functional pIC50 = 8.5 8.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 437 3 0 5 5.4 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4113300 160750 None 0 Human Functional pIC50 = 8.5 8.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 437 3 0 5 5.4 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)ccn1 nan
78319946 161026 None 0 Human Functional pIC50 = 8.5 8.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 423 4 0 5 5.4 Cc1cc(-c2nc(-c3ccc(OC4CC4)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4115420 161026 None 0 Human Functional pIC50 = 8.5 8.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 423 4 0 5 5.4 Cc1cc(-c2nc(-c3ccc(OC4CC4)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
131636324 160206 None 0 Human Functional pIC50 = 8.5 8.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 5 0 5 5.5 Cc1cc(-c2nc(-c3ccc(F)c(OCC4CCC4)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4108816 160206 None 0 Human Functional pIC50 = 8.5 8.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 5 0 5 5.5 Cc1cc(-c2nc(-c3ccc(F)c(OCC4CCC4)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
78320250 160556 None 0 Human Functional pIC50 = 8.5 8.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 447 4 0 6 5.1 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1OC(F)(F)F nan
CHEMBL4111755 160556 None 0 Human Functional pIC50 = 8.5 8.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 447 4 0 6 5.1 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1OC(F)(F)F nan
78320247 160552 None 0 Human Functional pIC50 = 8.5 8.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 4 0 5 5.0 Cc1cc(-c2nc(-c3ccc(OC4CC4)c(C)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4111744 160552 None 0 Human Functional pIC50 = 8.5 8.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 4 0 5 5.0 Cc1cc(-c2nc(-c3ccc(OC4CC4)c(C)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
78324635 160560 None 0 Human Functional pIC50 = 8.5 8.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 431 5 0 5 5.1 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
CHEMBL4111773 160560 None 0 Human Functional pIC50 = 8.5 8.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 431 5 0 5 5.1 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
131636416 160989 None 0 Human Functional pIC50 = 8.4 8.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 460 4 0 6 4.9 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C#N)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
CHEMBL4115199 160989 None 0 Human Functional pIC50 = 8.4 8.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 460 4 0 6 4.9 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C#N)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
131636417 160111 None 0 Human Functional pIC50 = 8.4 8.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 446 4 0 6 4.6 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C#N)c3)n3c2CCO[C@H](CF)C3)ccn1 nan
CHEMBL4107975 160111 None 0 Human Functional pIC50 = 8.4 8.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 446 4 0 6 4.6 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C#N)c3)n3c2CCO[C@H](CF)C3)ccn1 nan
131636305 160179 None 0 Human Functional pIC50 = 8.4 8.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 397 4 0 5 4.9 CC[C@@H]1Cn2c(-c3ccc(Cl)c(OC)c3)nc(-c3ccnc(C)c3)c2CCO1 nan
CHEMBL4108564 160179 None 0 Human Functional pIC50 = 8.4 8.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 397 4 0 5 4.9 CC[C@@H]1Cn2c(-c3ccc(Cl)c(OC)c3)nc(-c3ccnc(C)c3)c2CCO1 nan
78319945 160436 None 0 Human Functional pIC50 = 8.4 8.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 451 5 0 6 4.7 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)(F)F nan
CHEMBL4110721 160436 None 0 Human Functional pIC50 = 8.4 8.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 451 5 0 6 4.7 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)(F)F nan
78319941 161036 None 0 Human Functional pIC50 = 8.4 8.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 449 4 0 5 5.2 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)(F)F nan
CHEMBL4115490 161036 None 0 Human Functional pIC50 = 8.4 8.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 449 4 0 5 5.2 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)(F)F nan
131636446 160636 None 0 Human Functional pIC50 = 8.4 8.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 391 4 0 5 4.9 CCOc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C nan
CHEMBL4112442 160636 None 0 Human Functional pIC50 = 8.4 8.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 391 4 0 5 4.9 CCOc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C nan
22317318 56440 None 0 Rat Functional pIC50 = 7.5 7.5 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 395 2 1 3 5.5 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccccn3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631875 56440 None 0 Rat Functional pIC50 = 7.5 7.5 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 395 2 1 3 5.5 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccccn3)c1)=N2 10.1016/j.bmcl.2010.09.125
131636456 159962 None 0 Human Functional pIC50 = 7.5 7.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 415 5 1 6 4.0 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(CO)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4106741 159962 None 0 Human Functional pIC50 = 7.5 7.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 415 5 1 6 4.0 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(CO)c3)n3c2CCO[C@H](C)C3)ccn1 nan
131636412 160279 None 0 Human Functional pIC50 = 7.5 7.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 429 6 1 6 3.9 Cc1cc(-c2nc(-c3ccc(OCF)c(C)c3)n3c2CCO[C@H](CF)C3)cc(CO)n1 nan
CHEMBL4109387 160279 None 0 Human Functional pIC50 = 7.5 7.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 429 6 1 6 3.9 Cc1cc(-c2nc(-c3ccc(OCF)c(C)c3)n3c2CCO[C@H](CF)C3)cc(CO)n1 nan
131636306 151351 None 0 Human Functional pIC50 = 7.5 7.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 433 4 0 5 5.1 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C(F)F)OCC3)ccc1Cl nan
CHEMBL3960280 151351 None 0 Human Functional pIC50 = 7.5 7.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 433 4 0 5 5.1 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C(F)F)OCC3)ccc1Cl nan
15392101 100493 None 0 Rat Functional pIC50 = 4.5 4.5 - 1
Antagonist activity at rat mGlu2 expressed in CHO cells assessed as inhibition of (1S,3R)-ACPD-stimulated GTPgammaS bindingAntagonist activity at rat mGlu2 expressed in CHO cells assessed as inhibition of (1S,3R)-ACPD-stimulated GTPgammaS binding
ChEMBL 517 7 0 7 5.8 COc1ccc(C2C(C(=O)OCCN(C)C)=C(C)N=C3SC(c4c(Cl)cccc4Cl)=CN32)cc1 10.1016/j.bmcl.2007.10.026
CHEMBL290509 100493 None 0 Rat Functional pIC50 = 4.5 4.5 - 1
Antagonist activity at rat mGlu2 expressed in CHO cells assessed as inhibition of (1S,3R)-ACPD-stimulated GTPgammaS bindingAntagonist activity at rat mGlu2 expressed in CHO cells assessed as inhibition of (1S,3R)-ACPD-stimulated GTPgammaS binding
ChEMBL 517 7 0 7 5.8 COc1ccc(C2C(C(=O)OCCN(C)C)=C(C)N=C3SC(c4c(Cl)cccc4Cl)=CN32)cc1 10.1016/j.bmcl.2007.10.026
4694355 98793 None 28 Rat Functional pIC50 = 4.5 4.5 - 1
Antagonistic activity against Metabotropic glutamate receptor 2 was determinedAntagonistic activity against Metabotropic glutamate receptor 2 was determined
ChEMBL 257 2 4 3 -0.3 NC1(C(=O)O)CCc2cc(P(=O)(O)O)ccc21 10.1016/S0960-894X(97)00177-7
CHEMBL277961 98793 None 28 Rat Functional pIC50 = 4.5 4.5 - 1
Antagonistic activity against Metabotropic glutamate receptor 2 was determinedAntagonistic activity against Metabotropic glutamate receptor 2 was determined
ChEMBL 257 2 4 3 -0.3 NC1(C(=O)O)CCc2cc(P(=O)(O)O)ccc21 10.1016/S0960-894X(97)00177-7
134144056 150725 None 0 Human Functional pIC50 = 6.5 6.5 -1 2
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 307 5 4 5 -0.3 N[C@@]1(C(=O)O)[C@H](OCc2ccccc2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1016/j.bmcl.2016.10.067
CHEMBL3955458 150725 None 0 Human Functional pIC50 = 6.5 6.5 -1 2
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 307 5 4 5 -0.3 N[C@@]1(C(=O)O)[C@H](OCc2ccccc2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1016/j.bmcl.2016.10.067
131636303 160899 None 0 Human Functional pIC50 = 7.5 7.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 405 3 0 4 5.1 Cc1cc(-c2nc(-c3ccc(Cl)c(Cl)c3)n3c2CCO[C@H](CF)C3)ccn1 nan
CHEMBL4114464 160899 None 0 Human Functional pIC50 = 7.5 7.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 405 3 0 4 5.1 Cc1cc(-c2nc(-c3ccc(Cl)c(Cl)c3)n3c2CCO[C@H](CF)C3)ccn1 nan
131636293 160233 None 0 Human Functional pIC50 = 7.5 7.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 3 0 5 5.1 Cc1cc(-c2nc(-c3cccc(OC(F)(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4109021 160233 None 0 Human Functional pIC50 = 7.5 7.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 3 0 5 5.1 Cc1cc(-c2nc(-c3cccc(OC(F)(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
131636343 144959 None 0 Human Functional pIC50 = 7.5 7.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 4 0 5 4.5 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(F)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3909878 144959 None 0 Human Functional pIC50 = 7.5 7.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 4 0 5 4.5 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(F)c3)n3c2CCOCC3)cc(C)n1 nan
90354563 149770 None 0 Human Functional pIC50 = 7.5 7.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 427 3 0 5 4.6 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1Br nan
CHEMBL3947609 149770 None 0 Human Functional pIC50 = 7.5 7.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 427 3 0 5 4.6 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1Br nan
44348859 16571 None 0 Human Functional pIC50 = 5.5 5.5 -15 2
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 278 6 4 4 0.7 Nc1cccc(CC[C@](N)(C(=O)O)C2C[C@@H]2C(=O)O)c1 10.1021/jm970498o
CHEMBL123842 16571 None 0 Human Functional pIC50 = 5.5 5.5 -15 2
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 278 6 4 4 0.7 Nc1cccc(CC[C@](N)(C(=O)O)C2C[C@@H]2C(=O)O)c1 10.1021/jm970498o
21309795 150912 None 0 Human Functional pIC50 = 6.5 6.5 -3 2
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 327 4 3 3 1.8 N[C@@]1(C(=O)O)[C@H](Cc2ccc(F)c(Cl)c2)C[C@H]2[C@H](C(=O)O)[C@H]21 10.1016/j.bmcl.2016.10.067
CHEMBL3956934 150912 None 0 Human Functional pIC50 = 6.5 6.5 -3 2
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 327 4 3 3 1.8 N[C@@]1(C(=O)O)[C@H](Cc2ccc(F)c(Cl)c2)C[C@H]2[C@H](C(=O)O)[C@H]21 10.1016/j.bmcl.2016.10.067
90643961 112057 None 0 Rat Functional pIC50 = 5.5 5.5 -2 2
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 382 3 0 6 3.9 COc1cccc(-c2cc3n(C)c(=O)c4ccc(-c5cccnc5)cc4n3n2)c1 10.1016/j.bmcl.2014.04.051
CHEMBL3288649 112057 None 0 Rat Functional pIC50 = 5.5 5.5 -2 2
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 382 3 0 6 3.9 COc1cccc(-c2cc3n(C)c(=O)c4ccc(-c5cccnc5)cc4n3n2)c1 10.1016/j.bmcl.2014.04.051
155538001 172448 None 0 Rat Functional pIC50 = 6.5 6.5 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 406 6 1 7 3.7 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)cc1 10.1021/acs.jmedchem.8b01266
CHEMBL4475753 172448 None 0 Rat Functional pIC50 = 6.5 6.5 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 406 6 1 7 3.7 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)cc1 10.1021/acs.jmedchem.8b01266
CHEMBL4580695 172448 None 0 Rat Functional pIC50 = 6.5 6.5 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 406 6 1 7 3.7 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)cc1 10.1021/acs.jmedchem.8b01266
155538001 172448 None 0 Rat Functional pIC50 = 6.5 6.5 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 406 6 1 7 3.7 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)cc1 10.1021/acs.jmedchem.8b01266
CHEMBL4475753 172448 None 0 Rat Functional pIC50 = 6.5 6.5 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 406 6 1 7 3.7 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)cc1 10.1021/acs.jmedchem.8b01266
CHEMBL4580695 172448 None 0 Rat Functional pIC50 = 6.5 6.5 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 406 6 1 7 3.7 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)cc1 10.1021/acs.jmedchem.8b01266
172446301 195097 None 0 Human Functional pIC50 = 5.5 5.5 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 368 4 1 6 0.8 NC(=O)c1cc(N2CCOCC2)c2ccc(CN3C(=O)CCC3=O)cc2n1 10.1021/acsmedchemlett.3c00210
CHEMBL5396638 195097 None 0 Human Functional pIC50 = 5.5 5.5 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 368 4 1 6 0.8 NC(=O)c1cc(N2CCOCC2)c2ccc(CN3C(=O)CCC3=O)cc2n1 10.1021/acsmedchemlett.3c00210
145572237 196486 None 0 Human Functional pIC50 = 7.5 7.5 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 391 5 1 6 2.3 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C5CC5)C4)ccc23)cn1 10.1021/acsmedchemlett.3c00210
CHEMBL5425066 196486 None 0 Human Functional pIC50 = 7.5 7.5 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 391 5 1 6 2.3 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C5CC5)C4)ccc23)cn1 10.1021/acsmedchemlett.3c00210
131636355 160960 None 0 Human Functional pIC50 = 7.5 7.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 2 0 4 5.6 Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4114983 160960 None 0 Human Functional pIC50 = 7.5 7.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 2 0 4 5.6 Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)ccn1 nan
131636341 148039 None 0 Human Functional pIC50 = 7.5 7.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 428 3 0 6 4.6 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C#N)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3933840 148039 None 0 Human Functional pIC50 = 7.5 7.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 428 3 0 6 4.6 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C#N)c3)n3c2CCOCC3)cc(C)n1 nan
131636359 160866 None 0 Human Functional pIC50 = 7.5 7.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 381 3 0 5 4.3 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1F nan
CHEMBL4114183 160866 None 0 Human Functional pIC50 = 7.5 7.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 381 3 0 5 4.3 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1F nan
162665071 183834 None 0 Human Functional pIC50 = 6.5 6.5 1 2
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 323 5 4 5 0.5 N[C@@]1(C(=O)O)[C@H](CSc2ccccc2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4781638 183834 None 0 Human Functional pIC50 = 6.5 6.5 1 2
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 323 5 4 5 0.5 N[C@@]1(C(=O)O)[C@H](CSc2ccccc2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4803454 183834 None 0 Human Functional pIC50 = 6.5 6.5 1 2
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 323 5 4 5 0.5 N[C@@]1(C(=O)O)[C@H](CSc2ccccc2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
18548862 158031 None 0 Rat Functional pIC50 = 7.5 7.5 - 1
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 415 4 1 6 4.1 CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
CHEMBL408455 158031 None 0 Rat Functional pIC50 = 7.5 7.5 - 1
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 415 4 1 6 4.1 CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
134137754 148036 None 0 Human Functional pIC50 = 7.5 7.5 1 2
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 400 6 3 5 2.3 [N-]=[N+]=N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1OCc1ccc(Cl)c(Cl)c1 10.1016/j.bmcl.2016.10.067
CHEMBL3933829 148036 None 0 Human Functional pIC50 = 7.5 7.5 1 2
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 400 6 3 5 2.3 [N-]=[N+]=N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1OCc1ccc(Cl)c(Cl)c1 10.1016/j.bmcl.2016.10.067
131636320 150788 None 0 Human Functional pIC50 = 7.5 7.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 407 5 0 5 4.7 Cc1cc(-c2nc(-c3ccc(F)c(OCC4CC4)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3956003 150788 None 0 Human Functional pIC50 = 7.5 7.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 407 5 0 5 4.7 Cc1cc(-c2nc(-c3ccc(F)c(OCC4CC4)c3)n3c2CCOCC3)cc(C)n1 nan
155550453 174373 None 0 Rat Functional pIC50 = 6.5 6.5 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 461 6 1 7 3.6 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccc(C(F)(F)F)nc4)nn23)c(F)c1 10.1021/acs.jmedchem.8b01266
CHEMBL4549344 174373 None 0 Rat Functional pIC50 = 6.5 6.5 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 461 6 1 7 3.6 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccc(C(F)(F)F)nc4)nn23)c(F)c1 10.1021/acs.jmedchem.8b01266
155550453 174373 None 0 Rat Functional pIC50 = 6.5 6.5 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 461 6 1 7 3.6 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccc(C(F)(F)F)nc4)nn23)c(F)c1 10.1021/acs.jmedchem.8b01266
CHEMBL4549344 174373 None 0 Rat Functional pIC50 = 6.5 6.5 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 461 6 1 7 3.6 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4ccc(C(F)(F)F)nc4)nn23)c(F)c1 10.1021/acs.jmedchem.8b01266
22448579 155868 None 0 Rat Functional pIC50 = 7.5 7.5 4 2
Antagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK currentAntagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK current
ChEMBL 412 3 2 5 4.8 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(-c3ccccc3F)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL405895 155868 None 0 Rat Functional pIC50 = 7.5 7.5 4 2
Antagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK currentAntagonist activity at rat mGluR2 expressed in CHO cells assessed as inhibition of glutamta-induced GIRK current
ChEMBL 412 3 2 5 4.8 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(-c3ccccc3F)cc2N1 10.1016/j.bmcl.2008.02.076
131636302 160115 None 0 Human Functional pIC50 = 7.5 7.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 385 3 0 4 4.8 Cc1cc(-c2nc(-c3ccc(Cl)c(C)c3)n3c2CCO[C@H](CF)C3)ccn1 nan
CHEMBL4108010 160115 None 0 Human Functional pIC50 = 7.5 7.5 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 385 3 0 4 4.8 Cc1cc(-c2nc(-c3ccc(Cl)c(C)c3)n3c2CCO[C@H](CF)C3)ccn1 nan
22224825 159086 None 0 Rat Functional pIC50 = 7.4 7.4 - 1
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 397 3 1 5 4.5 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL409638 159086 None 0 Rat Functional pIC50 = 7.4 7.4 - 1
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 397 3 1 5 4.5 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2008.02.076
11211597 56324 None 0 Rat Functional pIC50 = 7.4 7.4 -1 3
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 395 2 1 3 5.5 Cc1cc(-c2cccc(C3=Nc4ccc(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
CHEMBL1629865 56324 None 0 Rat Functional pIC50 = 7.4 7.4 -1 3
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 395 2 1 3 5.5 Cc1cc(-c2cccc(C3=Nc4ccc(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
131636347 143098 None 0 Human Functional pIC50 = 7.4 7.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 3 0 5 4.5 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2CCOCC3)ccc1C(F)(F)F nan
CHEMBL3894707 143098 None 0 Human Functional pIC50 = 7.4 7.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 3 0 5 4.5 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2CCOCC3)ccc1C(F)(F)F nan
131636457 160643 None 0 Human Functional pIC50 = 7.4 7.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 399 3 0 4 5.3 Cc1cc(-c2nc(-c3ccc(Cl)c(CF)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4112521 160643 None 0 Human Functional pIC50 = 7.4 7.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 399 3 0 4 5.3 Cc1cc(-c2nc(-c3ccc(Cl)c(CF)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
131636386 161056 None 0 Human Functional pIC50 = 7.4 7.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 433 6 0 6 4.4 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)F nan
CHEMBL4115662 161056 None 0 Human Functional pIC50 = 7.4 7.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 433 6 0 6 4.4 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)F nan
131636358 149094 None 0 Human Functional pIC50 = 7.4 7.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 409 4 0 5 5.0 Cc1cc(-c2nc(-c3ccc(OC4CC4)c(Cl)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3942377 149094 None 0 Human Functional pIC50 = 7.4 7.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 409 4 0 5 5.0 Cc1cc(-c2nc(-c3ccc(OC4CC4)c(Cl)c3)n3c2CCOCC3)cc(C)n1 nan
44302608 100900 None 0 Human Functional pIC50 = 4.4 4.4 -2 2
In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.
ChEMBL 340 5 3 4 1.8 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2-c2ccccc2)C1 10.1016/s0960-894x(98)00352-7
CHEMBL293434 100900 None 0 Human Functional pIC50 = 4.4 4.4 -2 2
In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.
ChEMBL 340 5 3 4 1.8 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2-c2ccccc2)C1 10.1016/s0960-894x(98)00352-7
155531624 171776 None 0 Rat Functional pIC50 = 5.4 5.4 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 387 4 1 5 3.8 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCSCC3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4466304 171776 None 0 Rat Functional pIC50 = 5.4 5.4 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 387 4 1 5 3.8 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCSCC3)cc2n1 10.1021/acs.jmedchem.8b01266
155531624 171776 None 0 Rat Functional pIC50 = 5.4 5.4 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 387 4 1 5 3.8 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCSCC3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4466304 171776 None 0 Rat Functional pIC50 = 5.4 5.4 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 387 4 1 5 3.8 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCSCC3)cc2n1 10.1021/acs.jmedchem.8b01266
9952648 96361 None 0 Rat Functional pIC50 = 7.4 7.4 1 2
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 397 3 1 5 4.5 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL261288 96361 None 0 Rat Functional pIC50 = 7.4 7.4 1 2
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 397 3 1 5 4.5 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1 10.1016/j.bmcl.2008.02.076
172444897 195197 None 0 Human Functional pIC50 = 7.4 7.4 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 379 4 1 3 3.5 CN(C)C(=O)C(C)(C)c1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 10.1021/acsmedchemlett.3c00210
CHEMBL5398558 195197 None 0 Human Functional pIC50 = 7.4 7.4 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 379 4 1 3 3.5 CN(C)C(=O)C(C)(C)c1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 10.1021/acsmedchemlett.3c00210
131636291 160380 None 0 Human Functional pIC50 = 7.4 7.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 367 2 0 4 4.8 Cc1cc(-c2nc(-c3cccc(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4110331 160380 None 0 Human Functional pIC50 = 7.4 7.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 367 2 0 4 4.8 Cc1cc(-c2nc(-c3cccc(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
44302856 102786 None 0 Human Functional pIC50 = 4.4 4.4 1 2
In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.
ChEMBL 354 6 3 4 1.8 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(CC(c2ccccc2)c2ccccc2)C1 10.1016/s0960-894x(98)00352-7
CHEMBL304919 102786 None 0 Human Functional pIC50 = 4.4 4.4 1 2
In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.
ChEMBL 354 6 3 4 1.8 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(CC(c2ccccc2)c2ccccc2)C1 10.1016/s0960-894x(98)00352-7
11235624 56321 None 0 Human Functional pIC50 = 7.4 7.4 -6 3
Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 425 4 1 4 5.6 CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncc3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1629862 56321 None 0 Human Functional pIC50 = 7.4 7.4 -6 3
Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 425 4 1 4 5.6 CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncc3)c1)=N2 10.1016/j.bmcl.2010.09.125
131636394 160672 None 0 Human Functional pIC50 = 7.4 7.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 389 3 0 4 4.6 Cc1cc(-c2nc(-c3ccc(F)c(Cl)c3)n3c2CCO[C@H](CF)C3)ccn1 nan
CHEMBL4112680 160672 None 0 Human Functional pIC50 = 7.4 7.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 389 3 0 4 4.6 Cc1cc(-c2nc(-c3ccc(F)c(Cl)c3)n3c2CCO[C@H](CF)C3)ccn1 nan
131636398 160338 None 0 Human Functional pIC50 = 7.4 7.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 451 5 0 5 5.4 COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](CF)OCC3)ccc1Cl nan
CHEMBL4109944 160338 None 0 Human Functional pIC50 = 7.4 7.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 451 5 0 5 5.4 COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](CF)OCC3)ccc1Cl nan
134152341 153552 None 0 Human Functional pIC50 = 6.4 6.4 -2 2
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 375 5 4 5 1.0 N[C@@]1(C(=O)O)[C@H](OCc2cc(Cl)ccc2Cl)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1016/j.bmcl.2016.10.067
CHEMBL3979475 153552 None 0 Human Functional pIC50 = 6.4 6.4 -2 2
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 375 5 4 5 1.0 N[C@@]1(C(=O)O)[C@H](OCc2cc(Cl)ccc2Cl)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1016/j.bmcl.2016.10.067
155542028 173194 None 0 Rat Functional pIC50 = 5.4 5.4 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 371 4 1 5 3.0 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCOCC3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4520084 173194 None 0 Rat Functional pIC50 = 5.4 5.4 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 371 4 1 5 3.0 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCOCC3)cc2n1 10.1021/acs.jmedchem.8b01266
155542028 173194 None 0 Rat Functional pIC50 = 5.4 5.4 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 371 4 1 5 3.0 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCOCC3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4520084 173194 None 0 Rat Functional pIC50 = 5.4 5.4 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 371 4 1 5 3.0 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCOCC3)cc2n1 10.1021/acs.jmedchem.8b01266
18548824 157828 None 0 Rat Functional pIC50 = 7.4 7.4 - 1
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 385 2 1 5 4.1 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
CHEMBL408229 157828 None 0 Rat Functional pIC50 = 7.4 7.4 - 1
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 385 2 1 5 4.1 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
18548824 157828 None 0 Rat Functional pIC50 = 7.4 7.4 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 385 2 1 5 4.1 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL408229 157828 None 0 Rat Functional pIC50 = 7.4 7.4 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 385 2 1 5 4.1 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2010.09.125
90643966 112061 None 0 Rat Functional pIC50 = 5.4 5.4 -1 2
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 448 3 1 6 3.3 Cn1c(=O)c2ccc(-c3cccc(S(N)(=O)=O)c3)cc2n2nc(-c3ccc(F)cc3)cc12 10.1016/j.bmcl.2014.04.051
CHEMBL3288660 112061 None 0 Rat Functional pIC50 = 5.4 5.4 -1 2
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 448 3 1 6 3.3 Cn1c(=O)c2ccc(-c3cccc(S(N)(=O)=O)c3)cc2n2nc(-c3ccc(F)cc3)cc12 10.1016/j.bmcl.2014.04.051
11351088 56314 None 0 Rat Functional pIC50 = 8.4 8.4 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 437 3 1 3 6.4 CCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C)n1 10.1016/j.bmcl.2010.09.125
CHEMBL1629856 56314 None 0 Rat Functional pIC50 = 8.4 8.4 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 437 3 1 3 6.4 CCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C)n1 10.1016/j.bmcl.2010.09.125
22317928 56315 None 0 Rat Functional pIC50 = 8.4 8.4 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 449 3 1 3 6.7 Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C2CC2)n1 10.1016/j.bmcl.2010.09.125
CHEMBL1629857 56315 None 0 Rat Functional pIC50 = 8.4 8.4 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 449 3 1 3 6.7 Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C2CC2)n1 10.1016/j.bmcl.2010.09.125
11281280 56424 None 0 Rat Functional pIC50 = 8.4 8.4 1 3
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 409 2 1 3 5.8 Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
CHEMBL1631859 56424 None 0 Rat Functional pIC50 = 8.4 8.4 1 3
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 409 2 1 3 5.8 Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
71566598 142777 None 16 Human Functional pIC50 = 8.4 8.4 2 3
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 377 4 1 4 2.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1 10.1021/acsmedchemlett.3c00210
CHEMBL3892073 142777 None 16 Human Functional pIC50 = 8.4 8.4 2 3
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 377 4 1 4 2.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1 10.1021/acsmedchemlett.3c00210
131636425 160579 None 0 Human Functional pIC50 = 8.4 8.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 449 4 0 5 5.6 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(CF)n1 nan
CHEMBL4111952 160579 None 0 Human Functional pIC50 = 8.4 8.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 449 4 0 5 5.6 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(CF)n1 nan
131636383 160836 None 0 Human Functional pIC50 = 8.4 8.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 449 4 0 5 5.3 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
CHEMBL4113929 160836 None 0 Human Functional pIC50 = 8.4 8.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 449 4 0 5 5.3 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
69669747 183759 None 14 Human Functional pIC50 = 8.4 8.4 -2 4
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assay
ChEMBL 359 5 4 5 0.8 N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)c(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4751065 183759 None 14 Human Functional pIC50 = 8.4 8.4 -2 4
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assay
ChEMBL 359 5 4 5 0.8 N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)c(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4802733 183759 None 14 Human Functional pIC50 = 8.4 8.4 -2 4
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assay
ChEMBL 359 5 4 5 0.8 N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)c(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
78320560 160014 None 0 Human Functional pIC50 = 8.4 8.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 4 0 5 4.9 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)(F)F nan
CHEMBL4107140 160014 None 0 Human Functional pIC50 = 8.4 8.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 4 0 5 4.9 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)(F)F nan
78320248 160840 None 0 Human Functional pIC50 = 8.4 8.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 5 0 5 5.0 Cc1cc(-c2nc(-c3ccc(OC4CC4)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
CHEMBL4113962 160840 None 0 Human Functional pIC50 = 8.4 8.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 5 0 5 5.0 Cc1cc(-c2nc(-c3ccc(OC4CC4)c(C)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
131636390 160176 None 0 Human Functional pIC50 = 8.4 8.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 442 3 0 6 5.0 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C#N)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4108541 160176 None 0 Human Functional pIC50 = 8.4 8.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 442 3 0 6 5.0 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C#N)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
77461009 160391 None 0 Human Functional pIC50 = 8.4 8.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 431 3 0 5 5.2 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)(F)F nan
CHEMBL4110444 160391 None 0 Human Functional pIC50 = 8.4 8.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 431 3 0 5 5.2 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)(F)F nan
90354889 160797 None 0 Human Functional pIC50 = 8.4 8.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 391 4 0 5 4.8 CCc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1OC nan
CHEMBL4113601 160797 None 0 Human Functional pIC50 = 8.4 8.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 391 4 0 5 4.8 CCc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1OC nan
131636421 160064 None 0 Human Functional pIC50 = 8.4 8.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 449 4 0 5 5.4 COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)(F)F nan
CHEMBL4107565 160064 None 0 Human Functional pIC50 = 8.4 8.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 449 4 0 5 5.4 COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)(F)F nan
131636313 160695 None 0 Human Functional pIC50 = 8.4 8.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 4 0 5 5.3 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCO[C@H](C)C3)cc(CF)n1 nan
CHEMBL4112898 160695 None 0 Human Functional pIC50 = 8.4 8.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 4 0 5 5.3 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCO[C@H](C)C3)cc(CF)n1 nan
131636356 160863 None 0 Human Functional pIC50 = 8.4 8.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 451 3 0 5 5.7 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4114150 160863 None 0 Human Functional pIC50 = 8.4 8.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 451 3 0 5 5.7 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
131636348 159956 None 0 Human Functional pIC50 = 8.4 8.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 415 2 0 4 5.5 Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4106709 159956 None 0 Human Functional pIC50 = 8.4 8.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 415 2 0 4 5.5 Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
131636391 160202 None 0 Human Functional pIC50 = 8.3 8.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 428 3 0 6 4.7 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C#N)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4108785 160202 None 0 Human Functional pIC50 = 8.3 8.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 428 3 0 6 4.7 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C#N)c3)n3c2CCO[C@H](C)C3)ccn1 nan
131636431 160381 None 0 Human Functional pIC50 = 8.3 8.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 465 5 0 6 5.3 COc1ccc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](C)OCC3)cc1OC(F)(F)F nan
CHEMBL4110332 160381 None 0 Human Functional pIC50 = 8.3 8.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 465 5 0 6 5.3 COc1ccc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](C)OCC3)cc1OC(F)(F)F nan
131636429 160694 None 0 Human Functional pIC50 = 8.3 8.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 5 0 5 5.2 Cc1cc(-c2nc(-c3ccc(OC4CC4)c(C)c3)n3c2CCO[C@H](C)C3)cc(CF)n1 nan
CHEMBL4112889 160694 None 0 Human Functional pIC50 = 8.3 8.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 5 0 5 5.2 Cc1cc(-c2nc(-c3ccc(OC4CC4)c(C)c3)n3c2CCO[C@H](C)C3)cc(CF)n1 nan
78320559 160997 None 0 Human Functional pIC50 = 8.3 8.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 5 0 5 4.7 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)ccn1 nan
CHEMBL4115237 160997 None 0 Human Functional pIC50 = 8.3 8.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 5 0 5 4.7 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)ccn1 nan
131636295 161022 None 0 Human Functional pIC50 = 8.3 8.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 431 3 0 5 5.4 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4115390 161022 None 0 Human Functional pIC50 = 8.3 8.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 431 3 0 5 5.4 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
78320249 160358 None 0 Human Functional pIC50 = 8.3 8.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 433 4 0 6 4.8 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1OC(F)(F)F nan
CHEMBL4110153 160358 None 0 Human Functional pIC50 = 8.3 8.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 433 4 0 6 4.8 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1OC(F)(F)F nan
131636424 159995 None 0 Human Functional pIC50 = 8.3 8.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 460 4 0 6 5.1 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C#N)c3)n3c2CCO[C@H](C)C3)cc(CF)n1 nan
CHEMBL4106969 159995 None 0 Human Functional pIC50 = 8.3 8.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 460 4 0 6 5.1 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C#N)c3)n3c2CCO[C@H](C)C3)cc(CF)n1 nan
172457014 196336 None 0 Human Functional pIC50 = 7.4 7.4 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 421 4 1 4 3.3 CC(C)(C(=O)N1CCOCC1)c1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 10.1021/acsmedchemlett.3c00210
CHEMBL5421645 196336 None 0 Human Functional pIC50 = 7.4 7.4 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 421 4 1 4 3.3 CC(C)(C(=O)N1CCOCC1)c1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 10.1021/acsmedchemlett.3c00210
131636279 143812 None 0 Human Functional pIC50 = 7.4 7.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 437 3 0 5 5.4 Cc1cc(-c2nc(-c3ccc(Cl)c(OC(F)(F)F)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3900589 143812 None 0 Human Functional pIC50 = 7.4 7.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 437 3 0 5 5.4 Cc1cc(-c2nc(-c3ccc(Cl)c(OC(F)(F)F)c3)n3c2CCOCC3)cc(C)n1 nan
131636345 144202 None 0 Human Functional pIC50 = 7.4 7.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 399 4 0 5 4.7 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1C(F)F nan
CHEMBL3903640 144202 None 0 Human Functional pIC50 = 7.4 7.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 399 4 0 5 4.7 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1C(F)F nan
172443676 195479 None 0 Human Functional pIC50 = 5.4 5.4 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 378 4 1 5 1.7 CN1CC=C(c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)CC1 10.1021/acsmedchemlett.3c00210
CHEMBL5404496 195479 None 0 Human Functional pIC50 = 5.4 5.4 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 378 4 1 5 1.7 CN1CC=C(c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)CC1 10.1021/acsmedchemlett.3c00210
21309795 150912 None 0 Human Functional pIC50 = 6.4 6.4 -3 2
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 327 4 3 3 1.8 N[C@@]1(C(=O)O)[C@H](Cc2ccc(F)c(Cl)c2)C[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.6b01119
CHEMBL3956934 150912 None 0 Human Functional pIC50 = 6.4 6.4 -3 2
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 327 4 3 3 1.8 N[C@@]1(C(=O)O)[C@H](Cc2ccc(F)c(Cl)c2)C[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.6b01119
11281280 56424 None 0 Human Functional pIC50 = 7.4 7.4 -5 3
Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 409 2 1 3 5.8 Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
CHEMBL1631859 56424 None 0 Human Functional pIC50 = 7.4 7.4 -5 3
Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 409 2 1 3 5.8 Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
172454000 195655 None 0 Human Functional pIC50 = 7.4 7.4 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 380 4 1 6 2.4 Cc1ncc(-c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)s1 10.1021/acsmedchemlett.3c00210
CHEMBL5408200 195655 None 0 Human Functional pIC50 = 7.4 7.4 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 380 4 1 6 2.4 Cc1ncc(-c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)s1 10.1021/acsmedchemlett.3c00210
172460014 196241 None 0 Human Functional pIC50 = 7.4 7.4 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 433 4 1 4 4.1 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(C(N3CCOCC3)C(F)(F)F)cc2n1 10.1021/acsmedchemlett.3c00210
CHEMBL5419543 196241 None 0 Human Functional pIC50 = 7.4 7.4 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 433 4 1 4 4.1 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(C(N3CCOCC3)C(F)(F)F)cc2n1 10.1021/acsmedchemlett.3c00210
131636287 160604 None 0 Human Functional pIC50 = 7.4 7.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 371 2 0 4 4.7 Cc1cc(-c2nc(-c3ccc(Cl)c(F)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4112202 160604 None 0 Human Functional pIC50 = 7.4 7.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 371 2 0 4 4.7 Cc1cc(-c2nc(-c3ccc(Cl)c(F)c3)n3c2CCO[C@H](C)C3)ccn1 nan
131636411 160597 None 0 Human Functional pIC50 = 7.4 7.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 433 4 0 5 5.5 COc1ccc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](C)OCC3)cc1Cl nan
CHEMBL4112136 160597 None 0 Human Functional pIC50 = 7.4 7.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 433 4 0 5 5.5 COc1ccc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](C)OCC3)cc1Cl nan
44302686 203373 None 0 Human Functional pIC50 = 4.4 4.4 -1 2
In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.
ChEMBL 332 4 3 4 1.4 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2c(Cl)cccc2Cl)C1 10.1016/s0960-894x(98)00352-7
CHEMBL60164 203373 None 0 Human Functional pIC50 = 4.4 4.4 -1 2
In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.
ChEMBL 332 4 3 4 1.4 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2c(Cl)cccc2Cl)C1 10.1016/s0960-894x(98)00352-7
155540306 173002 None 0 Rat Functional pIC50 = 6.4 6.4 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 424 6 1 7 3.9 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)c(F)c1 10.1021/acs.jmedchem.8b01266
CHEMBL4516001 173002 None 0 Rat Functional pIC50 = 6.4 6.4 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 424 6 1 7 3.9 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)c(F)c1 10.1021/acs.jmedchem.8b01266
90643968 112062 None 0 Rat Functional pIC50 = 6.4 6.4 -6 2
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 370 2 0 5 4.1 Cn1c(=O)c2ccc(-c3cccnc3)cc2n2nc(-c3ccc(F)cc3)cc12 10.1016/j.bmcl.2014.04.051
CHEMBL3288662 112062 None 0 Rat Functional pIC50 = 6.4 6.4 -6 2
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 370 2 0 5 4.1 Cn1c(=O)c2ccc(-c3cccnc3)cc2n2nc(-c3ccc(F)cc3)cc12 10.1016/j.bmcl.2014.04.051
155540306 173002 None 0 Rat Functional pIC50 = 6.4 6.4 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 424 6 1 7 3.9 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)c(F)c1 10.1021/acs.jmedchem.8b01266
CHEMBL4516001 173002 None 0 Rat Functional pIC50 = 6.4 6.4 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 424 6 1 7 3.9 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)c(F)c1 10.1021/acs.jmedchem.8b01266
123641156 196451 None 0 Human Functional pIC50 = 7.4 7.4 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 379 4 1 4 3.4 CC1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CCO1 10.1021/acsmedchemlett.3c00210
CHEMBL5424217 196451 None 0 Human Functional pIC50 = 7.4 7.4 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 379 4 1 4 3.4 CC1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CCO1 10.1021/acsmedchemlett.3c00210
131636392 160412 None 0 Human Functional pIC50 = 7.4 7.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 469 5 1 6 4.4 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](CF)C3)cc(CO)n1 nan
CHEMBL4110601 160412 None 0 Human Functional pIC50 = 7.4 7.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 469 5 1 6 4.4 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](CF)C3)cc(CO)n1 nan
44348939 118558 None 0 Human Functional pIC50 = 6.4 6.4 -2 2
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 293 7 3 4 1.1 COc1cccc(CC[C@](N)(C(=O)O)C2C[C@@H]2C(=O)O)c1 10.1021/jm970498o
CHEMBL341457 118558 None 0 Human Functional pIC50 = 6.4 6.4 -2 2
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 293 7 3 4 1.1 COc1cccc(CC[C@](N)(C(=O)O)C2C[C@@H]2C(=O)O)c1 10.1021/jm970498o
1373 2475 None 35 Human Functional pIC50 = 5.4 5.4 -1 4
Antagonist activity at mGlu2 receptorAntagonist activity at mGlu2 receptor
ChEMBL 209 3 3 3 0.6 OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C 10.1021/jm060950g
139055582 2475 None 35 Human Functional pIC50 = 5.4 5.4 -1 4
Antagonist activity at mGlu2 receptorAntagonist activity at mGlu2 receptor
ChEMBL 209 3 3 3 0.6 OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C 10.1021/jm060950g
446355 2475 None 35 Human Functional pIC50 = 5.4 5.4 -1 4
Antagonist activity at mGlu2 receptorAntagonist activity at mGlu2 receptor
ChEMBL 209 3 3 3 0.6 OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C 10.1021/jm060950g
CHEMBL257626 2475 None 35 Human Functional pIC50 = 5.4 5.4 -1 4
Antagonist activity at mGlu2 receptorAntagonist activity at mGlu2 receptor
ChEMBL 209 3 3 3 0.6 OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C 10.1021/jm060950g
DB04256 2475 None 35 Human Functional pIC50 = 5.4 5.4 -1 4
Antagonist activity at mGlu2 receptorAntagonist activity at mGlu2 receptor
ChEMBL 209 3 3 3 0.6 OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C 10.1021/jm060950g
11777615 98915 None 0 Rat Functional pIC50 = 4.4 4.4 2 2
Antagonistic activity against Metabotropic glutamate receptor 2 was determinedAntagonistic activity against Metabotropic glutamate receptor 2 was determined
ChEMBL 265 2 3 4 1.2 CC1(C)CC(N)(C(=O)O)c2ccc(C(=O)O)cc2O1 10.1016/S0960-894X(97)00177-7
CHEMBL278949 98915 None 0 Rat Functional pIC50 = 4.4 4.4 2 2
Antagonistic activity against Metabotropic glutamate receptor 2 was determinedAntagonistic activity against Metabotropic glutamate receptor 2 was determined
ChEMBL 265 2 3 4 1.2 CC1(C)CC(N)(C(=O)O)c2ccc(C(=O)O)cc2O1 10.1016/S0960-894X(97)00177-7
10783272 86156 None 0 Human Functional pIC50 = 5.4 5.4 -15 2
Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2
ChEMBL 339 7 3 3 2.7 N[C@@](CC(c1ccccc1)c1ccccc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970497w
CHEMBL2311086 86156 None 0 Human Functional pIC50 = 5.4 5.4 -15 2
Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2
ChEMBL 339 7 3 3 2.7 N[C@@](CC(c1ccccc1)c1ccccc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970497w
131636380 160812 None 0 Human Functional pIC50 = 7.4 7.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 3 0 5 4.9 Cc1cc(-c2nc(-c3ccc(F)c(OC(F)(F)F)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4113748 160812 None 0 Human Functional pIC50 = 7.4 7.4 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 3 0 5 4.9 Cc1cc(-c2nc(-c3ccc(F)c(OC(F)(F)F)c3)n3c2CCO[C@H](C)C3)ccn1 nan
155538001 172448 None 0 Rat Functional pIC50 = 6.4 6.4 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 406 6 1 7 3.7 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)cc1 10.1021/acs.jmedchem.8b01266
CHEMBL4475753 172448 None 0 Rat Functional pIC50 = 6.4 6.4 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 406 6 1 7 3.7 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)cc1 10.1021/acs.jmedchem.8b01266
CHEMBL4580695 172448 None 0 Rat Functional pIC50 = 6.4 6.4 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 406 6 1 7 3.7 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)cc1 10.1021/acs.jmedchem.8b01266
155538001 172448 None 0 Rat Functional pIC50 = 6.4 6.4 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 406 6 1 7 3.7 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)cc1 10.1021/acs.jmedchem.8b01266
CHEMBL4475753 172448 None 0 Rat Functional pIC50 = 6.4 6.4 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 406 6 1 7 3.7 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)cc1 10.1021/acs.jmedchem.8b01266
CHEMBL4580695 172448 None 0 Rat Functional pIC50 = 6.4 6.4 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 406 6 1 7 3.7 COc1ccc(-c2cc(C(N)=O)nc3cc(COc4cnc(C)nc4)sc23)cc1 10.1021/acs.jmedchem.8b01266
131636274 144726 None 0 Human Functional pIC50 = 7.3 7.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 3 0 5 4.7 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3908096 144726 None 0 Human Functional pIC50 = 7.3 7.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 3 0 5 4.7 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCOCC3)cc(C)n1 nan
69669702 183781 None 0 Human Functional pIC50 = 7.3 7.3 3 2
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 354 5 4 5 0.9 Cc1cc(SC[C@@H]2[C@@H](N)[C@H]3[C@H](C(=O)O)[C@H]3[C@]2(N)C(=O)O)ccc1F 10.1021/acs.jmedchem.6b01119
CHEMBL4756556 183781 None 0 Human Functional pIC50 = 7.3 7.3 3 2
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 354 5 4 5 0.9 Cc1cc(SC[C@@H]2[C@@H](N)[C@H]3[C@H](C(=O)O)[C@H]3[C@]2(N)C(=O)O)ccc1F 10.1021/acs.jmedchem.6b01119
CHEMBL4802948 183781 None 0 Human Functional pIC50 = 7.3 7.3 3 2
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 354 5 4 5 0.9 Cc1cc(SC[C@@H]2[C@@H](N)[C@H]3[C@H](C(=O)O)[C@H]3[C@]2(N)C(=O)O)ccc1F 10.1021/acs.jmedchem.6b01119
131636368 160181 None 0 Human Functional pIC50 = 7.3 7.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 371 2 0 4 4.7 Cc1cc(-c2nc(-c3ccc(F)c(Cl)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4108571 160181 None 0 Human Functional pIC50 = 7.3 7.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 371 2 0 4 4.7 Cc1cc(-c2nc(-c3ccc(F)c(Cl)c3)n3c2CCO[C@H](C)C3)ccn1 nan
10732318 78774 None 0 Human Functional pIC50 = 6.4 6.4 6 2
Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2
ChEMBL 291 8 3 3 1.9 NC(CCCCc1ccccc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970497w
CHEMBL2112585 78774 None 0 Human Functional pIC50 = 6.4 6.4 6 2
Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2
ChEMBL 291 8 3 3 1.9 NC(CCCCc1ccccc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970497w
10385210 13037 None 0 Rat Functional pIC50 = 4.4 4.4 2 3
Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2
ChEMBL 309 5 3 6 0.0 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2cccc([N+](=O)[O-])c2)C1 10.1016/s0960-894x(01)00329-8
CHEMBL1189910 13037 None 0 Rat Functional pIC50 = 4.4 4.4 2 3
Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2
ChEMBL 309 5 3 6 0.0 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2cccc([N+](=O)[O-])c2)C1 10.1016/s0960-894x(01)00329-8
CHEMBL539760 13037 None 0 Rat Functional pIC50 = 4.4 4.4 2 3
Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2
ChEMBL 309 5 3 6 0.0 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2cccc([N+](=O)[O-])c2)C1 10.1016/s0960-894x(01)00329-8
10250423 13018 None 0 Rat Functional pIC50 = 4.4 4.4 -1 2
Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2; Maximum inhibition reached only 50%Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2; Maximum inhibition reached only 50%
ChEMBL 364 4 3 4 1.5 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2C#Cc2ccccc2)C1 10.1016/s0960-894x(01)00329-8
CHEMBL1189797 13018 None 0 Rat Functional pIC50 = 4.4 4.4 -1 2
Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2; Maximum inhibition reached only 50%Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2; Maximum inhibition reached only 50%
ChEMBL 364 4 3 4 1.5 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2C#Cc2ccccc2)C1 10.1016/s0960-894x(01)00329-8
CHEMBL539516 13018 None 0 Rat Functional pIC50 = 4.4 4.4 -1 2
Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2; Maximum inhibition reached only 50%Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2; Maximum inhibition reached only 50%
ChEMBL 364 4 3 4 1.5 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2C#Cc2ccccc2)C1 10.1016/s0960-894x(01)00329-8
57338826 149715 None 0 Human Functional pIC50 = 7.3 7.3 1 5
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 375 5 4 5 1.0 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1016/j.bmcl.2016.10.067
CHEMBL3947221 149715 None 0 Human Functional pIC50 = 7.3 7.3 1 5
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 375 5 4 5 1.0 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1016/j.bmcl.2016.10.067
131636459 160949 None 0 Human Functional pIC50 = 7.3 7.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 413 4 0 5 5.0 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(C)(F)F nan
CHEMBL4114912 160949 None 0 Human Functional pIC50 = 7.3 7.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 413 4 0 5 5.0 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(C)(F)F nan
44302931 163365 None 0 Human Functional pIC50 = 4.3 4.3 - 1
In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.
ChEMBL 270 4 3 4 0.5 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(CC2CCCCC2)C1 10.1016/s0960-894x(98)00352-7
CHEMBL418650 163365 None 0 Human Functional pIC50 = 4.3 4.3 - 1
In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.
ChEMBL 270 4 3 4 0.5 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(CC2CCCCC2)C1 10.1016/s0960-894x(98)00352-7
90643973 112065 None 0 Rat Functional pIC50 = 5.3 5.3 -1 2
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 382 4 1 6 3.4 O=c1c2ccc(-c3cccnc3)cc2n2nc(-c3ccccc3)cc2n1CCO 10.1016/j.bmcl.2014.04.051
CHEMBL3288674 112065 None 0 Rat Functional pIC50 = 5.3 5.3 -1 2
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 382 4 1 6 3.4 O=c1c2ccc(-c3cccnc3)cc2n2nc(-c3ccccc3)cc2n1CCO 10.1016/j.bmcl.2014.04.051
22224570 95968 None 0 Rat Functional pIC50 = 7.3 7.3 - 1
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 378 3 1 4 5.0 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccccc3)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL259269 95968 None 0 Rat Functional pIC50 = 7.3 7.3 - 1
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 378 3 1 4 5.0 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccccc3)cc2N1 10.1016/j.bmcl.2008.02.076
131636344 148402 None 0 Human Functional pIC50 = 7.3 7.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 389 4 0 5 4.2 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(F)c3)n3c2CCOCC3)ccn1 nan
CHEMBL3936936 148402 None 0 Human Functional pIC50 = 7.3 7.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 389 4 0 5 4.2 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(F)c3)n3c2CCOCC3)ccn1 nan
131636362 160106 None 0 Human Functional pIC50 = 7.3 7.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 405 2 0 4 5.0 Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(F)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4107924 160106 None 0 Human Functional pIC50 = 7.3 7.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 405 2 0 4 5.0 Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(F)c3)n3c2CCO[C@H](C)C3)ccn1 nan
22317491 56312 None 0 Rat Functional pIC50 = 7.3 7.3 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 396 2 1 4 4.9 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cncnc3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1629853 56312 None 0 Rat Functional pIC50 = 7.3 7.3 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 396 2 1 4 4.9 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cncnc3)c1)=N2 10.1016/j.bmcl.2010.09.125
131636437 144093 None 0 Human Functional pIC50 = 7.3 7.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 397 4 0 5 4.9 CCOc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)cc1Cl nan
CHEMBL3902842 144093 None 0 Human Functional pIC50 = 7.3 7.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 397 4 0 5 4.9 CCOc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)cc1Cl nan
1297 170355 None 23 Human Functional pIC50 = 4.3 4.3 -1 2
Ability to inhibit mGluR2-alpha induced cAMP formation was determined at BHK cells at 100 Micro M ConcentrationAbility to inhibit mGluR2-alpha induced cAMP formation was determined at BHK cells at 100 Micro M Concentration
ChEMBL 211 3 4 4 0.2 NC(C(=O)O)c1ccc(C(=O)O)c(O)c1 10.1021/jm00019a002
CHEMBL444589 170355 None 23 Human Functional pIC50 = 4.3 4.3 -1 2
Ability to inhibit mGluR2-alpha induced cAMP formation was determined at BHK cells at 100 Micro M ConcentrationAbility to inhibit mGluR2-alpha induced cAMP formation was determined at BHK cells at 100 Micro M Concentration
ChEMBL 211 3 4 4 0.2 NC(C(=O)O)c1ccc(C(=O)O)c(O)c1 10.1021/jm00019a002
162658340 183792 None 0 Human Functional pIC50 = 7.3 7.3 1 2
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 405 6 4 5 1.9 N[C@@]1(C(=O)O)[C@H](CSCc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4760856 183792 None 0 Human Functional pIC50 = 7.3 7.3 1 2
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 405 6 4 5 1.9 N[C@@]1(C(=O)O)[C@H](CSCc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4803084 183792 None 0 Human Functional pIC50 = 7.3 7.3 1 2
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 405 6 4 5 1.9 N[C@@]1(C(=O)O)[C@H](CSCc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
131636321 149453 None 0 Human Functional pIC50 = 7.3 7.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 409 5 0 5 5.0 Cc1cc(-c2nc(-c3ccc(F)c(OCC(C)C)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3945334 149453 None 0 Human Functional pIC50 = 7.3 7.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 409 5 0 5 5.0 Cc1cc(-c2nc(-c3ccc(F)c(OCC(C)C)c3)n3c2CCOCC3)cc(C)n1 nan
70051296 90092 None 0 Human Functional pIC50 = 5.3 5.3 -1 3
Antagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assay
ChEMBL 242 3 4 4 -1.4 CC(=O)N[C@@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]21 10.1021/jm4000165
CHEMBL2381648 90092 None 0 Human Functional pIC50 = 5.3 5.3 -1 3
Antagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assay
ChEMBL 242 3 4 4 -1.4 CC(=O)N[C@@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]21 10.1021/jm4000165
22317724 56304 None 0 Rat Functional pIC50 = 8.3 8.3 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 409 2 1 3 5.8 Cc1ccc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cn1 10.1016/j.bmcl.2010.09.125
CHEMBL1629845 56304 None 0 Rat Functional pIC50 = 8.3 8.3 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 409 2 1 3 5.8 Cc1ccc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cn1 10.1016/j.bmcl.2010.09.125
53317987 56317 None 0 Rat Functional pIC50 = 8.3 8.3 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 453 4 1 4 6.0 COCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C)n1 10.1016/j.bmcl.2010.09.125
CHEMBL1629859 56317 None 0 Rat Functional pIC50 = 8.3 8.3 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 453 4 1 4 6.0 COCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C)n1 10.1016/j.bmcl.2010.09.125
11362246 56425 None 0 Rat Functional pIC50 = 8.3 8.3 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 423 3 1 3 6.1 CCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
CHEMBL1631860 56425 None 0 Rat Functional pIC50 = 8.3 8.3 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 423 3 1 3 6.1 CCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
53325611 56432 None 0 Rat Functional pIC50 = 8.3 8.3 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 485 4 1 3 7.1 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(Cc4ccccc4)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631867 56432 None 0 Rat Functional pIC50 = 8.3 8.3 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 485 4 1 3 7.1 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(Cc4ccccc4)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
131636413 160184 None 0 Human Functional pIC50 = 8.3 8.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 465 6 0 6 5.4 COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](C)OCC3)ccc1OC(F)F nan
CHEMBL4108588 160184 None 0 Human Functional pIC50 = 8.3 8.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 465 6 0 6 5.4 COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](C)OCC3)ccc1OC(F)F nan
131636381 160663 None 0 Human Functional pIC50 = 8.3 8.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 409 4 0 5 5.1 Cc1cc(-c2nc(-c3ccc(OC4CC4)c(Cl)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4112623 160663 None 0 Human Functional pIC50 = 8.3 8.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 409 4 0 5 5.1 Cc1cc(-c2nc(-c3ccc(OC4CC4)c(Cl)c3)n3c2CCO[C@H](C)C3)ccn1 nan
131636384 160895 None 0 Human Functional pIC50 = 8.3 8.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 4 0 5 5.0 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)ccn1 nan
CHEMBL4114409 160895 None 0 Human Functional pIC50 = 8.3 8.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 4 0 5 5.0 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)ccn1 nan
78320251 161038 None 0 Human Functional pIC50 = 8.3 8.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 397 3 0 5 4.9 COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1Cl nan
CHEMBL4115497 161038 None 0 Human Functional pIC50 = 8.3 8.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 397 3 0 5 4.9 COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1Cl nan
131636430 160814 None 0 Human Functional pIC50 = 8.3 8.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 465 7 0 6 4.9 COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)F nan
CHEMBL4113756 160814 None 0 Human Functional pIC50 = 8.3 8.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 465 7 0 6 4.9 COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)F nan
90354553 160008 None 0 Human Functional pIC50 = 8.3 8.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 465 5 0 6 5.3 COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](C)OCC3)ccc1OC(F)(F)F nan
CHEMBL4107066 160008 None 0 Human Functional pIC50 = 8.3 8.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 465 5 0 6 5.3 COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](C)OCC3)ccc1OC(F)(F)F nan
131636464 160399 None 0 Human Functional pIC50 = 8.3 8.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 395 4 0 5 4.5 COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)cc1C nan
CHEMBL4110505 160399 None 0 Human Functional pIC50 = 8.3 8.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 395 4 0 5 4.5 COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)cc1C nan
131636420 160450 None 0 Human Functional pIC50 = 8.3 8.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 431 5 0 5 5.3 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(CF)n1 nan
CHEMBL4110839 160450 None 0 Human Functional pIC50 = 8.3 8.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 431 5 0 5 5.3 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(CF)n1 nan
131636426 160031 None 0 Human Functional pIC50 = 8.3 8.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 441 5 0 5 5.5 Cc1cc(-c2nc(-c3ccc(OC4CC4)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(CF)n1 nan
CHEMBL4107266 160031 None 0 Human Functional pIC50 = 8.3 8.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 441 5 0 5 5.5 Cc1cc(-c2nc(-c3ccc(OC4CC4)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(CF)n1 nan
78320557 160409 None 0 Human Functional pIC50 = 8.3 8.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 443 5 0 5 5.6 Cc1cc(-c2nc(-c3ccc(OC(C)C)c(Cl)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
CHEMBL4110578 160409 None 0 Human Functional pIC50 = 8.3 8.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 443 5 0 5 5.6 Cc1cc(-c2nc(-c3ccc(OC(C)C)c(Cl)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
1393 1539 None 42 Human Functional pIC50 = 8.3 8.3 2 6
Antagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assay
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm4000165
1396 1539 None 42 Human Functional pIC50 = 8.3 8.3 2 6
Antagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assay
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm4000165
213056 1539 None 42 Human Functional pIC50 = 8.3 8.3 2 6
Antagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assay
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm4000165
CHEMBL8759 1539 None 42 Human Functional pIC50 = 8.3 8.3 2 6
Antagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assay
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm4000165
78324634 160396 None 0 Human Functional pIC50 = 8.3 8.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 413 4 0 5 5.1 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4110486 160396 None 0 Human Functional pIC50 = 8.3 8.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 413 4 0 5 5.1 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
131636363 160134 None 0 Human Functional pIC50 = 8.2 8.2 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 2 0 4 5.9 Cc1cc(-c2nc(-c3ccc(Cl)c(C(F)(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4108148 160134 None 0 Human Functional pIC50 = 8.2 8.2 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 2 0 4 5.9 Cc1cc(-c2nc(-c3ccc(Cl)c(C(F)(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
90354342 160314 None 0 Human Functional pIC50 = 8.2 8.2 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 415 4 0 5 5.0 COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](C)OCC3)ccc1Cl nan
CHEMBL4109709 160314 None 0 Human Functional pIC50 = 8.2 8.2 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 415 4 0 5 5.0 COc1cc(-c2nc(-c3cc(C)nc(CF)c3)c3n2C[C@@H](C)OCC3)ccc1Cl nan
131636441 160231 None 0 Human Functional pIC50 = 8.2 8.2 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 405 5 0 5 5.2 CCOc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1CC nan
CHEMBL4109004 160231 None 0 Human Functional pIC50 = 8.2 8.2 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 405 5 0 5 5.2 CCOc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1CC nan
53320632 56311 None 0 Rat Functional pIC50 = 7.3 7.3 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 396 2 1 4 4.9 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncn3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1629852 56311 None 0 Rat Functional pIC50 = 7.3 7.3 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 396 2 1 4 4.9 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncn3)c1)=N2 10.1016/j.bmcl.2010.09.125
131636445 160057 None 0 Human Functional pIC50 = 7.3 7.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 5 0 5 5.0 Cc1cc(-c2nc(-c3ccc(C)c(OCC4CC4)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4107450 160057 None 0 Human Functional pIC50 = 7.3 7.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 403 5 0 5 5.0 Cc1cc(-c2nc(-c3ccc(C)c(OCC4CC4)c3)n3c2CCO[C@H](C)C3)ccn1 nan
1222 101792 None 46 Human Functional pIC50 = 4.3 4.3 - 1
Antagonistic activity against mGluR2 was determinedAntagonistic activity against mGluR2 was determined
ChEMBL 209 3 3 3 0.6 CC(N)(C(=O)O)c1ccc(C(=O)O)cc1 10.1021/jm960059+
CHEMBL299683 101792 None 46 Human Functional pIC50 = 4.3 4.3 - 1
Antagonistic activity against mGluR2 was determinedAntagonistic activity against mGluR2 was determined
ChEMBL 209 3 3 3 0.6 CC(N)(C(=O)O)c1ccc(C(=O)O)cc1 10.1021/jm960059+
6324634 148032 None 10 Human Functional pIC50 = 4.3 4.3 6 2
In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.
ChEMBL 355 10 3 3 3.5 N[C@@H](C[C@H](CCCC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O 10.1016/s0960-894x(98)00352-7
CHEMBL39338 148032 None 10 Human Functional pIC50 = 4.3 4.3 6 2
In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.
ChEMBL 355 10 3 3 3.5 N[C@@H](C[C@H](CCCC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O 10.1016/s0960-894x(98)00352-7
44302609 205090 None 0 Human Functional pIC50 = 4.3 4.3 - 1
In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.
ChEMBL 314 4 3 4 1.3 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccc3ccccc3c2)C1 10.1016/s0960-894x(98)00352-7
CHEMBL61281 205090 None 0 Human Functional pIC50 = 4.3 4.3 - 1
In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.
ChEMBL 314 4 3 4 1.3 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccc3ccccc3c2)C1 10.1016/s0960-894x(98)00352-7
6324634 148032 None 10 Human Functional pIC50 = 4.3 4.3 6 2
Tested for agonist activity in non-neuronal cells (RGT) expressing human Metabotropic glutamate receptor 2 by measuring ACPD (3 uM) induced inhibition of forskolin (15 uM)-stimulated cAMP formationTested for agonist activity in non-neuronal cells (RGT) expressing human Metabotropic glutamate receptor 2 by measuring ACPD (3 uM) induced inhibition of forskolin (15 uM)-stimulated cAMP formation
ChEMBL 355 10 3 3 3.5 N[C@@H](C[C@H](CCCC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O 10.1016/s0960-894x(98)00091-2
CHEMBL39338 148032 None 10 Human Functional pIC50 = 4.3 4.3 6 2
Tested for agonist activity in non-neuronal cells (RGT) expressing human Metabotropic glutamate receptor 2 by measuring ACPD (3 uM) induced inhibition of forskolin (15 uM)-stimulated cAMP formationTested for agonist activity in non-neuronal cells (RGT) expressing human Metabotropic glutamate receptor 2 by measuring ACPD (3 uM) induced inhibition of forskolin (15 uM)-stimulated cAMP formation
ChEMBL 355 10 3 3 3.5 N[C@@H](C[C@H](CCCC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O 10.1016/s0960-894x(98)00091-2
131636364 160955 None 0 Human Functional pIC50 = 7.3 7.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 367 3 0 5 4.0 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1F nan
CHEMBL4114951 160955 None 0 Human Functional pIC50 = 7.3 7.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 367 3 0 5 4.0 COc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1F nan
10091203 12956 None 0 Rat Functional pIC50 = 4.3 4.3 -2 3
Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2
ChEMBL 308 5 4 5 -0.2 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(C(C(=O)O)c2ccccc2)C1 10.1016/s0960-894x(01)00329-8
CHEMBL1189303 12956 None 0 Rat Functional pIC50 = 4.3 4.3 -2 3
Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2
ChEMBL 308 5 4 5 -0.2 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(C(C(=O)O)c2ccccc2)C1 10.1016/s0960-894x(01)00329-8
CHEMBL538489 12956 None 0 Rat Functional pIC50 = 4.3 4.3 -2 3
Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2
ChEMBL 308 5 4 5 -0.2 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(C(C(=O)O)c2ccccc2)C1 10.1016/s0960-894x(01)00329-8
11269030 56320 None 0 Human Functional pIC50 = 7.3 7.3 -1 3
Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 381 2 1 3 5.2 O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(C(F)(F)F)cc2N1 10.1016/j.bmcl.2010.09.125
CHEMBL1629861 56320 None 0 Human Functional pIC50 = 7.3 7.3 -1 3
Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 381 2 1 3 5.2 O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(C(F)(F)F)cc2N1 10.1016/j.bmcl.2010.09.125
10201802 96700 None 0 Rat Functional pIC50 = 7.3 7.3 - 1
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 413 3 1 5 4.4 CN(C)c1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2008.02.076
CHEMBL263649 96700 None 0 Rat Functional pIC50 = 7.3 7.3 - 1
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 413 3 1 5 4.4 CN(C)c1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2008.02.076
172457886 196412 None 0 Human Functional pIC50 = 7.3 7.3 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 346 4 1 6 2.1 Cn1cc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)cn1 10.1021/acsmedchemlett.3c00210
CHEMBL5423342 196412 None 0 Human Functional pIC50 = 7.3 7.3 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 346 4 1 6 2.1 Cn1cc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)cn1 10.1021/acsmedchemlett.3c00210
10428048 3361 None 25 Human Functional pIC50 = 6.3 6.3 -3 2
Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis
ChEMBL 351 4 0 4 5.3 Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl 10.1039/C3MD00110E
3955 3361 None 25 Human Functional pIC50 = 6.3 6.3 -3 2
Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis
ChEMBL 351 4 0 4 5.3 Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl 10.1039/C3MD00110E
CHEMBL305406 3361 None 25 Human Functional pIC50 = 6.3 6.3 -3 2
Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis
ChEMBL 351 4 0 4 5.3 Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl 10.1039/C3MD00110E
71566598 142777 None 16 Rat Functional pIC50 = 7.3 7.3 -2 3
Negative allosteric modulation of rat mGluR2 by GTPgammaS binding assayNegative allosteric modulation of rat mGluR2 by GTPgammaS binding assay
ChEMBL 377 4 1 4 2.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1 10.1016/j.bmcl.2020.127066
CHEMBL3892073 142777 None 16 Rat Functional pIC50 = 7.3 7.3 -2 3
Negative allosteric modulation of rat mGluR2 by GTPgammaS binding assayNegative allosteric modulation of rat mGluR2 by GTPgammaS binding assay
ChEMBL 377 4 1 4 2.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1 10.1016/j.bmcl.2020.127066
131636332 151380 None 0 Human Functional pIC50 = 7.3 7.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 405 2 0 4 5.0 Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(F)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3960577 151380 None 0 Human Functional pIC50 = 7.3 7.3 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 405 2 0 4 5.0 Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(F)c3)n3c2CCOCC3)cc(C)n1 nan
155545491 173485 None 0 Rat Functional pIC50 = 6.3 6.3 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 399 4 1 5 3.8 C[C@H]1CN(Cc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)C[C@@H](C)O1 10.1021/acs.jmedchem.8b01266
CHEMBL4527834 173485 None 0 Rat Functional pIC50 = 6.3 6.3 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 399 4 1 5 3.8 C[C@H]1CN(Cc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)C[C@@H](C)O1 10.1021/acs.jmedchem.8b01266
155545491 173485 None 0 Rat Functional pIC50 = 6.3 6.3 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 399 4 1 5 3.8 C[C@H]1CN(Cc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)C[C@@H](C)O1 10.1021/acs.jmedchem.8b01266
CHEMBL4527834 173485 None 0 Rat Functional pIC50 = 6.3 6.3 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 399 4 1 5 3.8 C[C@H]1CN(Cc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)C[C@@H](C)O1 10.1021/acs.jmedchem.8b01266
137634033 156732 None 0 Human Functional pIC50 = 5.3 5.3 -1 2
Antagonist activity at human mGlu2 receptor expressed in HEK cells assessed as reversal of DCG-4 inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in HEK cells assessed as reversal of DCG-4 inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 332 6 4 4 0.2 N[C@@]1(C(=O)O)C[C@H](NC(=O)CCc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4069251 156732 None 0 Human Functional pIC50 = 5.3 5.3 -1 2
Antagonist activity at human mGlu2 receptor expressed in HEK cells assessed as reversal of DCG-4 inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in HEK cells assessed as reversal of DCG-4 inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 332 6 4 4 0.2 N[C@@]1(C(=O)O)C[C@H](NC(=O)CCc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
172455421 196266 None 0 Human Functional pIC50 = 7.3 7.3 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 372 5 1 6 2.6 Cc1ncc(CCc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)cn1 10.1021/acsmedchemlett.3c00210
CHEMBL5420002 196266 None 0 Human Functional pIC50 = 7.3 7.3 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 372 5 1 6 2.6 Cc1ncc(CCc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)cn1 10.1021/acsmedchemlett.3c00210
90643964 112059 None 0 Rat Functional pIC50 = 6.3 6.3 -1 2
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 386 2 0 5 4.6 Cn1c(=O)c2ccc(-c3cccnc3)cc2n2nc(-c3cccc(Cl)c3)cc12 10.1016/j.bmcl.2014.04.051
CHEMBL3288656 112059 None 0 Rat Functional pIC50 = 6.3 6.3 -1 2
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 386 2 0 5 4.6 Cn1c(=O)c2ccc(-c3cccnc3)cc2n2nc(-c3cccc(Cl)c3)cc12 10.1016/j.bmcl.2014.04.051
131636436 153651 None 0 Human Functional pIC50 = 7.2 7.2 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 419 4 0 5 5.1 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(Cl)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3980239 153651 None 0 Human Functional pIC50 = 7.2 7.2 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 419 4 0 5 5.1 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(Cl)c3)n3c2CCOCC3)cc(C)n1 nan
155554668 174707 None 0 Rat Functional pIC50 = 6.2 6.2 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 394 5 1 6 3.9 Cc1ncc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)cn1 10.1021/acs.jmedchem.8b01266
CHEMBL4557272 174707 None 0 Rat Functional pIC50 = 6.2 6.2 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 394 5 1 6 3.9 Cc1ncc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)cn1 10.1021/acs.jmedchem.8b01266
155554668 174707 None 0 Rat Functional pIC50 = 6.2 6.2 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 394 5 1 6 3.9 Cc1ncc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)cn1 10.1021/acs.jmedchem.8b01266
CHEMBL4557272 174707 None 0 Rat Functional pIC50 = 6.2 6.2 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 394 5 1 6 3.9 Cc1ncc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)cn1 10.1021/acs.jmedchem.8b01266
131636322 145481 None 0 Human Functional pIC50 = 7.2 7.2 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 395 5 0 5 4.7 CCCOc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1F nan
CHEMBL3913916 145481 None 0 Human Functional pIC50 = 7.2 7.2 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 395 5 0 5 4.7 CCCOc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1F nan
22317741 56428 None 0 Rat Functional pIC50 = 8.2 8.2 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 435 3 1 3 6.4 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C4CC4)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631863 56428 None 0 Rat Functional pIC50 = 8.2 8.2 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 435 3 1 3 6.4 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C4CC4)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
22317620 56434 None 0 Rat Functional pIC50 = 8.2 8.2 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 439 4 1 4 5.7 COCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
CHEMBL1631869 56434 None 0 Rat Functional pIC50 = 8.2 8.2 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 439 4 1 4 5.7 COCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
CHEMBL5076351 216918 None 0 Human Functional pIC50 = 8.2 8.2 - 1
Negative allosteric modulation activity at human recombinant mGlur2 expressed in CHO cells in presence of cAMP by chemiluminescence based assayNegative allosteric modulation activity at human recombinant mGlur2 expressed in CHO cells in presence of cAMP by chemiluminescence based assay
ChEMBL None None None CC1(C)CCc2c(-c3ccc(F)cc3F)cc(C(N)=O)nc2O1 10.1021/acs.jmedchem.1c02004
90355554 160024 None 0 Human Functional pIC50 = 8.2 8.2 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 429 5 0 5 5.2 CCOc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)cc1Cl nan
CHEMBL4107197 160024 None 0 Human Functional pIC50 = 8.2 8.2 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 429 5 0 5 5.2 CCOc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](CF)OCC3)cc1Cl nan
131636428 160999 None 0 Human Functional pIC50 = 8.2 8.2 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 449 6 0 5 5.2 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)cc(CF)n1 nan
CHEMBL4115246 160999 None 0 Human Functional pIC50 = 8.2 8.2 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 449 6 0 5 5.2 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](CF)C3)cc(CF)n1 nan
131636307 160027 None 0 Human Functional pIC50 = 8.2 8.2 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 413 4 0 5 5.1 COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](C)OCC3)ccc1C nan
CHEMBL4107211 160027 None 0 Human Functional pIC50 = 8.2 8.2 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 413 4 0 5 5.1 COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](C)OCC3)ccc1C nan
67637415 183793 None 0 Human Functional pIC50 = 8.2 8.2 2 2
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 438 7 4 7 1.9 Cc1cc(SC[C@@H]2[C@@H](Sc3nc[nH]n3)[C@H]3[C@H](C(=O)O)[C@H]3[C@]2(N)C(=O)O)ccc1F 10.1021/acs.jmedchem.6b01119
CHEMBL4759992 183793 None 0 Human Functional pIC50 = 8.2 8.2 2 2
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 438 7 4 7 1.9 Cc1cc(SC[C@@H]2[C@@H](Sc3nc[nH]n3)[C@H]3[C@H](C(=O)O)[C@H]3[C@]2(N)C(=O)O)ccc1F 10.1021/acs.jmedchem.6b01119
CHEMBL4803099 183793 None 0 Human Functional pIC50 = 8.2 8.2 2 2
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 438 7 4 7 1.9 Cc1cc(SC[C@@H]2[C@@H](Sc3nc[nH]n3)[C@H]3[C@H](C(=O)O)[C@H]3[C@]2(N)C(=O)O)ccc1F 10.1021/acs.jmedchem.6b01119
131636377 159987 None 0 Human Functional pIC50 = 8.2 8.2 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 447 4 0 6 5.1 COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1OC(F)(F)F nan
CHEMBL4106932 159987 None 0 Human Functional pIC50 = 8.2 8.2 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 447 4 0 6 5.1 COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1OC(F)(F)F nan
117821319 118882 None 0 Human Functional pIC50 = 8.2 8.2 - 1
Negative allosteric modulation of human mGluR2 receptor expressed in CHO cell membranes assessed as inhibition of glutamate responses after 30 mins by [35S]GTPgammaS binding assayNegative allosteric modulation of human mGluR2 receptor expressed in CHO cell membranes assessed as inhibition of glutamate responses after 30 mins by [35S]GTPgammaS binding assay
ChEMBL 431 2 0 5 4.7 C[C@H]1CN(c2ccc(C(F)(F)F)c(Cl)c2)C(=O)c2c(-c3ccnc(C#N)c3)cnn21 10.1021/ml5005365
CHEMBL3421840 118882 None 0 Human Functional pIC50 = 8.2 8.2 - 1
Negative allosteric modulation of human mGluR2 receptor expressed in CHO cell membranes assessed as inhibition of glutamate responses after 30 mins by [35S]GTPgammaS binding assayNegative allosteric modulation of human mGluR2 receptor expressed in CHO cell membranes assessed as inhibition of glutamate responses after 30 mins by [35S]GTPgammaS binding assay
ChEMBL 431 2 0 5 4.7 C[C@H]1CN(c2ccc(C(F)(F)F)c(Cl)c2)C(=O)c2c(-c3ccnc(C#N)c3)cnn21 10.1021/ml5005365
131636438 151313 None 0 Human Functional pIC50 = 7.2 7.2 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 423 5 0 5 5.2 Cc1cc(-c2nc(-c3ccc(OCC4CC4)c(Cl)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3960039 151313 None 0 Human Functional pIC50 = 7.2 7.2 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 423 5 0 5 5.2 Cc1cc(-c2nc(-c3ccc(OCC4CC4)c(Cl)c3)n3c2CCOCC3)cc(C)n1 nan
44309100 102686 None 0 Rat Functional pIC50 = 5.2 5.2 - 1
Antagonist activity at rat mGlu2 expressed in CHO cells assessed as inhibition of (1S,3R)-ACPD-stimulated GTPgammaS bindingAntagonist activity at rat mGlu2 expressed in CHO cells assessed as inhibition of (1S,3R)-ACPD-stimulated GTPgammaS binding
ChEMBL 297 4 0 4 4.0 CC(C)O/C(=C\n1cncn1)c1ccc(Cl)cc1Cl 10.1016/j.bmcl.2007.10.026
CHEMBL304285 102686 None 0 Rat Functional pIC50 = 5.2 5.2 - 1
Antagonist activity at rat mGlu2 expressed in CHO cells assessed as inhibition of (1S,3R)-ACPD-stimulated GTPgammaS bindingAntagonist activity at rat mGlu2 expressed in CHO cells assessed as inhibition of (1S,3R)-ACPD-stimulated GTPgammaS binding
ChEMBL 297 4 0 4 4.0 CC(C)O/C(=C\n1cncn1)c1ccc(Cl)cc1Cl 10.1016/j.bmcl.2007.10.026
131636340 144852 None 0 Human Functional pIC50 = 7.2 7.2 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 407 3 0 5 4.5 Cc1cc(-c2nc(-c3ccnc(F)c3)c3n2CCOCC3)ccc1OC(F)(F)F nan
CHEMBL3909077 144852 None 0 Human Functional pIC50 = 7.2 7.2 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 407 3 0 5 4.5 Cc1cc(-c2nc(-c3ccnc(F)c3)c3n2CCOCC3)ccc1OC(F)(F)F nan
44302930 100768 None 0 Human Functional pIC50 = 4.2 4.2 - 1
In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.
ChEMBL 278 5 3 4 0.2 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(CCc2ccccc2)C1 10.1016/s0960-894x(98)00352-7
CHEMBL292553 100768 None 0 Human Functional pIC50 = 4.2 4.2 - 1
In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.
ChEMBL 278 5 3 4 0.2 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(CCc2ccccc2)C1 10.1016/s0960-894x(98)00352-7
52944782 16954 None 0 Human Functional pIC50 = 4.2 4.2 - 1
Antagonist activity at mGlu2 receptor expressed in CHO cells assessed as increase of cAMP levelAntagonist activity at mGlu2 receptor expressed in CHO cells assessed as increase of cAMP level
ChEMBL 241 4 3 3 0.9 N[C@H](C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1C1CCCCC1 10.1016/j.bmc.2010.06.051
CHEMBL1253502 16954 None 0 Human Functional pIC50 = 4.2 4.2 - 1
Antagonist activity at mGlu2 receptor expressed in CHO cells assessed as increase of cAMP levelAntagonist activity at mGlu2 receptor expressed in CHO cells assessed as increase of cAMP level
ChEMBL 241 4 3 3 0.9 N[C@H](C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1C1CCCCC1 10.1016/j.bmc.2010.06.051
19702198 161416 None 11 Rat Functional pIC50 = 4.2 4.2 1 2
Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2
ChEMBL 173 3 3 3 -0.5 CC(N)(C(=O)O)C1CC1C(=O)O 10.1016/s0960-894x(01)00329-8
CHEMBL412445 161416 None 11 Rat Functional pIC50 = 4.2 4.2 1 2
Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2
ChEMBL 173 3 3 3 -0.5 CC(N)(C(=O)O)C1CC1C(=O)O 10.1016/s0960-894x(01)00329-8
131636335 153358 None 0 Human Functional pIC50 = 7.2 7.2 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 367 2 0 4 4.8 Cc1cc(-c2nc(-c3ccc(Cl)c(C)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3977681 153358 None 0 Human Functional pIC50 = 7.2 7.2 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 367 2 0 4 4.8 Cc1cc(-c2nc(-c3ccc(Cl)c(C)c3)n3c2CCOCC3)cc(C)n1 nan
131636278 147555 None 0 Human Functional pIC50 = 7.2 7.2 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 363 3 0 5 4.1 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1C nan
CHEMBL3930304 147555 None 0 Human Functional pIC50 = 7.2 7.2 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 363 3 0 5 4.1 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2CCOCC3)ccc1C nan
10607617 78767 None 0 Human Functional pIC50 = 5.2 5.2 -2 2
Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2
ChEMBL 187 4 3 3 -0.1 CCC(N)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970497w
CHEMBL2112579 78767 None 0 Human Functional pIC50 = 5.2 5.2 -2 2
Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2
ChEMBL 187 4 3 3 -0.1 CCC(N)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970497w
134155683 151450 None 0 Human Functional pIC50 = 7.2 7.2 1 2
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 377 5 3 4 2.0 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@@H](F)[C@H]2[C@H](C(=O)O)[C@H]21 10.1016/j.bmcl.2016.10.067
CHEMBL3961306 151450 None 0 Human Functional pIC50 = 7.2 7.2 1 2
Antagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at recombinant human mGlu2 receptor expressed in hamster AV12 cells co-expressing human EAAT1 assessed as reduction of DCG-4-inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 377 5 3 4 2.0 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@@H](F)[C@H]2[C@H](C(=O)O)[C@H]21 10.1016/j.bmcl.2016.10.067
155553540 174283 None 0 Rat Functional pIC50 = 5.2 5.2 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 355 4 1 4 3.8 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCCC3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4547431 174283 None 0 Rat Functional pIC50 = 5.2 5.2 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 355 4 1 4 3.8 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCCC3)cc2n1 10.1021/acs.jmedchem.8b01266
155553540 174283 None 0 Rat Functional pIC50 = 5.2 5.2 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 355 4 1 4 3.8 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCCC3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4547431 174283 None 0 Rat Functional pIC50 = 5.2 5.2 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 355 4 1 4 3.8 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(CN3CCCC3)cc2n1 10.1021/acs.jmedchem.8b01266
172456116 196208 None 0 Human Functional pIC50 = 7.2 7.2 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 401 5 1 6 2.2 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)F)C4)ccc23)cn1 10.1021/acsmedchemlett.3c00210
CHEMBL5418867 196208 None 0 Human Functional pIC50 = 7.2 7.2 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 401 5 1 6 2.2 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)F)C4)ccc23)cn1 10.1021/acsmedchemlett.3c00210
172455372 196215 None 0 Human Functional pIC50 = 7.2 7.2 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 363 4 1 6 1.4 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)cn1 10.1021/acsmedchemlett.3c00210
CHEMBL5419051 196215 None 0 Human Functional pIC50 = 7.2 7.2 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 363 4 1 6 1.4 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)cn1 10.1021/acsmedchemlett.3c00210
155551226 174086 None 0 Rat Functional pIC50 = 6.2 6.2 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 393 5 1 5 4.5 Cc1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)cn1 10.1021/acs.jmedchem.8b01266
CHEMBL4541942 174086 None 0 Rat Functional pIC50 = 6.2 6.2 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 393 5 1 5 4.5 Cc1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)cn1 10.1021/acs.jmedchem.8b01266
155559283 174962 None 0 Rat Functional pIC50 = 6.2 6.2 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 380 5 1 6 3.6 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3cncnc3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4563286 174962 None 0 Rat Functional pIC50 = 6.2 6.2 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 380 5 1 6 3.6 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3cncnc3)cc2n1 10.1021/acs.jmedchem.8b01266
155551226 174086 None 0 Rat Functional pIC50 = 6.2 6.2 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 393 5 1 5 4.5 Cc1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)cn1 10.1021/acs.jmedchem.8b01266
CHEMBL4541942 174086 None 0 Rat Functional pIC50 = 6.2 6.2 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 393 5 1 5 4.5 Cc1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)cn1 10.1021/acs.jmedchem.8b01266
155559283 174962 None 0 Rat Functional pIC50 = 6.2 6.2 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 380 5 1 6 3.6 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3cncnc3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4563286 174962 None 0 Rat Functional pIC50 = 6.2 6.2 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 380 5 1 6 3.6 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3cncnc3)cc2n1 10.1021/acs.jmedchem.8b01266
172456049 196153 None 0 Human Functional pIC50 = 7.2 7.2 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 393 5 1 5 2.6 COC1CC=C(c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)CC1 10.1021/acsmedchemlett.3c00210
CHEMBL5417694 196153 None 0 Human Functional pIC50 = 7.2 7.2 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 393 5 1 5 2.6 COC1CC=C(c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)CC1 10.1021/acsmedchemlett.3c00210
11304010 56323 None 0 Human Functional pIC50 = 8.2 8.2 -2 3
Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 395 2 1 3 5.8 Cc1cc(-c2cccc(C3=Nc4cc(Cl)c(Cl)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
CHEMBL1629864 56323 None 0 Human Functional pIC50 = 8.2 8.2 -2 3
Antagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at human mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 395 2 1 3 5.8 Cc1cc(-c2cccc(C3=Nc4cc(Cl)c(Cl)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
22317892 56319 None 0 Rat Functional pIC50 = 8.2 8.2 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 477 2 1 3 6.9 Cc1cc(-c2cccc(C3=Nc4cc(C(F)(F)F)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C)n1 10.1016/j.bmcl.2010.09.125
CHEMBL1629860 56319 None 0 Rat Functional pIC50 = 8.2 8.2 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 477 2 1 3 6.9 Cc1cc(-c2cccc(C3=Nc4cc(C(F)(F)F)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C)n1 10.1016/j.bmcl.2010.09.125
22317279 56430 None 0 Rat Functional pIC50 = 8.2 8.2 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 463 3 1 3 7.2 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C4CCCC4)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631865 56430 None 0 Rat Functional pIC50 = 8.2 8.2 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 463 3 1 3 7.2 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C4CCCC4)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
89554880 150132 None 0 Human Functional pIC50 = 8.2 8.2 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 372 5 1 4 3.7 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3cncnc3)cc2n1 10.1021/acsmedchemlett.3c00210
CHEMBL3950572 150132 None 0 Human Functional pIC50 = 8.2 8.2 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 372 5 1 4 3.7 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3cncnc3)cc2n1 10.1021/acsmedchemlett.3c00210
131636308 160896 None 0 Human Functional pIC50 = 8.2 8.2 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 431 5 0 5 5.1 COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](CF)OCC3)ccc1C nan
CHEMBL4114419 160896 None 0 Human Functional pIC50 = 8.2 8.2 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 431 5 0 5 5.1 COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](CF)OCC3)ccc1C nan
90354432 160913 None 0 Human Functional pIC50 = 8.1 8.1 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 465 5 1 6 4.4 COc1cc(-c2nc(-c3cc(C)nc(CO)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)(F)F nan
CHEMBL4114578 160913 None 0 Human Functional pIC50 = 8.1 8.1 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 465 5 1 6 4.4 COc1cc(-c2nc(-c3cc(C)nc(CO)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)(F)F nan
78319943 160005 None 0 Human Functional pIC50 = 8.1 8.1 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 399 4 0 5 4.8 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4107040 160005 None 0 Human Functional pIC50 = 8.1 8.1 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 399 4 0 5 4.8 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(C)c3)n3c2CCO[C@H](C)C3)ccn1 nan
131636404 160433 None 0 Human Functional pIC50 = 8.1 8.1 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 415 2 0 4 5.5 Cc1cc(-c2nc(-c3ccc(C)c(C(F)(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4110709 160433 None 0 Human Functional pIC50 = 8.1 8.1 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 415 2 0 4 5.5 Cc1cc(-c2nc(-c3ccc(C)c(C(F)(F)F)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
90354881 160185 None 0 Human Functional pIC50 = 8.1 8.1 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 419 4 0 5 5.1 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4108597 160185 None 0 Human Functional pIC50 = 8.1 8.1 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 419 4 0 5 5.1 Cc1cc(-c2nc(-c3ccc(OC(F)F)c(Cl)c3)n3c2CCO[C@H](C)C3)ccn1 nan
131636327 160736 None 0 Human Functional pIC50 = 8.1 8.1 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 377 4 0 5 4.5 CCc1ccc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)cc1OC nan
CHEMBL4113208 160736 None 0 Human Functional pIC50 = 8.1 8.1 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 377 4 0 5 4.5 CCc1ccc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)cc1OC nan
1378 2417 None 39 Human Functional pIC50 = 8.1 8.1 -2 14
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assay
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/acs.jmedchem.6b01119
1399 2417 None 39 Human Functional pIC50 = 8.1 8.1 -2 14
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assay
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/acs.jmedchem.6b01119
9819927 2417 None 39 Human Functional pIC50 = 8.1 8.1 -2 14
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assay
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/acs.jmedchem.6b01119
CHEMBL432038 2417 None 39 Human Functional pIC50 = 8.1 8.1 -2 14
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cell membrane co-expressing Galpha15 assessed as assessed as reduction in glutamate-induced calcium influx incubated for 90 to 120 min by Fluo-4-AM dye based FLIPR assay
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/acs.jmedchem.6b01119
131636281 160778 None 0 Human Functional pIC50 = 8.1 8.1 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 3 0 5 5.1 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4113495 160778 None 0 Human Functional pIC50 = 8.1 8.1 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 3 0 5 5.1 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
90354538 160456 None 0 Human Functional pIC50 = 8.1 8.1 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 485 5 0 5 5.8 COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)(F)F nan
CHEMBL4110899 160456 None 0 Human Functional pIC50 = 8.1 8.1 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 485 5 0 5 5.8 COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](CF)OCC3)ccc1C(F)(F)F nan
131636440 161008 None 0 Human Functional pIC50 = 8.1 8.1 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 391 5 0 5 4.8 CCOc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1CC nan
CHEMBL4115297 161008 None 0 Human Functional pIC50 = 8.1 8.1 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 391 5 0 5 4.8 CCOc1cc(-c2nc(-c3ccnc(C)c3)c3n2C[C@@H](C)OCC3)ccc1CC nan
10979251 90094 None 0 Human Functional pIC50 = 5.2 5.2 -5 3
Antagonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as reversal of DCG-4-inhibited, forskolin-stimulated cAMP production after 1 hr by fluorescence assayAntagonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as reversal of DCG-4-inhibited, forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 293 4 3 4 1.3 N[C@@]1(C(=O)O)C[C@@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL2381650 90094 None 0 Human Functional pIC50 = 5.2 5.2 -5 3
Antagonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as reversal of DCG-4-inhibited, forskolin-stimulated cAMP production after 1 hr by fluorescence assayAntagonist activity at human recombinant mGlu2 receptor expressed in AV12 cells assessed as reversal of DCG-4-inhibited, forskolin-stimulated cAMP production after 1 hr by fluorescence assay
ChEMBL 293 4 3 4 1.3 N[C@@]1(C(=O)O)C[C@@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
10979251 90094 None 0 Human Functional pIC50 = 5.2 5.2 -5 3
Antagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assay
ChEMBL 293 4 3 4 1.3 N[C@@]1(C(=O)O)C[C@@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm4000165
CHEMBL2381650 90094 None 0 Human Functional pIC50 = 5.2 5.2 -5 3
Antagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 assessed as inhibition of forskolin-stimulated cAMP production after 20 mins by HTRF assay
ChEMBL 293 4 3 4 1.3 N[C@@]1(C(=O)O)C[C@@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm4000165
22317408 56309 None 0 Rat Functional pIC50 = 7.1 7.1 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 396 2 1 4 4.9 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnnc3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1629850 56309 None 0 Rat Functional pIC50 = 7.1 7.1 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 396 2 1 4 4.9 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnnc3)c1)=N2 10.1016/j.bmcl.2010.09.125
131636433 144665 None 0 Human Functional pIC50 = 7.1 7.1 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 419 4 0 5 5.1 Cc1cc(-c2nc(-c3ccc(Cl)c(OC(F)F)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3907628 144665 None 0 Human Functional pIC50 = 7.1 7.1 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 419 4 0 5 5.1 Cc1cc(-c2nc(-c3ccc(Cl)c(OC(F)F)c3)n3c2CCOCC3)cc(C)n1 nan
10297067 96357 None 0 Rat Functional pIC50 = 7.1 7.1 - 1
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 441 5 2 5 5.4 CC(C)CNc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2008.02.076
CHEMBL261263 96357 None 0 Rat Functional pIC50 = 7.1 7.1 - 1
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 441 5 2 5 5.4 CC(C)CNc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2008.02.076
131636277 151743 None 0 Human Functional pIC50 = 7.1 7.1 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 3 0 5 4.8 Cc1cc(-c2nc(-c3ccc(F)c(OC(F)(F)F)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3963950 151743 None 0 Human Functional pIC50 = 7.1 7.1 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 3 0 5 4.8 Cc1cc(-c2nc(-c3ccc(F)c(OC(F)(F)F)c3)n3c2CCOCC3)cc(C)n1 nan
18548910 95987 None 0 Rat Functional pIC50 = 7.1 7.1 - 1
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 401 3 1 6 3.8 COc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
CHEMBL259340 95987 None 0 Rat Functional pIC50 = 7.1 7.1 - 1
Antagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as blockade of (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 401 3 1 6 3.8 COc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
172456755 196402 None 0 Human Functional pIC50 = 7.1 7.1 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 363 4 1 6 1.5 Cc1cnn(-c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)c1 10.1021/acsmedchemlett.3c00210
CHEMBL5423035 196402 None 0 Human Functional pIC50 = 7.1 7.1 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 363 4 1 6 1.5 Cc1cnn(-c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)c1 10.1021/acsmedchemlett.3c00210
155565564 175674 None 0 Rat Functional pIC50 = 6.1 6.1 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 407 5 1 5 4.8 Cc1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)c(C)n1 10.1021/acs.jmedchem.8b01266
CHEMBL4579281 175674 None 0 Rat Functional pIC50 = 6.1 6.1 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 407 5 1 5 4.8 Cc1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)c(C)n1 10.1021/acs.jmedchem.8b01266
155565564 175674 None 0 Rat Functional pIC50 = 6.1 6.1 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 407 5 1 5 4.8 Cc1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)c(C)n1 10.1021/acs.jmedchem.8b01266
CHEMBL4579281 175674 None 0 Rat Functional pIC50 = 6.1 6.1 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 407 5 1 5 4.8 Cc1ccc(OCc2cc3nc(C(N)=O)cc(-c4ccc(F)cc4)c3s2)c(C)n1 10.1021/acs.jmedchem.8b01266
18548737 56419 None 0 Rat Functional pIC50 = 7.1 7.1 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 385 2 1 5 4.1 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3cncn3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631854 56419 None 0 Rat Functional pIC50 = 7.1 7.1 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 385 2 1 5 4.1 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3cncn3)c1)=N2 10.1016/j.bmcl.2010.09.125
44302819 163331 None 0 Human Functional pIC50 = 4.1 4.1 - 1
In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.
ChEMBL 298 4 3 4 0.8 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2Cl)C1 10.1016/s0960-894x(98)00352-7
CHEMBL418462 163331 None 0 Human Functional pIC50 = 4.1 4.1 - 1
In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.In vitro antagonist activity at recombinant human Metabotropic glutamate receptor 2 expressed in RGT cells.
ChEMBL 298 4 3 4 0.8 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2Cl)C1 10.1016/s0960-894x(98)00352-7
155564600 175656 None 0 Rat Functional pIC50 = 6.1 6.1 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 393 5 1 5 4.5 Cc1ncccc1OCc1cc2nc(C(N)=O)cc(-c3ccc(F)cc3)c2s1 10.1021/acs.jmedchem.8b01266
CHEMBL4578758 175656 None 0 Rat Functional pIC50 = 6.1 6.1 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 393 5 1 5 4.5 Cc1ncccc1OCc1cc2nc(C(N)=O)cc(-c3ccc(F)cc3)c2s1 10.1021/acs.jmedchem.8b01266
155564600 175656 None 0 Rat Functional pIC50 = 6.1 6.1 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 393 5 1 5 4.5 Cc1ncccc1OCc1cc2nc(C(N)=O)cc(-c3ccc(F)cc3)c2s1 10.1021/acs.jmedchem.8b01266
CHEMBL4578758 175656 None 0 Rat Functional pIC50 = 6.1 6.1 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 393 5 1 5 4.5 Cc1ncccc1OCc1cc2nc(C(N)=O)cc(-c3ccc(F)cc3)c2s1 10.1021/acs.jmedchem.8b01266
162666357 183837 None 0 Human Functional pIC50 = 7.1 7.1 3 2
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 341 5 4 5 0.6 N[C@@]1(C(=O)O)[C@H](CSc2cccc(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4784701 183837 None 0 Human Functional pIC50 = 7.1 7.1 3 2
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 341 5 4 5 0.6 N[C@@]1(C(=O)O)[C@H](CSc2cccc(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4803523 183837 None 0 Human Functional pIC50 = 7.1 7.1 3 2
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 341 5 4 5 0.6 N[C@@]1(C(=O)O)[C@H](CSc2cccc(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
137656301 158774 None 0 Human Functional pIC50 = 5.1 5.1 - 1
Antagonist activity at human mGlu2 receptor expressed in HEK cells assessed as reversal of DCG-4 inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in HEK cells assessed as reversal of DCG-4 inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 324 5 4 4 0.6 N[C@@]1(C(=O)O)C[C@H](NC(=O)CC2CCCCC2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4093017 158774 None 0 Human Functional pIC50 = 5.1 5.1 - 1
Antagonist activity at human mGlu2 receptor expressed in HEK cells assessed as reversal of DCG-4 inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assayAntagonist activity at human mGlu2 receptor expressed in HEK cells assessed as reversal of DCG-4 inhibited forskolin-stimulated cAMP formation after 20 mins by HTRF assay
ChEMBL 324 5 4 4 0.6 N[C@@]1(C(=O)O)C[C@H](NC(=O)CC2CCCCC2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
44300389 13664 None 0 Rat Functional pIC50 = 4.1 4.1 -1 2
Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2
ChEMBL 342 4 3 4 0.9 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2Br)C1 10.1016/s0960-894x(01)00329-8
CHEMBL1194613 13664 None 0 Rat Functional pIC50 = 4.1 4.1 -1 2
Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2
ChEMBL 342 4 3 4 0.9 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2Br)C1 10.1016/s0960-894x(01)00329-8
CHEMBL552984 13664 None 0 Rat Functional pIC50 = 4.1 4.1 -1 2
Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2Inhibitory concentration required for antagonistic activity at Metabotropic glutamate receptor 2
ChEMBL 342 4 3 4 0.9 N[C@]1(C(=O)O)C[C@H](C(=O)O)N(Cc2ccccc2Br)C1 10.1016/s0960-894x(01)00329-8
131636292 160620 None 0 Human Functional pIC50 = 7.1 7.1 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 353 2 0 4 4.5 Cc1cc(-c2nc(-c3cccc(Cl)c3)n3c2CCO[C@H](C)C3)ccn1 nan
CHEMBL4112325 160620 None 0 Human Functional pIC50 = 7.1 7.1 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 353 2 0 4 4.5 Cc1cc(-c2nc(-c3cccc(Cl)c3)n3c2CCO[C@H](C)C3)ccn1 nan
131636439 153917 None 0 Human Functional pIC50 = 7.1 7.1 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 433 5 0 5 5.1 Cc1cc(-c2nc(-c3ccc(OCC(F)F)c(Cl)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3982561 153917 None 0 Human Functional pIC50 = 7.1 7.1 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 433 5 0 5 5.1 Cc1cc(-c2nc(-c3ccc(OCC(F)F)c(Cl)c3)n3c2CCOCC3)cc(C)n1 nan
117821004 118881 None 0 Human Functional pIC50 = 7.1 7.1 - 1
Negative allosteric modulation of human mGluR2 receptor expressed in CHO cell membranes assessed as inhibition of glutamate responses after 30 mins by [35S]GTPgammaS binding assayNegative allosteric modulation of human mGluR2 receptor expressed in CHO cell membranes assessed as inhibition of glutamate responses after 30 mins by [35S]GTPgammaS binding assay
ChEMBL 400 3 0 4 4.9 CCC1CN(c2ccc(C(F)(F)F)cc2)C(=O)c2c(-c3ccnc(C)c3)cnn21 10.1021/ml5005365
CHEMBL3421839 118881 None 0 Human Functional pIC50 = 7.1 7.1 - 1
Negative allosteric modulation of human mGluR2 receptor expressed in CHO cell membranes assessed as inhibition of glutamate responses after 30 mins by [35S]GTPgammaS binding assayNegative allosteric modulation of human mGluR2 receptor expressed in CHO cell membranes assessed as inhibition of glutamate responses after 30 mins by [35S]GTPgammaS binding assay
ChEMBL 400 3 0 4 4.9 CCC1CN(c2ccc(C(F)(F)F)cc2)C(=O)c2c(-c3ccnc(C)c3)cnn21 10.1021/ml5005365
155511336 169642 None 0 Rat Functional pIC50 = 6.1 6.1 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 431 5 1 6 3.6 NC(=O)c1cc(-c2ccc(F)cc2)n2nc(COc3ccnc(C(F)(F)F)c3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4435396 169642 None 0 Rat Functional pIC50 = 6.1 6.1 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 431 5 1 6 3.6 NC(=O)c1cc(-c2ccc(F)cc2)n2nc(COc3ccnc(C(F)(F)F)c3)cc2n1 10.1021/acs.jmedchem.8b01266
155511336 169642 None 0 Rat Functional pIC50 = 6.1 6.1 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 431 5 1 6 3.6 NC(=O)c1cc(-c2ccc(F)cc2)n2nc(COc3ccnc(C(F)(F)F)c3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4435396 169642 None 0 Rat Functional pIC50 = 6.1 6.1 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 431 5 1 6 3.6 NC(=O)c1cc(-c2ccc(F)cc2)n2nc(COc3ccnc(C(F)(F)F)c3)cc2n1 10.1021/acs.jmedchem.8b01266
11235624 56321 None 0 Rat Functional pIC50 = 8.1 8.1 -1 3
Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 425 4 1 4 5.6 CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncc3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1629862 56321 None 0 Rat Functional pIC50 = 8.1 8.1 -1 3
Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK currentAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as inhibition of GIRK current
ChEMBL 425 4 1 4 5.6 CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncc3)c1)=N2 10.1016/j.bmcl.2010.09.125
11442010 56325 None 0 Rat Functional pIC50 = 8.1 8.1 -2 3
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 439 4 1 4 5.9 CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1629866 56325 None 0 Rat Functional pIC50 = 8.1 8.1 -2 3
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 439 4 1 4 5.9 CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
71565593 151050 None 0 Human Functional pIC50 = 8.1 8.1 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 377 4 1 4 3.2 CC1CC=C(c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)CC1 10.1021/acsmedchemlett.3c00210
CHEMBL3958138 151050 None 0 Human Functional pIC50 = 8.1 8.1 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 377 4 1 4 3.2 CC1CC=C(c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)CC1 10.1021/acsmedchemlett.3c00210
25210562 217455 None 21 Human Functional pIC50 = 8.1 8.1 - 1
Negative allosteric modulator activity at human recombinant mGlur2 expressed in HEK293 cells by calcium assayNegative allosteric modulator activity at human recombinant mGlur2 expressed in HEK293 cells by calcium assay
ChEMBL None None None N#Cc1cc(C2=Nc3ccc(Br)cc3NC(=O)C2)ccn1 10.1021/acs.jmedchem.1c02004
CHEMBL5085417 217455 None 21 Human Functional pIC50 = 8.1 8.1 - 1
Negative allosteric modulator activity at human recombinant mGlur2 expressed in HEK293 cells by calcium assayNegative allosteric modulator activity at human recombinant mGlur2 expressed in HEK293 cells by calcium assay
ChEMBL None None None N#Cc1cc(C2=Nc3ccc(Br)cc3NC(=O)C2)ccn1 10.1021/acs.jmedchem.1c02004
131636350 143909 None 0 Human Functional pIC50 = 8.1 8.1 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 389 3 0 4 5.1 Cc1cc(-c2nc(-c3ccc(Cl)c(C(F)F)c3)n3c2CCOCC3)ccn1 nan
CHEMBL3901364 143909 None 0 Human Functional pIC50 = 8.1 8.1 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 389 3 0 4 5.1 Cc1cc(-c2nc(-c3ccc(Cl)c(C(F)F)c3)n3c2CCOCC3)ccn1 nan
117824335 118880 None 1 Human Functional pIC50 = 8.1 8.1 - 1
Negative allosteric modulation of human mGluR2 receptor expressed in CHO cell membranes assessed as inhibition of glutamate responses after 30 mins by [35S]GTPgammaS binding assayNegative allosteric modulation of human mGluR2 receptor expressed in CHO cell membranes assessed as inhibition of glutamate responses after 30 mins by [35S]GTPgammaS binding assay
ChEMBL 386 2 0 4 4.5 Cc1cc(-c2cnn3c2C(=O)N(c2ccc(C(F)(F)F)cc2)C[C@@H]3C)ccn1 10.1021/ml5005365
CHEMBL3421838 118880 None 1 Human Functional pIC50 = 8.1 8.1 - 1
Negative allosteric modulation of human mGluR2 receptor expressed in CHO cell membranes assessed as inhibition of glutamate responses after 30 mins by [35S]GTPgammaS binding assayNegative allosteric modulation of human mGluR2 receptor expressed in CHO cell membranes assessed as inhibition of glutamate responses after 30 mins by [35S]GTPgammaS binding assay
ChEMBL 386 2 0 4 4.5 Cc1cc(-c2cnn3c2C(=O)N(c2ccc(C(F)(F)F)cc2)C[C@@H]3C)ccn1 10.1021/ml5005365
49836087 1061 None 0 Human Functional pIC50 = 6.1 6.1 16 2
Negative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assayNegative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assay
ChEMBL 328 2 2 4 3.3 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)Cl 10.1021/jm101069m
6222 1061 None 0 Human Functional pIC50 = 6.1 6.1 16 2
Negative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assayNegative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assay
ChEMBL 328 2 2 4 3.3 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)Cl 10.1021/jm101069m
CHEMBL1630805 1061 None 0 Human Functional pIC50 = 6.1 6.1 16 2
Negative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assayNegative allosteric modulator activity at human mGluR2 expressed in HEK cells in presence of glutamate EC80 concentration by Ca2+ functional assay
ChEMBL 328 2 2 4 3.3 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)Cl 10.1021/jm101069m
3335 3015 None 1 Human Functional pIC50 = 5.1 5.1 1 2
Concentration required for the half-maximal inhibition of cAMP hydrolysis in BHK cells expressing mGluR2Concentration required for the half-maximal inhibition of cAMP hydrolysis in BHK cells expressing mGluR2
ChEMBL 235 4 3 3 0.5 OC(=O)[C@H]([C@H]1[C@H]([C@@H]1C(=O)O)c1ccccc1)N 10.1021/jm960059+
5311344 3015 None 1 Human Functional pIC50 = 5.1 5.1 1 2
Concentration required for the half-maximal inhibition of cAMP hydrolysis in BHK cells expressing mGluR2Concentration required for the half-maximal inhibition of cAMP hydrolysis in BHK cells expressing mGluR2
ChEMBL 235 4 3 3 0.5 OC(=O)[C@H]([C@H]1[C@H]([C@@H]1C(=O)O)c1ccccc1)N 10.1021/jm960059+
CHEMBL39573 3015 None 1 Human Functional pIC50 = 5.1 5.1 1 2
Concentration required for the half-maximal inhibition of cAMP hydrolysis in BHK cells expressing mGluR2Concentration required for the half-maximal inhibition of cAMP hydrolysis in BHK cells expressing mGluR2
ChEMBL 235 4 3 3 0.5 OC(=O)[C@H]([C@H]1[C@H]([C@@H]1C(=O)O)c1ccccc1)N 10.1021/jm960059+
131636449 160512 None 0 Human Functional pIC50 = 7.1 7.1 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 461 5 0 6 5.3 Cc1cc(-c2nc(-c3ccc(C)c(OCC4CCOCC4)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4111376 160512 None 0 Human Functional pIC50 = 7.1 7.1 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 461 5 0 6 5.3 Cc1cc(-c2nc(-c3ccc(C)c(OCC4CCOCC4)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
90643970 112063 None 0 Rat Functional pIC50 = 6.1 6.1 1 2
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 464 3 1 6 3.8 Cn1c(=O)c2ccc(-c3cccc(S(N)(=O)=O)c3)cc2n2nc(-c3ccc(Cl)cc3)cc12 10.1016/j.bmcl.2014.04.051
CHEMBL3288664 112063 None 0 Rat Functional pIC50 = 6.1 6.1 1 2
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 464 3 1 6 3.8 Cn1c(=O)c2ccc(-c3cccc(S(N)(=O)=O)c3)cc2n2nc(-c3ccc(Cl)cc3)cc12 10.1016/j.bmcl.2014.04.051
10587622 78771 None 0 Human Functional pIC50 = 6.1 6.1 -1 2
Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2
ChEMBL 263 6 3 3 1.1 NC(CCc1ccccc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970497w
CHEMBL2112582 78771 None 0 Human Functional pIC50 = 6.1 6.1 -1 2
Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2Ability to block 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in non-neuronal cell line expressing human Metabotropic glutamate receptor 2
ChEMBL 263 6 3 3 1.1 NC(CCc1ccccc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970497w
10587622 78771 None 0 Human Functional pIC50 = 6.1 6.1 -1 2
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 263 6 3 3 1.1 NC(CCc1ccccc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970498o
CHEMBL2112582 78771 None 0 Human Functional pIC50 = 6.1 6.1 -1 2
Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2Effect on 1S,3R-ACPD-induced inhibition of forskolin stimulated cyclic-AMP in RGT cells expressing human Metabotropic glutamate receptor 2
ChEMBL 263 6 3 3 1.1 NC(CCc1ccccc1)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm970498o
90643956 112054 None 0 Rat Functional pIC50 = 6.1 6.1 -5 2
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 352 2 0 5 3.9 Cn1c(=O)c2ccc(-c3cccnc3)cc2n2nc(-c3ccccc3)cc12 10.1016/j.bmcl.2014.04.051
CHEMBL3288639 112054 None 0 Rat Functional pIC50 = 6.1 6.1 -5 2
Inhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentrationInhibition of rat mGlu2 receptor transfected in HEK293 cells coexpressing mouse Galpha15 assessed as decrease in glutamate-induced calcium signaling by fluorescence plate reader analysis in presence of glutamate at EC76 concentration
ChEMBL 352 2 0 5 3.9 Cn1c(=O)c2ccc(-c3cccnc3)cc2n2nc(-c3ccccc3)cc12 10.1016/j.bmcl.2014.04.051
155564325 175522 None 0 Rat Functional pIC50 = 7.1 7.1 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 429 5 1 5 3.8 NC(=O)c1cc(-c2ccc(F)cc2)n2nc(CCc3ccnc(C(F)(F)F)c3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4575990 175522 None 0 Rat Functional pIC50 = 7.1 7.1 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 429 5 1 5 3.8 NC(=O)c1cc(-c2ccc(F)cc2)n2nc(CCc3ccnc(C(F)(F)F)c3)cc2n1 10.1021/acs.jmedchem.8b01266
155564325 175522 None 0 Rat Functional pIC50 = 7.1 7.1 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 429 5 1 5 3.8 NC(=O)c1cc(-c2ccc(F)cc2)n2nc(CCc3ccnc(C(F)(F)F)c3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4575990 175522 None 0 Rat Functional pIC50 = 7.1 7.1 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 429 5 1 5 3.8 NC(=O)c1cc(-c2ccc(F)cc2)n2nc(CCc3ccnc(C(F)(F)F)c3)cc2n1 10.1021/acs.jmedchem.8b01266
155521127 170653 None 0 Rat Functional pIC50 = 6.1 6.1 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 413 5 1 5 4.8 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3ccc(Cl)nc3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4450016 170653 None 0 Rat Functional pIC50 = 6.1 6.1 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 413 5 1 5 4.8 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3ccc(Cl)nc3)cc2n1 10.1021/acs.jmedchem.8b01266
155521127 170653 None 0 Rat Functional pIC50 = 6.1 6.1 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 413 5 1 5 4.8 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3ccc(Cl)nc3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4450016 170653 None 0 Rat Functional pIC50 = 6.1 6.1 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 413 5 1 5 4.8 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3ccc(Cl)nc3)cc2n1 10.1021/acs.jmedchem.8b01266
76332991 106155 None 0 Human Functional pIC50 = 7.1 7.1 - 1
Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis
ChEMBL 428 2 1 4 3.9 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(I)cc2N1 10.1039/C3MD00110E
CHEMBL3133882 106155 None 0 Human Functional pIC50 = 7.1 7.1 - 1
Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis
ChEMBL 428 2 1 4 3.9 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(I)cc2N1 10.1039/C3MD00110E
76322144 106160 None 0 Human Functional pIC50 = 7.1 7.1 - 1
Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis
ChEMBL 534 4 1 5 5.6 COc1cc2c(cc1-c1ccc(I)cc1)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1039/C3MD00110E
CHEMBL3133887 106160 None 0 Human Functional pIC50 = 7.1 7.1 - 1
Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis
ChEMBL 534 4 1 5 5.6 COc1cc2c(cc1-c1ccc(I)cc1)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1039/C3MD00110E
155515940 170111 None 0 Rat Functional pIC50 = 6.1 6.1 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 397 5 1 5 4.3 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3ccc(F)nc3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4442453 170111 None 0 Rat Functional pIC50 = 6.1 6.1 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 397 5 1 5 4.3 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3ccc(F)nc3)cc2n1 10.1021/acs.jmedchem.8b01266
155515940 170111 None 0 Rat Functional pIC50 = 6.1 6.1 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 397 5 1 5 4.3 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3ccc(F)nc3)cc2n1 10.1021/acs.jmedchem.8b01266
CHEMBL4442453 170111 None 0 Rat Functional pIC50 = 6.1 6.1 - 1
Negative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assayNegative allosteric modulation of rat mGlu2R expressed in HEK293 cells co-expressing Galpha15 assessed as decrease in glutamate-induced calcium mobilization preincubated for 2.3 mins followed by glutamate addition and measured after 1.7 mins by Fluo-4-AM dye based fluorescence assay
ChEMBL 397 5 1 5 4.3 NC(=O)c1cc(-c2ccc(F)cc2)c2sc(COc3ccc(F)nc3)cc2n1 10.1021/acs.jmedchem.8b01266
9888376 95268 None 1 Rat Functional pIC50 = 8.1 8.1 - 1
Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 420 2 1 4 4.9 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2007.12.005
CHEMBL256011 95268 None 1 Rat Functional pIC50 = 8.1 8.1 - 1
Antagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP productionAntagonist activity at rat mGluR2 assessed as effect on (1S,3R)-ACPD-induced inhibition of forskolin-stimulated cAMP production
ChEMBL 420 2 1 4 4.9 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2007.12.005
18548795 56417 None 0 Rat Functional pIC50 = 8.1 8.1 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 399 2 1 4 5.4 Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)on1 10.1016/j.bmcl.2010.09.125
CHEMBL1631757 56417 None 0 Rat Functional pIC50 = 8.1 8.1 - 1
Antagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP productionAntagonist activity at recombinant rat mGluR2 expressed in forskolin-stimulated CHO cells assessed as inhibition of (1S,3R)-ACPD induced cAMP production
ChEMBL 399 2 1 4 5.4 Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)on1 10.1016/j.bmcl.2010.09.125
131636414 160348 None 0 Human Functional pIC50 = 8.1 8.1 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 483 7 0 6 5.4 COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)F nan
CHEMBL4110033 160348 None 0 Human Functional pIC50 = 8.1 8.1 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 483 7 0 6 5.4 COc1cc(-c2nc(-c3cc(C)nc(C(F)F)c3)c3n2C[C@@H](CF)OCC3)ccc1OC(F)F nan
131636334 150243 None 0 Human Functional pIC50 = 8.0 8.0 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 2 0 4 5.5 Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(Cl)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3951588 150243 None 0 Human Functional pIC50 = 8.0 8.0 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 421 2 0 4 5.5 Cc1cc(-c2nc(-c3ccc(C(F)(F)F)c(Cl)c3)n3c2CCOCC3)cc(C)n1 nan
131636352 160529 None 0 Human Functional pIC50 = 8.0 8.0 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 413 4 0 5 5.1 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)F nan
CHEMBL4111531 160529 None 0 Human Functional pIC50 = 8.0 8.0 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 413 4 0 5 5.1 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1C(F)F nan
131636387 161014 None 0 Human Functional pIC50 = 8.0 8.0 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 453 4 0 5 5.2 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
CHEMBL4115328 161014 None 0 Human Functional pIC50 = 8.0 8.0 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 453 4 0 5 5.2 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)c(F)c3)n3c2CCO[C@H](CF)C3)cc(C)n1 nan
89545222 160472 None 4 Human Functional pIC50 = 8.0 8.0 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 433 4 1 6 2.9 C[C@@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1 10.1021/acsmedchemlett.3c00210
CHEMBL4111091 160472 None 4 Human Functional pIC50 = 8.0 8.0 - 1
Negative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysisNegative allosteric modulation at human mGluR2 receptor stably expressed in DHFR null CHO cells co-expressing Galpha16 assessed as effect on intracellular calcium flux measured after 5 min by Fluo-4AM dye based FLIPR analysis
ChEMBL 433 4 1 6 2.9 C[C@@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1 10.1021/acsmedchemlett.3c00210
131636371 160234 None 0 Human Functional pIC50 = 8.0 8.0 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 429 5 0 6 4.8 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1OC(F)F nan
CHEMBL4109036 160234 None 0 Human Functional pIC50 = 8.0 8.0 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 429 5 0 6 4.8 COc1cc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)ccc1OC(F)F nan
131636452 160764 None 0 Human Functional pIC50 = 8.0 8.0 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 439 4 0 6 4.6 Cc1cc(-c2nc(-c3ccc(OC4COC4)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
CHEMBL4113408 160764 None 0 Human Functional pIC50 = 8.0 8.0 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 439 4 0 6 4.6 Cc1cc(-c2nc(-c3ccc(OC4COC4)c(Cl)c3)n3c2CCO[C@H](C)C3)cc(C)n1 nan
67633284 183753 None 0 Human Functional pIC50 = 8.0 8.0 5 2
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 391 5 4 5 1.8 N[C@@]1(C(=O)O)[C@H](CSc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4748699 183753 None 0 Human Functional pIC50 = 8.0 8.0 5 2
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 391 5 4 5 1.8 N[C@@]1(C(=O)O)[C@H](CSc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4802655 183753 None 0 Human Functional pIC50 = 8.0 8.0 5 2
Antagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assayAntagonist activity at human recombinant mGlu2 receptor stably expressed in golden hamster AV12 cells co-expressing rat EAAT1 assessed as reduction in DCG IV-induced inhibition of forskolin-stimulated cAMP accumulation preincubated for 20 mins followed by incubation with cAMP-d2 conjugate and anti-cAMP cryptate for 1 hr by HTRF assay
ChEMBL 391 5 4 5 1.8 N[C@@]1(C(=O)O)[C@H](CSc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
131636275 142948 None 0 Human Functional pIC50 = 7.1 7.1 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 389 3 0 5 4.4 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCOCC3)ccn1 nan
CHEMBL3893337 142948 None 0 Human Functional pIC50 = 7.1 7.1 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 389 3 0 5 4.4 Cc1cc(-c2nc(-c3ccc(OC(F)(F)F)cc3)n3c2CCOCC3)ccn1 nan
76322143 106158 None 0 Human Functional pIC50 = 7.0 7.0 - 1
Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis
ChEMBL 400 3 1 5 4.4 COc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1039/C3MD00110E
CHEMBL3133885 106158 None 0 Human Functional pIC50 = 7.0 7.0 - 1
Non-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysisNon-competitive antagonist activity at human recombinant mGluR2 expressed in Chem-1 cell membrane assessed as inhibition of L-glutamate-induced [35S]GTPgammaS binding after 30 mins by liquid scintillation counting analysis
ChEMBL 400 3 1 5 4.4 COc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1039/C3MD00110E
131636330 148556 None 0 Human Functional pIC50 = 7.0 7.0 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 371 2 0 4 4.6 Cc1cc(-c2nc(-c3ccc(Cl)c(F)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3938055 148556 None 0 Human Functional pIC50 = 7.0 7.0 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 371 2 0 4 4.6 Cc1cc(-c2nc(-c3ccc(Cl)c(F)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL5089623 217707 None 3 Human Functional pIC50 = 7.0 7.0 - 1
Negative allosteric modulation activity at human recombinant mGlur2 expressed in CHO cells in presence of cAMP by chemiluminescence based assayNegative allosteric modulation activity at human recombinant mGlur2 expressed in CHO cells in presence of cAMP by chemiluminescence based assay
ChEMBL None None None COc1ccc(-c2cc(C(N)=O)nc3c2CCC(C)(C)O3)c(F)c1 10.1021/acs.jmedchem.1c02004
CHEMBL5089623 217707 None 3 Human Functional pIC50 = 7.0 7.0 - 1
Negative allosteric modulation activity at human recombinant mGlur2 expressed in CHO cells in presence of cAMP by chemiluminescence based assayNegative allosteric modulation activity at human recombinant mGlur2 expressed in CHO cells in presence of cAMP by chemiluminescence based assay
ChEMBL None None None COc1ccc(-c2cc(C(N)=O)nc3c2CCC(C)(C)O3)c(F)c1 10.1021/acs.jmedchem.1c02004
131636318 143681 None 0 Human Functional pIC50 = 7.0 7.0 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 5 0 5 4.6 Cc1cc(-c2nc(-c3ccc(F)c(OCC(F)F)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3899445 143681 None 0 Human Functional pIC50 = 7.0 7.0 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 417 5 0 5 4.6 Cc1cc(-c2nc(-c3ccc(F)c(OCC(F)F)c3)n3c2CCOCC3)cc(C)n1 nan
131636288 160918 None 0 Human Functional pIC50 = 7.0 7.0 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 381 3 0 5 4.3 COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1F nan
CHEMBL4114600 160918 None 0 Human Functional pIC50 = 7.0 7.0 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 381 3 0 5 4.3 COc1ccc(-c2nc(-c3cc(C)nc(C)c3)c3n2C[C@@H](C)OCC3)cc1F nan
90354465 148333 None 0 Human Functional pIC50 = 7.0 7.0 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 4 0 5 4.9 Cc1cc(-c2nc(-c3ccc(OCC(F)(F)F)c(F)c3)n3c2CCOCC3)cc(C)n1 nan
CHEMBL3936284 148333 None 0 Human Functional pIC50 = 7.0 7.0 - 1
[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.[35S]GTPgammaS Binding Assay: The frozen cell membrane fraction prepared as described above was thawed before use, and the resultant was diluted with a buffer for a binding assay (final concentrations: 20 mM HEPES, 100 mM NaCl, 1 mM MgCl2, 3 uM GDP, 300 ug/mL saponin, 0.1% BSA). The compound of each example was added to a cell membrane fraction containing 1.8 to 3 ug/assay of membrane protein on a plate, followed by incubation at room temperature for 30 minutes. Thereafter, with glutamic acid (in a final concentration of 10 uM) added thereto, incubation was performed at room temperature for 15 minutes, and thereafter, [35S]GTPγS (in a final concentration of 0.8 kBq) and 588 ug WGA-SPA beads were added thereto, followed by incubation at room temperature for 1 hour. After the incubation, the plate was subjected to the centrifugal separation at 2,500 rpm and room temperature, and then, membrane cell binding radioactivity was measured with a top count. A [35S]GTPγS binding amount obtained in the presence of glutamic acid was defined as specific binding. On the basis of ratios of inhibiting the specific binding at various concentrations of the compounds of the respective examples, inhibition curves were obtained. Concentrations of the compounds of the respective examples at which the specific [35S]GTPγS binding amount was suppressed by 50% (IC50 values) were calculated on the basis of the inhibition curves.
ChEMBL 435 4 0 5 4.9 Cc1cc(-c2nc(-c3ccc(OCC(F)(F)F)c(F)c3)n3c2CCOCC3)cc(C)n1 nan
44322537 209111 None 0 Human Functional pKi = 6 6.0 - 0
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 517 7 0 7 6.2 CCC1=C(C(=O)OCN(C)C)C(c2ccccc2OC)N2C=C(c3c(Cl)cccc3Cl)SC2=N1 10.1021/jm000007r
CHEMBL89293 209111 None 0 Human Functional pKi = 6 6.0 - 0
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 517 7 0 7 6.2 CCC1=C(C(=O)OCN(C)C)C(c2ccccc2OC)N2C=C(c3c(Cl)cccc3Cl)SC2=N1 10.1021/jm000007r
1393 1539 None 42 Human Functional pKi = 8.0 8.0 2 6
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm000007r
1396 1539 None 42 Human Functional pKi = 8.0 8.0 2 6
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm000007r
213056 1539 None 42 Human Functional pKi = 8.0 8.0 2 6
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm000007r
CHEMBL8759 1539 None 42 Human Functional pKi = 8.0 8.0 2 6
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm000007r
10428048 3361 None 25 Human Functional pKi = 7.0 7.0 -3 2
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 351 4 0 4 5.3 Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl 10.1021/jm000007r
3955 3361 None 25 Human Functional pKi = 7.0 7.0 -3 2
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 351 4 0 4 5.3 Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl 10.1021/jm000007r
CHEMBL305406 3361 None 25 Human Functional pKi = 7.0 7.0 -3 2
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 351 4 0 4 5.3 Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl 10.1021/jm000007r
44322840 112634 None 0 Human Functional pKi = 7.0 7.0 - 0
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 201 2 4 4 -1.5 N[C@]1(C(=O)O)C2C(C[C@H]1O)[C@@H]2C(=O)O 10.1021/jm000007r
CHEMBL330097 112634 None 0 Human Functional pKi = 7.0 7.0 - 0
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 201 2 4 4 -1.5 N[C@]1(C(=O)O)C2C(C[C@H]1O)[C@@H]2C(=O)O 10.1021/jm000007r
1415 2614 None 31 Human Functional pKi = 5.0 5.0 - 2
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 245 3 4 3 -0.3 OC(=O)C(c1ccc(cc1)P(=O)(O)O)(N)C 10.1021/jm000007r
3972752 2614 None 31 Human Functional pKi = 5.0 5.0 - 2
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 245 3 4 3 -0.3 OC(=O)C(c1ccc(cc1)P(=O)(O)O)(N)C 10.1021/jm000007r
CHEMBL86508 2614 None 31 Human Functional pKi = 5.0 5.0 - 2
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 245 3 4 3 -0.3 OC(=O)C(c1ccc(cc1)P(=O)(O)O)(N)C 10.1021/jm000007r
1310 2315 None 61 Human Functional pKi = 4.9 4.9 -389 17
Potency against cloned Metabotropic glutamate receptor 2 agonistPotency against cloned Metabotropic glutamate receptor 2 agonist
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm000007r
1369 2315 None 61 Human Functional pKi = 4.9 4.9 -389 17
Potency against cloned Metabotropic glutamate receptor 2 agonistPotency against cloned Metabotropic glutamate receptor 2 agonist
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm000007r
33032 2315 None 61 Human Functional pKi = 4.9 4.9 -389 17
Potency against cloned Metabotropic glutamate receptor 2 agonistPotency against cloned Metabotropic glutamate receptor 2 agonist
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm000007r
44272391 2315 None 61 Human Functional pKi = 4.9 4.9 -389 17
Potency against cloned Metabotropic glutamate receptor 2 agonistPotency against cloned Metabotropic glutamate receptor 2 agonist
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm000007r
88747398 2315 None 61 Human Functional pKi = 4.9 4.9 -389 17
Potency against cloned Metabotropic glutamate receptor 2 agonistPotency against cloned Metabotropic glutamate receptor 2 agonist
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm000007r
CHEMBL575060 2315 None 61 Human Functional pKi = 4.9 4.9 -389 17
Potency against cloned Metabotropic glutamate receptor 2 agonistPotency against cloned Metabotropic glutamate receptor 2 agonist
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm000007r
DB00142 2315 None 61 Human Functional pKi = 4.9 4.9 -389 17
Potency against cloned Metabotropic glutamate receptor 2 agonistPotency against cloned Metabotropic glutamate receptor 2 agonist
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm000007r
10359073 155064 None 0 Human Functional pKi = 4.8 4.8 -1 2
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 327 8 3 3 2.7 N[C@@H](C[C@H](CC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O 10.1021/jm000007r
CHEMBL40123 155064 None 0 Human Functional pKi = 4.8 4.8 -1 2
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 327 8 3 3 2.7 N[C@@H](C[C@H](CC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O 10.1021/jm000007r
10197984 2421 None 36 Human Functional pKi = 8.6 8.6 1 5
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10.1021/jm000007r
1394 2421 None 36 Human Functional pKi = 8.6 8.6 1 5
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10.1021/jm000007r
CHEMBL275079 2421 None 36 Human Functional pKi = 8.6 8.6 1 5
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10.1021/jm000007r
3246152 161386 None 27 Human Functional pKi = 5.7 5.7 - 0
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 161 4 3 3 -0.5 C[C@@H](C[C@H](N)C(=O)O)C(=O)O 10.1021/jm000007r
CHEMBL41221 161386 None 27 Human Functional pKi = 5.7 5.7 - 0
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 161 4 3 3 -0.5 C[C@@H](C[C@H](N)C(=O)O)C(=O)O 10.1021/jm000007r
1297 170355 None 23 Human Functional pKi = 4.7 4.7 -1 2
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 211 3 4 4 0.2 NC(C(=O)O)c1ccc(C(=O)O)c(O)c1 10.1021/jm000007r
CHEMBL444589 170355 None 23 Human Functional pKi = 4.7 4.7 -1 2
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 211 3 4 4 0.2 NC(C(=O)O)c1ccc(C(=O)O)c(O)c1 10.1021/jm000007r
1378 2417 None 39 Human Functional pKi = 7.7 7.7 -2 14
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/jm000007r
1399 2417 None 39 Human Functional pKi = 7.7 7.7 -2 14
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/jm000007r
9819927 2417 None 39 Human Functional pKi = 7.7 7.7 -2 14
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/jm000007r
CHEMBL432038 2417 None 39 Human Functional pKi = 7.7 7.7 -2 14
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/jm000007r
439282 141671 None 3 Human Functional pKi = 6.6 6.6 - 0
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 159 4 3 3 -0.6 C=C(C[C@H](N)C(=O)O)C(=O)O 10.1021/jm000007r
CHEMBL38499 141671 None 3 Human Functional pKi = 6.6 6.6 - 0
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 159 4 3 3 -0.6 C=C(C[C@H](N)C(=O)O)C(=O)O 10.1021/jm000007r
11820180 18069 None 1 Human Functional pKi = 4.6 4.6 - 0
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 203 4 3 6 -2.1 N[C@@H](CCn1oc(=O)[nH]c1=O)C(=O)O 10.1021/jm000007r
CHEMBL126608 18069 None 1 Human Functional pKi = 4.6 4.6 - 0
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 203 4 3 6 -2.1 N[C@@H](CCn1oc(=O)[nH]c1=O)C(=O)O 10.1021/jm000007r
10058694 209061 None 1 Human Functional pKi = 8.4 8.4 - 0
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 203 2 3 4 -0.8 N[C@@]1(C(=O)O)CSC2C1[C@H]2C(=O)O 10.1021/jm000007r
CHEMBL88999 209061 None 1 Human Functional pKi = 8.4 8.4 - 0
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 203 2 3 4 -0.8 N[C@@]1(C(=O)O)CSC2C1[C@H]2C(=O)O 10.1021/jm000007r
4694355 98793 None 28 Human Functional pKi = 4.5 4.5 - 1
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 257 2 4 3 -0.3 NC1(C(=O)O)CCc2cc(P(=O)(O)O)ccc21 10.1021/jm000007r
CHEMBL277961 98793 None 28 Human Functional pKi = 4.5 4.5 - 1
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 257 2 4 3 -0.3 NC1(C(=O)O)CCc2cc(P(=O)(O)O)ccc21 10.1021/jm000007r
16739377 92210 None 0 Rat Functional pKi = 4.5 4.5 - 0
Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level
ChEMBL 253 4 3 5 1.3 NC(C(=O)O)c1cnn(O)c1CC1CCCCC1 10.1016/j.bmc.2007.02.047
CHEMBL242344 92210 None 0 Rat Functional pKi = 4.5 4.5 - 0
Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level
ChEMBL 253 4 3 5 1.3 NC(C(=O)O)c1cnn(O)c1CC1CCCCC1 10.1016/j.bmc.2007.02.047
16739377 92210 None 0 Rat Functional pKi = 4.5 4.5 - 0
Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level
ChEMBL 253 4 3 5 1.3 NC(C(=O)O)c1cnn(O)c1CC1CCCCC1 10.1016/j.bmc.2007.02.047
CHEMBL242344 92210 None 0 Rat Functional pKi = 4.5 4.5 - 0
Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level
ChEMBL 253 4 3 5 1.3 NC(C(=O)O)c1cnn(O)c1CC1CCCCC1 10.1016/j.bmc.2007.02.047
44322921 209295 None 1 Human Functional pKi = 6.5 6.5 - 0
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 185 2 3 3 -0.5 N[C@@]1(C(=O)O)CC2CC1[C@H]2C(=O)O 10.1021/jm000007r
CHEMBL90501 209295 None 1 Human Functional pKi = 6.5 6.5 - 0
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 185 2 3 3 -0.5 N[C@@]1(C(=O)O)CC2CC1[C@H]2C(=O)O 10.1021/jm000007r
59066632 209028 None 52 Human Functional pKi = 4.5 4.5 1 2
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 161 5 3 3 -0.3 N[C@@H](CCCC(=O)O)C(=O)O 10.1021/jm000007r
92136 209028 None 52 Human Functional pKi = 4.5 4.5 1 2
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 161 5 3 3 -0.3 N[C@@H](CCCC(=O)O)C(=O)O 10.1021/jm000007r
CHEMBL88804 209028 None 52 Human Functional pKi = 4.5 4.5 1 2
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 161 5 3 3 -0.3 N[C@@H](CCCC(=O)O)C(=O)O 10.1021/jm000007r
44322745 106222 None 0 Human Functional pKi = 4.4 4.4 - 0
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 203 3 3 6 -2.1 C[C@](N)(Cn1c(=O)[nH]oc1=O)C(=O)O 10.1021/jm000007r
CHEMBL313713 106222 None 0 Human Functional pKi = 4.4 4.4 - 0
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 203 3 3 6 -2.1 C[C@](N)(Cn1c(=O)[nH]oc1=O)C(=O)O 10.1021/jm000007r
1392 73 None 32 Human Functional pKi = 6.4 6.4 - 4
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 174 2 4 4 -1.8 OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O 10.1021/jm000007r
5310984 73 None 32 Human Functional pKi = 6.4 6.4 - 4
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 174 2 4 4 -1.8 OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O 10.1021/jm000007r
CHEMBL40086 73 None 32 Human Functional pKi = 6.4 6.4 - 4
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 174 2 4 4 -1.8 OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O 10.1021/jm000007r
10330132 101437 None 1 Human Functional pKi = 5.3 5.3 - 2
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 189 2 4 5 -2.2 NN1C[C@@](N)(C(=O)O)C[C@@H]1C(=O)O 10.1021/jm000007r
CHEMBL297150 101437 None 1 Human Functional pKi = 5.3 5.3 - 2
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 189 2 4 5 -2.2 NN1C[C@@](N)(C(=O)O)C[C@@H]1C(=O)O 10.1021/jm000007r
1368 2290 None 30 Human Functional pKi = 6.3 6.3 1 11
Agonist potency against cloned Metabotropic glutamate receptor 2 agonistAgonist potency against cloned Metabotropic glutamate receptor 2 agonist
ChEMBL 159 3 3 3 -0.9 N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O 10.1021/jm000007r
5310956 2290 None 30 Human Functional pKi = 6.3 6.3 1 11
Agonist potency against cloned Metabotropic glutamate receptor 2 agonistAgonist potency against cloned Metabotropic glutamate receptor 2 agonist
ChEMBL 159 3 3 3 -0.9 N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O 10.1021/jm000007r
CHEMBL280563 2290 None 30 Human Functional pKi = 6.3 6.3 1 11
Agonist potency against cloned Metabotropic glutamate receptor 2 agonistAgonist potency against cloned Metabotropic glutamate receptor 2 agonist
ChEMBL 159 3 3 3 -0.9 N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O 10.1021/jm000007r
104766 33 None 30 Human Functional pKi = 5.3 5.3 -2 14
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1021/jm000007r
1365 33 None 30 Human Functional pKi = 5.3 5.3 -2 14
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1021/jm000007r
CHEMBL34453 33 None 30 Human Functional pKi = 5.3 5.3 -2 14
Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).Agonist potency against cloned Metabotropic glutamate receptor 2 (mGluR-2).
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1021/jm000007r
6324634 148032 None 10 Human Functional pKi = 4.3 4.3 6 2
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 355 10 3 3 3.5 N[C@@H](C[C@H](CCCC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O 10.1021/jm000007r
CHEMBL39338 148032 None 10 Human Functional pKi = 4.3 4.3 6 2
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 355 10 3 3 3.5 N[C@@H](C[C@H](CCCC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O 10.1021/jm000007r
1222 101792 None 46 Human Functional pKi = 4.3 4.3 - 1
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 209 3 3 3 0.6 CC(N)(C(=O)O)c1ccc(C(=O)O)cc1 10.1021/jm000007r
CHEMBL299683 101792 None 46 Human Functional pKi = 4.3 4.3 - 1
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 209 3 3 3 0.6 CC(N)(C(=O)O)c1ccc(C(=O)O)cc1 10.1021/jm000007r
10198359 73984 None 10 Human Functional pKi = 4.3 4.3 -10 4
Partial agonist potency against cloned Metabotropic glutamate receptor 2Partial agonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 221 3 3 3 -0.8 N[C@H](C(=O)O)C12C3C4C1C1C2C3C41C(=O)O 10.1021/jm000007r
CHEMBL2021372 73984 None 10 Human Functional pKi = 4.3 4.3 -10 4
Partial agonist potency against cloned Metabotropic glutamate receptor 2Partial agonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 221 3 3 3 -0.8 N[C@H](C(=O)O)C12C3C4C1C1C2C3C41C(=O)O 10.1021/jm000007r
44428738 168853 None 0 Rat Functional pKi = 4.2 4.2 - 0
Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level
ChEMBL 275 6 3 5 1.4 NC(C(=O)O)c1cnn(O)c1CCCc1ccccc1 10.1016/j.bmc.2007.02.047
CHEMBL437169 168853 None 0 Rat Functional pKi = 4.2 4.2 - 0
Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level
ChEMBL 275 6 3 5 1.4 NC(C(=O)O)c1cnn(O)c1CCCc1ccccc1 10.1016/j.bmc.2007.02.047
44428738 168853 None 0 Rat Functional pKi = 4.2 4.2 - 0
Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level
ChEMBL 275 6 3 5 1.4 NC(C(=O)O)c1cnn(O)c1CCCc1ccccc1 10.1016/j.bmc.2007.02.047
CHEMBL437169 168853 None 0 Rat Functional pKi = 4.2 4.2 - 0
Antagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP levelAntagonist activity at rat mGluR2 receptor expressed in CHO cells assessed as effect on intracellular cAMP level
ChEMBL 275 6 3 5 1.4 NC(C(=O)O)c1cnn(O)c1CCCc1ccccc1 10.1016/j.bmc.2007.02.047
44322529 209324 None 1 Human Functional pKi = 7.1 7.1 - 0
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 367 6 3 4 3.1 N[C@H](C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1CCC1c2ccccc2Oc2ccccc21 10.1021/jm000007r
CHEMBL90675 209324 None 1 Human Functional pKi = 7.1 7.1 - 0
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 367 6 3 4 3.1 N[C@H](C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1CCC1c2ccccc2Oc2ccccc21 10.1021/jm000007r
1439 2469 None 12 Human Functional pKi = 4.1 4.1 - 1
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 173 3 3 3 -0.5 OC(=O)[C@H]1C[C@@H]1[C@@](C(=O)O)(N)C 10.1021/jm000007r
5311457 2469 None 12 Human Functional pKi = 4.1 4.1 - 1
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 173 3 3 3 -0.5 OC(=O)[C@H]1C[C@@H]1[C@@](C(=O)O)(N)C 10.1021/jm000007r
CHEMBL41013 2469 None 12 Human Functional pKi = 4.1 4.1 - 1
Antagonist potency against cloned Metabotropic glutamate receptor 2Antagonist potency against cloned Metabotropic glutamate receptor 2
ChEMBL 173 3 3 3 -0.5 OC(=O)[C@H]1C[C@@H]1[C@@](C(=O)O)(N)C 10.1021/jm000007r
1310 2315 None 61 Rat Functional pEC50 = 8.3 8.3 -457 17
NoneNone
Drug Central 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
1369 2315 None 61 Rat Functional pEC50 = 8.3 8.3 -457 17
NoneNone
Drug Central 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
33032 2315 None 61 Rat Functional pEC50 = 8.3 8.3 -457 17
NoneNone
Drug Central 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
44272391 2315 None 61 Rat Functional pEC50 = 8.3 8.3 -457 17
NoneNone
Drug Central 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
88747398 2315 None 61 Rat Functional pEC50 = 8.3 8.3 -457 17
NoneNone
Drug Central 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
CHEMBL575060 2315 None 61 Rat Functional pEC50 = 8.3 8.3 -457 17
NoneNone
Drug Central 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
DB00142 2315 None 61 Rat Functional pEC50 = 8.3 8.3 -457 17
NoneNone
Drug Central 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
1310 2315 None 61 Human Functional pEC50 = 8.2 8.2 -389 17
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
Drug Central 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
1369 2315 None 61 Human Functional pEC50 = 8.2 8.2 -389 17
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
Drug Central 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
33032 2315 None 61 Human Functional pEC50 = 8.2 8.2 -389 17
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
Drug Central 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
44272391 2315 None 61 Human Functional pEC50 = 8.2 8.2 -389 17
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
Drug Central 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
88747398 2315 None 61 Human Functional pEC50 = 8.2 8.2 -389 17
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
Drug Central 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
CHEMBL575060 2315 None 61 Human Functional pEC50 = 8.2 8.2 -389 17
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
Drug Central 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
DB00142 2315 None 61 Human Functional pEC50 = 8.2 8.2 -389 17
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
Drug Central 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
25195461 2144 None 42 Human Functional pEC50 = 6.8 6.8 - 1
Measured in a [<sup>35</sup>S]GTP&gamma;S binding assay with human metabotropic glutamate type 2 receptor expressed in CHO cells.Measured in a [<sup>35</sup>S]GTP&gamma;S binding assay with human metabotropic glutamate type 2 receptor expressed in CHO cells.
Guide to Pharmacology 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 25692015
8946 2144 None 42 Human Functional pEC50 = 6.8 6.8 - 1
Measured in a [<sup>35</sup>S]GTP&gamma;S binding assay with human metabotropic glutamate type 2 receptor expressed in CHO cells.Measured in a [<sup>35</sup>S]GTP&gamma;S binding assay with human metabotropic glutamate type 2 receptor expressed in CHO cells.
Guide to Pharmacology 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 25692015
CHEMBL3337527 2144 None 42 Human Functional pEC50 = 6.8 6.8 - 1
Measured in a [<sup>35</sup>S]GTP&gamma;S binding assay with human metabotropic glutamate type 2 receptor expressed in CHO cells.Measured in a [<sup>35</sup>S]GTP&gamma;S binding assay with human metabotropic glutamate type 2 receptor expressed in CHO cells.
Guide to Pharmacology 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 25692015
DB12059 2144 None 42 Human Functional pEC50 = 6.8 6.8 - 1
Measured in a [<sup>35</sup>S]GTP&gamma;S binding assay with human metabotropic glutamate type 2 receptor expressed in CHO cells.Measured in a [<sup>35</sup>S]GTP&gamma;S binding assay with human metabotropic glutamate type 2 receptor expressed in CHO cells.
Guide to Pharmacology 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 25692015
1310 2315 None 61 Human Functional pEC50 = 5.1 5.1 -389 17
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10443583
1369 2315 None 61 Human Functional pEC50 = 5.1 5.1 -389 17
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10443583
33032 2315 None 61 Human Functional pEC50 = 5.1 5.1 -389 17
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10443583
44272391 2315 None 61 Human Functional pEC50 = 5.1 5.1 -389 17
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10443583
88747398 2315 None 61 Human Functional pEC50 = 5.1 5.1 -389 17
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10443583
CHEMBL575060 2315 None 61 Human Functional pEC50 = 5.1 5.1 -389 17
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10443583
DB00142 2315 None 61 Human Functional pEC50 = 5.1 5.1 -389 17
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10443583
11281345 113 None 0 Human Functional pEC50 = 5.7 5.7 - 1
UnclassifiedUnclassified
Guide to Pharmacology 411 8 1 5 3.3 CCS(=O)(=O)N(c1ccc(cc1)Oc1ccc(cc1)C(=O)N)Cc1cccnc1 15717213
6258 113 None 0 Human Functional pEC50 = 5.7 5.7 - 1
UnclassifiedUnclassified
Guide to Pharmacology 411 8 1 5 3.3 CCS(=O)(=O)N(c1ccc(cc1)Oc1ccc(cc1)C(=O)N)Cc1cccnc1 15717213
25002940 1105 None 0 Human Functional pEC50 = 6.4 6.4 - 1
UnclassifiedUnclassified
Guide to Pharmacology 377 6 0 5 4.8 CCCCn1ccc(c(c1=O)C#N)c1ccc(c(c1)F)Oc1ccnc(c1)C 22364337
6320 1105 None 0 Human Functional pEC50 = 6.4 6.4 - 1
UnclassifiedUnclassified
Guide to Pharmacology 377 6 0 5 4.8 CCCCn1ccc(c(c1=O)C#N)c1ccc(c(c1)F)Oc1ccnc(c1)C 22364337
CHEMBL2029821 1105 None 0 Human Functional pEC50 = 6.4 6.4 - 1
UnclassifiedUnclassified
Guide to Pharmacology 377 6 0 5 4.8 CCCCn1ccc(c(c1=O)C#N)c1ccc(c(c1)F)Oc1ccnc(c1)C 22364337
25125217 555 None 27 Human Functional pEC50 = 6.7 6.7 - 1
UnclassifiedUnclassified
Guide to Pharmacology 487 6 1 7 3.5 Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1 None
7678 555 None 27 Human Functional pEC50 = 6.7 6.7 - 1
UnclassifiedUnclassified
Guide to Pharmacology 487 6 1 7 3.5 Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1 None
CHEMBL3937907 555 None 27 Human Functional pEC50 = 6.7 6.7 - 1
UnclassifiedUnclassified
Guide to Pharmacology 487 6 1 7 3.5 Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1 None
DB16073 555 None 27 Human Functional pEC50 = 6.7 6.7 - 1
UnclassifiedUnclassified
Guide to Pharmacology 487 6 1 7 3.5 Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1 None
46182736 989 None 0 Rat Functional pEC50 = 6.8 6.8 - 1
UnclassifiedUnclassified
Guide to Pharmacology 479 6 1 5 6.8 OC(=O)c1cc(ccc1Cl)c1cccc(c1)COc1ccc2c(c1)sn(c2=O)C1CCCC1 21155570
6323 989 None 0 Rat Functional pEC50 = 6.8 6.8 - 1
UnclassifiedUnclassified
Guide to Pharmacology 479 6 1 5 6.8 OC(=O)c1cc(ccc1Cl)c1cccc(c1)COc1ccc2c(c1)sn(c2=O)C1CCCC1 21155570
CHEMBL1651219 989 None 0 Rat Functional pEC50 = 6.8 6.8 - 1
UnclassifiedUnclassified
Guide to Pharmacology 479 6 1 5 6.8 OC(=O)c1cc(ccc1Cl)c1cccc(c1)COc1ccc2c(c1)sn(c2=O)C1CCCC1 21155570
46190878 1872 None 8 Human Functional pEC50 = 6.9 6.9 - 1
UnclassifiedUnclassified
Guide to Pharmacology 342 3 0 6 2.3 Clc1cnc(nc1)N1CCN(CC1)Cc1nc2c(n1C)cccc2 20005096
6253 1872 None 8 Human Functional pEC50 = 6.9 6.9 - 1
UnclassifiedUnclassified
Guide to Pharmacology 342 3 0 6 2.3 Clc1cnc(nc1)N1CCN(CC1)Cc1nc2c(n1C)cccc2 20005096
CHEMBL595759 1872 None 8 Human Functional pEC50 = 6.9 6.9 - 1
UnclassifiedUnclassified
Guide to Pharmacology 342 3 0 6 2.3 Clc1cnc(nc1)N1CCN(CC1)Cc1nc2c(n1C)cccc2 20005096
3954 664 None 44 Human Functional pEC50 = 7 7.0 6 3
UnclassifiedUnclassified
Guide to Pharmacology 454 6 1 3 6.8 Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1 16046122
9868580 664 None 44 Human Functional pEC50 = 7 7.0 6 3
UnclassifiedUnclassified
Guide to Pharmacology 454 6 1 3 6.8 Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1 16046122
CHEMBL593013 664 None 44 Human Functional pEC50 = 7 7.0 6 3
UnclassifiedUnclassified
Guide to Pharmacology 454 6 1 3 6.8 Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1 16046122
3372 813 None 0 Human Functional pEC50 = 7 7.0 - 1
UnclassifiedUnclassified
Guide to Pharmacology 377 6 0 4 4.0 N#Cc1ccc(cc1)c1cccc(c1)N(S(=O)(=O)CC)Cc1cccnc1 15717213
9864510 813 None 0 Human Functional pEC50 = 7 7.0 - 1
UnclassifiedUnclassified
Guide to Pharmacology 377 6 0 4 4.0 N#Cc1ccc(cc1)c1cccc(c1)N(S(=O)(=O)CC)Cc1cccnc1 15717213
CHEMBL4303163 813 None 0 Human Functional pEC50 = 7 7.0 - 1
UnclassifiedUnclassified
Guide to Pharmacology 377 6 0 4 4.0 N#Cc1ccc(cc1)c1cccc(c1)N(S(=O)(=O)CC)Cc1cccnc1 15717213
46830123 1073 None 0 Human Functional pEC50 = 7.1 7.1 - 1
UnclassifiedUnclassified
Guide to Pharmacology 350 4 0 4 4.3 N#Cc1cccc(c1)N1C[C@H](OC1=O)COc1ccc(cc1)C(C)(C)C 20409708
6321 1073 None 0 Human Functional pEC50 = 7.1 7.1 - 1
UnclassifiedUnclassified
Guide to Pharmacology 350 4 0 4 4.3 N#Cc1cccc(c1)N1C[C@H](OC1=O)COc1ccc(cc1)C(C)(C)C 20409708
CHEMBL1094763 1073 None 0 Human Functional pEC50 = 7.1 7.1 - 1
UnclassifiedUnclassified
Guide to Pharmacology 350 4 0 4 4.3 N#Cc1cccc(c1)N1C[C@H](OC1=O)COc1ccc(cc1)C(C)(C)C 20409708
46190877 1871 None 8 Human Functional pEC50 = 7.1 7.1 - 1
UnclassifiedUnclassified
Guide to Pharmacology 409 3 0 5 4.0 Clc1cc(cnc1N1CCN(CC1)Cc1nc2c(n1C)cccc2)C(F)(F)F 20005096
6252 1871 None 8 Human Functional pEC50 = 7.1 7.1 - 1
UnclassifiedUnclassified
Guide to Pharmacology 409 3 0 5 4.0 Clc1cc(cnc1N1CCN(CC1)Cc1nc2c(n1C)cccc2)C(F)(F)F 20005096
CHEMBL605836 1871 None 8 Human Functional pEC50 = 7.1 7.1 - 1
UnclassifiedUnclassified
Guide to Pharmacology 409 3 0 5 4.0 Clc1cc(cnc1N1CCN(CC1)Cc1nc2c(n1C)cccc2)C(F)(F)F 20005096
6256 1009 None 0 Rat Functional pEC50 = 7.2 7.2 - 1
UnclassifiedUnclassified
Guide to Pharmacology 382 6 0 5 3.5 Clc1cccc(c1)COC[C@@H]1[C@@H]2[C@H]1CN(C2)Cc1nc2c(n1C)cccn2 18812259
73755202 1009 None 0 Rat Functional pEC50 = 7.2 7.2 - 1
UnclassifiedUnclassified
Guide to Pharmacology 382 6 0 5 3.5 Clc1cccc(c1)COC[C@@H]1[C@@H]2[C@H]1CN(C2)Cc1nc2c(n1C)cccn2 18812259
59234231 2143 None 4 Rat Functional pEC50 = 7.3 7.3 1 2
UnclassifiedUnclassified
Guide to Pharmacology 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 23766542
6330 2143 None 4 Rat Functional pEC50 = 7.3 7.3 1 2
UnclassifiedUnclassified
Guide to Pharmacology 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 23766542
6331 2143 None 4 Rat Functional pEC50 = 7.3 7.3 1 2
UnclassifiedUnclassified
Guide to Pharmacology 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 23766542
CHEMBL3337510 2143 None 4 Rat Functional pEC50 = 7.3 7.3 1 2
UnclassifiedUnclassified
Guide to Pharmacology 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 23766542
59234231 2143 None 4 Human Functional pEC50 = 7.3 7.3 -1 2
UnclassifiedUnclassified
Guide to Pharmacology 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 23766542
6330 2143 None 4 Human Functional pEC50 = 7.3 7.3 -1 2
UnclassifiedUnclassified
Guide to Pharmacology 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 23766542
6331 2143 None 4 Human Functional pEC50 = 7.3 7.3 -1 2
UnclassifiedUnclassified
Guide to Pharmacology 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 23766542
CHEMBL3337510 2143 None 4 Human Functional pEC50 = 7.3 7.3 -1 2
UnclassifiedUnclassified
Guide to Pharmacology 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 23766542
6255 987 None 0 Rat Functional pEC50 = 7.5 7.5 - 1
UnclassifiedUnclassified
Guide to Pharmacology 416 6 0 5 3.9 Cn1c(CN2C[C@@H]3[C@H](C2)[C@H]3COCc2ccc(cn2)C(F)(F)F)nc2c1cccc2 18812259
73755201 987 None 0 Rat Functional pEC50 = 7.5 7.5 - 1
UnclassifiedUnclassified
Guide to Pharmacology 416 6 0 5 3.9 Cn1c(CN2C[C@@H]3[C@H](C2)[C@H]3COCc2ccc(cn2)C(F)(F)F)nc2c1cccc2 18812259
6254 985 None 0 Rat Functional pEC50 = 7.6 7.6 - 1
UnclassifiedUnclassified
Guide to Pharmacology 382 6 0 5 3.5 Clc1ccc(nc1)COC[C@@H]1[C@@H]2[C@H]1CN(C2)Cc1nc2c(n1C)cccc2 18812259
73755200 985 None 0 Rat Functional pEC50 = 7.6 7.6 - 1
UnclassifiedUnclassified
Guide to Pharmacology 382 6 0 5 3.5 Clc1ccc(nc1)COC[C@@H]1[C@@H]2[C@H]1CN(C2)Cc1nc2c(n1C)cccc2 18812259
44335556 1300 None 0 Human Functional pEC50 = 7.6 7.6 - 1
UnclassifiedUnclassified
Guide to Pharmacology 414 7 0 4 4.3 FC(CS(=O)(=O)N(c1cccc(c1)OC1CCCC1)Cc1cccnc1)(F)F 15717213
6257 1300 None 0 Human Functional pEC50 = 7.6 7.6 - 1
UnclassifiedUnclassified
Guide to Pharmacology 414 7 0 4 4.3 FC(CS(=O)(=O)N(c1cccc(c1)OC1CCCC1)Cc1cccnc1)(F)F 15717213
CHEMBL321968 1300 None 0 Human Functional pEC50 = 7.6 7.6 - 1
UnclassifiedUnclassified
Guide to Pharmacology 414 7 0 4 4.3 FC(CS(=O)(=O)N(c1cccc(c1)OC1CCCC1)Cc1cccnc1)(F)F 15717213
44595851 3802 None 6 Human Functional pEC50 = 7.7 7.7 -3 2
UnclassifiedUnclassified
Guide to Pharmacology 475 8 2 6 4.5 Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C 20947638
6259 3802 None 6 Human Functional pEC50 = 7.7 7.7 -3 2
UnclassifiedUnclassified
Guide to Pharmacology 475 8 2 6 4.5 Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C 20947638
CHEMBL4092105 3802 None 6 Human Functional pEC50 = 7.7 7.7 -3 2
UnclassifiedUnclassified
Guide to Pharmacology 475 8 2 6 4.5 Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C 20947638
49765871 2145 None 41 Human Functional pEC50 = 7.8 7.8 - 1
UnclassifiedUnclassified
Guide to Pharmacology 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 23072213
6317 2145 None 41 Human Functional pEC50 = 7.8 7.8 - 1
UnclassifiedUnclassified
Guide to Pharmacology 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 23072213
CHEMBL2179319 2145 None 41 Human Functional pEC50 = 7.8 7.8 - 1
UnclassifiedUnclassified
Guide to Pharmacology 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 23072213
11362035 42 None 1 Human Functional pEC50 = 7.9 7.9 - 1
UnclassifiedUnclassified
Guide to Pharmacology 416 9 0 4 4.5 CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C 15149652
6328 42 None 1 Human Functional pEC50 = 7.9 7.9 - 1
UnclassifiedUnclassified
Guide to Pharmacology 416 9 0 4 4.5 CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C 15149652
6329 42 None 1 Human Functional pEC50 = 7.9 7.9 - 1
UnclassifiedUnclassified
Guide to Pharmacology 416 9 0 4 4.5 CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C 15149652
CHEMBL105296 42 None 1 Human Functional pEC50 = 7.9 7.9 - 1
UnclassifiedUnclassified
Guide to Pharmacology 416 9 0 4 4.5 CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C 15149652
44595851 3802 None 6 Rat Functional pEC50 = 7.9 7.9 3 2
UnclassifiedUnclassified
Guide to Pharmacology 475 8 2 6 4.5 Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C 20947638
6259 3802 None 6 Rat Functional pEC50 = 7.9 7.9 3 2
UnclassifiedUnclassified
Guide to Pharmacology 475 8 2 6 4.5 Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C 20947638
CHEMBL4092105 3802 None 6 Rat Functional pEC50 = 7.9 7.9 3 2
UnclassifiedUnclassified
Guide to Pharmacology 475 8 2 6 4.5 Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C 20947638
3335 3015 None 1 Rat Functional pIC50 = 5.1 5.1 -1 2
UnclassifiedUnclassified
Guide to Pharmacology 235 4 3 3 0.5 OC(=O)[C@H]([C@H]1[C@H]([C@@H]1C(=O)O)c1ccccc1)N 8667369
5311344 3015 None 1 Rat Functional pIC50 = 5.1 5.1 -1 2
UnclassifiedUnclassified
Guide to Pharmacology 235 4 3 3 0.5 OC(=O)[C@H]([C@H]1[C@H]([C@@H]1C(=O)O)c1ccccc1)N 8667369
CHEMBL39573 3015 None 1 Rat Functional pIC50 = 5.1 5.1 -1 2
UnclassifiedUnclassified
Guide to Pharmacology 235 4 3 3 0.5 OC(=O)[C@H]([C@H]1[C@H]([C@@H]1C(=O)O)c1ccccc1)N 8667369
1402 122 None 35 Human Functional pIC50 = 5.8 5.8 - 1
UnclassifiedUnclassified
Guide to Pharmacology 452 8 0 5 4.8 COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 12852748
1402 122 None 35 Human Functional pIC50 = 5.8 5.8 - 1
UnclassifiedUnclassified
Guide to Pharmacology 452 8 0 5 4.8 COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 14500736
1402 122 None 35 Human Functional pIC50 = 5.8 5.8 - 1
UnclassifiedUnclassified
Guide to Pharmacology 452 8 0 5 4.8 COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 15149652
1402 122 None 35 Human Functional pIC50 = 5.8 5.8 - 1
UnclassifiedUnclassified
Guide to Pharmacology 452 8 0 5 4.8 COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 15717213
9825084 122 None 35 Human Functional pIC50 = 5.8 5.8 - 1
UnclassifiedUnclassified
Guide to Pharmacology 452 8 0 5 4.8 COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 12852748
9825084 122 None 35 Human Functional pIC50 = 5.8 5.8 - 1
UnclassifiedUnclassified
Guide to Pharmacology 452 8 0 5 4.8 COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 14500736
9825084 122 None 35 Human Functional pIC50 = 5.8 5.8 - 1
UnclassifiedUnclassified
Guide to Pharmacology 452 8 0 5 4.8 COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 15149652
9825084 122 None 35 Human Functional pIC50 = 5.8 5.8 - 1
UnclassifiedUnclassified
Guide to Pharmacology 452 8 0 5 4.8 COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 15717213
CHEMBL108939 122 None 35 Human Functional pIC50 = 5.8 5.8 - 1
UnclassifiedUnclassified
Guide to Pharmacology 452 8 0 5 4.8 COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 12852748
CHEMBL108939 122 None 35 Human Functional pIC50 = 5.8 5.8 - 1
UnclassifiedUnclassified
Guide to Pharmacology 452 8 0 5 4.8 COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 14500736
CHEMBL108939 122 None 35 Human Functional pIC50 = 5.8 5.8 - 1
UnclassifiedUnclassified
Guide to Pharmacology 452 8 0 5 4.8 COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 15149652
CHEMBL108939 122 None 35 Human Functional pIC50 = 5.8 5.8 - 1
UnclassifiedUnclassified
Guide to Pharmacology 452 8 0 5 4.8 COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 15717213
49858117 1089 None 4 Human Functional pIC50 = 5.8 5.8 5 2
UnclassifiedUnclassified
Guide to Pharmacology 308 2 2 4 3.0 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)C 21105727
6223 1089 None 4 Human Functional pIC50 = 5.8 5.8 5 2
UnclassifiedUnclassified
Guide to Pharmacology 308 2 2 4 3.0 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)C 21105727
CHEMBL1630806 1089 None 4 Human Functional pIC50 = 5.8 5.8 5 2
UnclassifiedUnclassified
Guide to Pharmacology 308 2 2 4 3.0 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)C 21105727
49858118 1110 None 0 Human Functional pIC50 = 6 6.0 10 2
UnclassifiedUnclassified
Guide to Pharmacology 324 3 2 5 2.7 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)OC 21105727
6224 1110 None 0 Human Functional pIC50 = 6 6.0 10 2
UnclassifiedUnclassified
Guide to Pharmacology 324 3 2 5 2.7 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)OC 21105727
CHEMBL1630807 1110 None 0 Human Functional pIC50 = 6 6.0 10 2
UnclassifiedUnclassified
Guide to Pharmacology 324 3 2 5 2.7 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)OC 21105727
49836087 1061 None 0 Human Functional pIC50 = 6.1 6.1 16 2
UnclassifiedUnclassified
Guide to Pharmacology 328 2 2 4 3.3 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)Cl 21105727
6222 1061 None 0 Human Functional pIC50 = 6.1 6.1 16 2
UnclassifiedUnclassified
Guide to Pharmacology 328 2 2 4 3.3 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)Cl 21105727
CHEMBL1630805 1061 None 0 Human Functional pIC50 = 6.1 6.1 16 2
UnclassifiedUnclassified
Guide to Pharmacology 328 2 2 4 3.3 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)Cl 21105727
10428048 3361 None 25 Rat Functional pIC50 = 7 7.0 3 2
UnclassifiedUnclassified
Guide to Pharmacology 351 4 0 4 5.3 Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl 10465539
3955 3361 None 25 Rat Functional pIC50 = 7 7.0 3 2
UnclassifiedUnclassified
Guide to Pharmacology 351 4 0 4 5.3 Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl 10465539
CHEMBL305406 3361 None 25 Rat Functional pIC50 = 7 7.0 3 2
UnclassifiedUnclassified
Guide to Pharmacology 351 4 0 4 5.3 Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl 10465539
6219 2585 None 0 Human Functional pIC50 = 7.5 7.5 -1 3
UnclassifiedUnclassified
Guide to Pharmacology 401 1 1 3 4.0 N#Cc1cccc(c1)C1=Nc2ccc(cc2NC(=O)CC1)I 17416742
73755191 2585 None 0 Human Functional pIC50 = 7.5 7.5 -1 3
UnclassifiedUnclassified
Guide to Pharmacology 401 1 1 3 4.0 N#Cc1cccc(c1)C1=Nc2ccc(cc2NC(=O)CC1)I 17416742
6221 2587 None 0 Human Functional pIC50 = 7.5 7.5 -2 3
UnclassifiedUnclassified
Guide to Pharmacology 354 1 1 4 3.6 N#Cc1nccc(c1)C1=Nc2ccc(cc2NC(=O)CC1)Br 17416742
73755193 2587 None 0 Human Functional pIC50 = 7.5 7.5 -2 3
UnclassifiedUnclassified
Guide to Pharmacology 354 1 1 4 3.6 N#Cc1nccc(c1)C1=Nc2ccc(cc2NC(=O)CC1)Br 17416742
11158623 3351 None 11 Rat Functional pIC50 = 7.6 7.6 1 4
UnclassifiedUnclassified
Guide to Pharmacology 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 20971004
11158623 3351 None 11 Rat Functional pIC50 = 7.6 7.6 1 4
UnclassifiedUnclassified
Guide to Pharmacology 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 22091727
6226 3351 None 11 Rat Functional pIC50 = 7.6 7.6 1 4
UnclassifiedUnclassified
Guide to Pharmacology 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 20971004
6226 3351 None 11 Rat Functional pIC50 = 7.6 7.6 1 4
UnclassifiedUnclassified
Guide to Pharmacology 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 22091727
CHEMBL1629855 3351 None 11 Rat Functional pIC50 = 7.6 7.6 1 4
UnclassifiedUnclassified
Guide to Pharmacology 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 20971004
CHEMBL1629855 3351 None 11 Rat Functional pIC50 = 7.6 7.6 1 4
UnclassifiedUnclassified
Guide to Pharmacology 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 22091727
6219 2585 None 0 Rat Functional pIC50 = 7.6 7.6 1 3
UnclassifiedUnclassified
Guide to Pharmacology 401 1 1 3 4.0 N#Cc1cccc(c1)C1=Nc2ccc(cc2NC(=O)CC1)I 17416742
73755191 2585 None 0 Rat Functional pIC50 = 7.6 7.6 1 3
UnclassifiedUnclassified
Guide to Pharmacology 401 1 1 3 4.0 N#Cc1cccc(c1)C1=Nc2ccc(cc2NC(=O)CC1)I 17416742
6220 2586 None 0 Rat Functional pIC50 = 7.7 7.7 -1 3
UnclassifiedUnclassified
Guide to Pharmacology 405 2 1 3 5.4 O=C1CCC(=Nc2c(N1)ccc(c2)Br)c1cccc(c1)c1ccncc1 17416742
73755192 2586 None 0 Rat Functional pIC50 = 7.7 7.7 -1 3
UnclassifiedUnclassified
Guide to Pharmacology 405 2 1 3 5.4 O=C1CCC(=Nc2c(N1)ccc(c2)Br)c1cccc(c1)c1ccncc1 17416742
6220 2586 None 0 Human Functional pIC50 = 7.7 7.7 1 3
UnclassifiedUnclassified
Guide to Pharmacology 405 2 1 3 5.4 O=C1CCC(=Nc2c(N1)ccc(c2)Br)c1cccc(c1)c1ccncc1 17416742
73755192 2586 None 0 Human Functional pIC50 = 7.7 7.7 1 3
UnclassifiedUnclassified
Guide to Pharmacology 405 2 1 3 5.4 O=C1CCC(=Nc2c(N1)ccc(c2)Br)c1cccc(c1)c1ccncc1 17416742
11158623 3351 None 11 Human Functional pIC50 = 7.9 7.9 -7 4
UnclassifiedUnclassified
Guide to Pharmacology 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 20971004
6226 3351 None 11 Human Functional pIC50 = 7.9 7.9 -7 4
UnclassifiedUnclassified
Guide to Pharmacology 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 20971004
CHEMBL1629855 3351 None 11 Human Functional pIC50 = 7.9 7.9 -7 4
UnclassifiedUnclassified
Guide to Pharmacology 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 20971004
6221 2587 None 0 Rat Functional pIC50 = 7.9 7.9 1 3
UnclassifiedUnclassified
Guide to Pharmacology 354 1 1 4 3.6 N#Cc1nccc(c1)C1=Nc2ccc(cc2NC(=O)CC1)Br 17416742
73755193 2587 None 0 Rat Functional pIC50 = 7.9 7.9 1 3
UnclassifiedUnclassified
Guide to Pharmacology 354 1 1 4 3.6 N#Cc1nccc(c1)C1=Nc2ccc(cc2NC(=O)CC1)Br 17416742
6324 3353 None 0 Rat Functional pIC50 = 8.3 8.3 - 1
UnclassifiedUnclassified
Guide to Pharmacology 512 2 1 6 4.5 FC(c1cc(nc2n1ncc2C#Cc1cncc(c1)S(=O)(=O)O)c1ccc(cc1)C(F)(F)F)(F)F 21470207
73755205 3353 None 0 Rat Functional pIC50 = 8.3 8.3 - 1
UnclassifiedUnclassified
Guide to Pharmacology 512 2 1 6 4.5 FC(c1cc(nc2n1ncc2C#Cc1cncc(c1)S(=O)(=O)O)c1ccc(cc1)C(F)(F)F)(F)F 21470207
10047169 3224 None 0 Human Functional pIC50 None 6.5 6.5 - 1
UnclassifiedUnclassified
Guide to Pharmacology 410 11 2 7 4.0 CCCc1c(OCCCCOc2ccc(cc2)c2n[nH]nn2)ccc(c1O)C(=O)C 15317469
1403 3224 None 0 Human Functional pIC50 None 6.5 6.5 - 1
UnclassifiedUnclassified
Guide to Pharmacology 410 11 2 7 4.0 CCCc1c(OCCCCOc2ccc(cc2)c2n[nH]nn2)ccc(c1O)C(=O)C 15317469
CHEMBL182371 3224 None 0 Human Functional pIC50 None 6.5 6.5 - 1
UnclassifiedUnclassified
Guide to Pharmacology 410 11 2 7 4.0 CCCc1c(OCCCCOc2ccc(cc2)c2n[nH]nn2)ccc(c1O)C(=O)C 15317469
10275802 107 None 0 Human Functional pIC50 None 6.6 6.6 - 1
UnclassifiedUnclassified
Guide to Pharmacology 452 8 0 5 4.8 COc1ccccc1Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 12852748
10275802 107 None 0 Human Functional pIC50 None 6.6 6.6 - 1
UnclassifiedUnclassified
Guide to Pharmacology 452 8 0 5 4.8 COc1ccccc1Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 14500736
10275802 107 None 0 Human Functional pIC50 None 6.6 6.6 - 1
UnclassifiedUnclassified
Guide to Pharmacology 452 8 0 5 4.8 COc1ccccc1Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 15717213
1401 107 None 0 Human Functional pIC50 None 6.6 6.6 - 1
UnclassifiedUnclassified
Guide to Pharmacology 452 8 0 5 4.8 COc1ccccc1Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 12852748
1401 107 None 0 Human Functional pIC50 None 6.6 6.6 - 1
UnclassifiedUnclassified
Guide to Pharmacology 452 8 0 5 4.8 COc1ccccc1Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 14500736
1401 107 None 0 Human Functional pIC50 None 6.6 6.6 - 1
UnclassifiedUnclassified
Guide to Pharmacology 452 8 0 5 4.8 COc1ccccc1Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 15717213


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Ligands (move mouse cursor over ligand name to see structure) Receptor Activity Chemical information
Sel. page Common
name		 GPCRdb
ID		 Reference
ligand		 Vendors

 Species

 Assay
Type		 Activity
Type		 Activity
Relation		 Activity
Value		 p-value
(-log)		 Fold
selectivity		 Tested
GPCRs		 Assay
Description		 Source

 Mol
weight		 Rot
Bonds		 H don

 H acc

 LogP

 Smiles

 DOI
9794208 90084 None 2 Human Binding pEC50 = 9.8 9.8 - 0
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 199 2 3 4 -1.3 N[C@@]1(C(=O)O)CC(=O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/jm4000165
CHEMBL2381640 90084 None 2 Human Binding pEC50 = 9.8 9.8 - 0
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 199 2 3 4 -1.3 N[C@@]1(C(=O)O)CC(=O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/jm4000165
139119037 90096 None 0 Human Binding pEC50 = 9.3 9.3 - 0
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 203 2 3 3 -0.5 N[C@@]1(C(=O)O)C[C@@H](F)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm4000165
15479143 90096 None 0 Human Binding pEC50 = 9.3 9.3 - 0
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 203 2 3 3 -0.5 N[C@@]1(C(=O)O)C[C@@H](F)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm4000165
CHEMBL2381652 90096 None 0 Human Binding pEC50 = 9.3 9.3 - 0
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 203 2 3 3 -0.5 N[C@@]1(C(=O)O)C[C@@H](F)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm4000165
70051926 90085 None 1 Human Binding pEC50 = 8.9 8.9 - 0
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 197 2 3 3 -0.3 C=C1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/jm4000165
CHEMBL2381641 90085 None 1 Human Binding pEC50 = 8.9 8.9 - 0
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 197 2 3 3 -0.3 C=C1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/jm4000165
44335501 109713 None 0 Human Binding pEC50 = 7 7.0 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 428 7 0 4 3.9 O=S(=O)(CC(F)(F)F)N(Cc1cccnc1)c1cccc(OCC(F)(F)F)c1 10.1016/j.bmcl.2004.04.017
CHEMBL322465 109713 None 0 Human Binding pEC50 = 7 7.0 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 428 7 0 4 3.9 O=S(=O)(CC(F)(F)F)N(Cc1cccnc1)c1cccc(OCC(F)(F)F)c1 10.1016/j.bmcl.2004.04.017
50993966 57347 None 0 Rat Binding pEC50 = 7 7.0 - 0
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 449 7 1 3 5.9 CC(C)CN1Cc2cc(OCc3cccc(-c4ccc(Cl)c(C(=O)O)c4)c3)ccc2C1=O 10.1021/jm1012165
CHEMBL1651212 57347 None 0 Rat Binding pEC50 = 7 7.0 - 0
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 449 7 1 3 5.9 CC(C)CN1Cc2cc(OCc3cccc(-c4ccc(Cl)c(C(=O)O)c4)c3)ccc2C1=O 10.1021/jm1012165
24815976 202215 None 0 Human Binding pEC50 = 7 7.0 - 3
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 373 3 0 3 5.0 Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL593745 202215 None 0 Human Binding pEC50 = 7 7.0 - 3
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 373 3 0 3 5.0 Cn1c(CN2CCC(c3ccc(C(F)(F)F)cc3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
24815883 203919 None 0 Human Binding pEC50 = 7 7.0 - 2
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 373 3 0 3 5.0 Cn1c(CN2CCC(c3cccc(C(F)(F)F)c3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL604993 203919 None 0 Human Binding pEC50 = 7 7.0 - 2
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 373 3 0 3 5.0 Cn1c(CN2CCC(c3cccc(C(F)(F)F)c3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
46225581 204444 None 0 Human Binding pEC50 = 7 7.0 - 3
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 339 3 0 3 4.6 Cn1c(CN2CCC(c3cccc(Cl)c3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL608103 204444 None 0 Human Binding pEC50 = 7 7.0 - 3
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 339 3 0 3 4.6 Cn1c(CN2CCC(c3cccc(Cl)c3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
11768848 115316 None 8 Human Binding pEC50 = 5 5.0 - 1
Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells
ChEMBL 159 3 3 3 -0.7 N[C@@]1(C(=O)O)C[C@H]1CC(=O)O 10.1039/C1MD00186H
CHEMBL3347671 115316 None 8 Human Binding pEC50 = 5 5.0 - 1
Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells
ChEMBL 159 3 3 3 -0.7 N[C@@]1(C(=O)O)C[C@H]1CC(=O)O 10.1039/C1MD00186H
10198359 73984 None 10 Human Binding pEC50 = 5 5.0 - 1
Concentration required to inhibit mGluR2 receptorConcentration required to inhibit mGluR2 receptor
ChEMBL 221 3 3 3 -0.8 N[C@H](C(=O)O)C12C3C4C1C1C2C3C41C(=O)O 10.1016/s0960-894x(98)00265-0
CHEMBL2021372 73984 None 10 Human Binding pEC50 = 5 5.0 - 1
Concentration required to inhibit mGluR2 receptorConcentration required to inhibit mGluR2 receptor
ChEMBL 221 3 3 3 -0.8 N[C@H](C(=O)O)C12C3C4C1C1C2C3C41C(=O)O 10.1016/s0960-894x(98)00265-0
90643871 111927 None 0 Rat Binding pEC50 = 7.0 7.0 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 418 11 2 5 5.0 Cc1c(OCCCCOc2ccc(C(=O)O)cc2F)ccc(C(=O)CC(C)C)c1O 10.1021/jm5000563
CHEMBL3287693 111927 None 0 Rat Binding pEC50 = 7.0 7.0 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 418 11 2 5 5.0 Cc1c(OCCCCOc2ccc(C(=O)O)cc2F)ccc(C(=O)CC(C)C)c1O 10.1021/jm5000563
164617451 185058 None 0 Rat Binding pEC50 = 7.0 7.0 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 444 11 2 6 5.3 COc1cc(OCCCCOc2ccc(C(=O)CC(C)(C)C)c(O)c2C)cc(C(=O)O)c1 10.1016/j.bmcl.2021.128342
CHEMBL4853794 185058 None 0 Rat Binding pEC50 = 7.0 7.0 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 444 11 2 6 5.3 COc1cc(OCCCCOc2ccc(C(=O)CC(C)(C)C)c(O)c2C)cc(C(=O)O)c1 10.1016/j.bmcl.2021.128342
90643884 111953 None 0 Rat Binding pEC50 = 7.0 7.0 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 416 12 2 6 4.6 CCCC(=O)c1ccc(OCCCCOc2cc(C(=O)O)ccc2OC)c(C)c1O 10.1021/jm5000563
CHEMBL3287719 111953 None 0 Rat Binding pEC50 = 7.0 7.0 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 416 12 2 6 4.6 CCCC(=O)c1ccc(OCCCCOc2cc(C(=O)O)ccc2OC)c(C)c1O 10.1021/jm5000563
89735528 138084 None 0 Human Binding pEC50 = 7.0 7.0 - 0
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 309 2 0 4 3.8 Cc1cccc(-c2ccc3c(n2)n(C)c(=O)n3CC(C)(C)C)c1 10.1016/j.bmcl.2016.01.021
CHEMBL3764544 138084 None 0 Human Binding pEC50 = 7.0 7.0 - 0
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 309 2 0 4 3.8 Cc1cccc(-c2ccc3c(n2)n(C)c(=O)n3CC(C)(C)C)c1 10.1016/j.bmcl.2016.01.021
90643857 111956 None 0 Rat Binding pEC50 = 7.0 7.0 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 400 11 2 5 4.9 CCCC(=O)c1ccc(OCCCCOc2ccc(C(=O)O)cc2C)c(C)c1O 10.1021/jm5000563
CHEMBL3287722 111956 None 0 Rat Binding pEC50 = 7.0 7.0 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 400 11 2 5 4.9 CCCC(=O)c1ccc(OCCCCOc2ccc(C(=O)O)cc2C)c(C)c1O 10.1021/jm5000563
10050046 66094 None 0 Human Binding pEC50 = 6.0 6.0 - 0
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 463 12 2 7 3.5 CCCc1c(OCCCCOc2ccc(C(=O)NS(C)(=O)=O)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2004.08.020
CHEMBL183756 66094 None 0 Human Binding pEC50 = 6.0 6.0 - 0
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 463 12 2 7 3.5 CCCc1c(OCCCCOc2ccc(C(=O)NS(C)(=O)=O)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2004.08.020
11656255 123378 None 0 Human Binding pEC50 = 6.0 6.0 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 498 8 1 5 6.9 CCCCC1(C2CCCC2)Cc2cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
CHEMBL361570 123378 None 0 Human Binding pEC50 = 6.0 6.0 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 498 8 1 5 6.9 CCCCC1(C2CCCC2)Cc2cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
90643896 111938 None 0 Rat Binding pEC50 = 6.0 6.0 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 388 10 2 6 3.8 COc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(C)=O)c(O)c1C 10.1021/jm5000563
CHEMBL3287704 111938 None 0 Rat Binding pEC50 = 6.0 6.0 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 388 10 2 6 3.8 COc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(C)=O)c(O)c1C 10.1021/jm5000563
68109941 156213 None 0 Human Binding pEC50 = 8.0 8.0 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cells assessed as cellular impedance measured for 20 mins with 15 sec time interval followed by 40 mins with 5 mins time interval and subsequently measured with 15 mins time interval in presence of endogenous glutamate levels by RTCAPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cells assessed as cellular impedance measured for 20 mins with 15 sec time interval followed by 40 mins with 5 mins time interval and subsequently measured with 15 mins time interval in presence of endogenous glutamate levels by RTCA
ChEMBL 504 6 2 5 6.5 O[C@]1(C2CC2)CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4063313 156213 None 0 Human Binding pEC50 = 8.0 8.0 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cells assessed as cellular impedance measured for 20 mins with 15 sec time interval followed by 40 mins with 5 mins time interval and subsequently measured with 15 mins time interval in presence of endogenous glutamate levels by RTCAPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cells assessed as cellular impedance measured for 20 mins with 15 sec time interval followed by 40 mins with 5 mins time interval and subsequently measured with 15 mins time interval in presence of endogenous glutamate levels by RTCA
ChEMBL 504 6 2 5 6.5 O[C@]1(C2CC2)CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
53390518 82726 None 0 Rat Binding pEC50 = 7.0 7.0 - 0
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 461 6 1 3 6.2 O=C(O)c1ccc(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)c(Cl)c1 10.1021/jm3005306
CHEMBL2179635 82726 None 0 Rat Binding pEC50 = 7.0 7.0 - 0
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 461 6 1 3 6.2 O=C(O)c1ccc(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)c(Cl)c1 10.1021/jm3005306
53390519 82727 None 0 Rat Binding pEC50 = 7.0 7.0 - 0
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 441 6 1 3 5.8 Cc1ccc(C(=O)O)cc1-c1cccc(COc2ccc3c(c2)CN(C2CCCC2)C3=O)c1 10.1021/jm3005306
CHEMBL2179636 82727 None 0 Rat Binding pEC50 = 7.0 7.0 - 0
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 441 6 1 3 5.8 Cc1ccc(C(=O)O)cc1-c1cccc(COc2ccc3c(c2)CN(C2CCCC2)C3=O)c1 10.1021/jm3005306
23521689 4845 None 0 Human Binding pEC50 = 6.0 6.0 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 380 7 0 4 3.7 CCS(=O)(=O)N(Cc1cccnc1)c1cccc(C(=O)c2ccccc2)c1 10.1016/j.bmcl.2004.04.017
CHEMBL104248 4845 None 0 Human Binding pEC50 = 6.0 6.0 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 380 7 0 4 3.7 CCS(=O)(=O)N(Cc1cccnc1)c1cccc(C(=O)c2ccccc2)c1 10.1016/j.bmcl.2004.04.017
89735510 137984 None 0 Human Binding pEC50 = 7.0 7.0 - 0
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 325 3 1 5 2.9 Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3cccc(CO)c3)nc21 10.1016/j.bmcl.2016.01.021
CHEMBL3763263 137984 None 0 Human Binding pEC50 = 7.0 7.0 - 0
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 325 3 1 5 2.9 Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3cccc(CO)c3)nc21 10.1016/j.bmcl.2016.01.021
164610619 184860 None 0 Rat Binding pEC50 = 7.0 7.0 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 432 9 2 5 5.3 Cc1c(OC[C@@H](C)COc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
CHEMBL4850952 184860 None 0 Rat Binding pEC50 = 7.0 7.0 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 432 9 2 5 5.3 Cc1c(OC[C@@H](C)COc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
164627219 186487 None 0 Rat Binding pEC50 = 7.0 7.0 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 418 8 2 5 5.0 Cc1c(OC[C@@H](C)Oc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
CHEMBL4875653 186487 None 0 Rat Binding pEC50 = 7.0 7.0 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 418 8 2 5 5.0 Cc1c(OC[C@@H](C)Oc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
44578904 181675 None 0 Rat Binding pEC50 = 7.0 7.0 - 0
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 409 6 0 4 5.0 Cn1c(CN2C[C@@H]3C(COc4cccc(-c5ccccc5)c4)[C@@H]3C2)nc2ccccc21 10.1016/j.bmcl.2008.09.026
CHEMBL476791 181675 None 0 Rat Binding pEC50 = 7.0 7.0 - 0
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 409 6 0 4 5.0 Cn1c(CN2C[C@@H]3C(COc4cccc(-c5ccccc5)c4)[C@@H]3C2)nc2ccccc21 10.1016/j.bmcl.2008.09.026
90643904 111947 None 0 Rat Binding pEC50 = 7.0 7.0 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 416 11 2 6 4.5 COc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)C(C)C)c(O)c1C 10.1021/jm5000563
CHEMBL3287713 111947 None 0 Rat Binding pEC50 = 7.0 7.0 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 416 11 2 6 4.5 COc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)C(C)C)c(O)c1C 10.1021/jm5000563
90643900 111942 None 0 Rat Binding pEC50 = 6.9 6.9 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 402 11 2 6 4.2 CCC(=O)c1ccc(OCCCCOc2ccc(C(=O)O)cc2OC)c(C)c1O 10.1021/jm5000563
CHEMBL3287708 111942 None 0 Rat Binding pEC50 = 6.9 6.9 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 402 11 2 6 4.2 CCC(=O)c1ccc(OCCCCOc2ccc(C(=O)O)cc2OC)c(C)c1O 10.1021/jm5000563
71117141 147537 None 0 Human Binding pEC50 = 6.9 6.9 - 0
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 435 4 0 8 2.1 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)Cn3cncn3)nc21 nan
CHEMBL3930164 147537 None 0 Human Binding pEC50 = 6.9 6.9 - 0
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 435 4 0 8 2.1 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)Cn3cncn3)nc21 nan
69929497 140375 None 0 Human Binding pEC50 = 6.9 6.9 - 0
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 434 3 0 7 2.7 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CC4CCC3CN4C(=O)c3cccnc3)nc21 10.1021/acsmedchemlett.5b00459
CHEMBL3805900 140375 None 0 Human Binding pEC50 = 6.9 6.9 - 0
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 434 3 0 7 2.7 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CC4CCC3CN4C(=O)c3cccnc3)nc21 10.1021/acsmedchemlett.5b00459
90643881 111948 None 0 Rat Binding pEC50 = 6.9 6.9 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 416 11 2 6 4.5 COc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)C(C)C)c(O)c1C 10.1021/jm5000563
CHEMBL3287714 111948 None 0 Rat Binding pEC50 = 6.9 6.9 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 416 11 2 6 4.5 COc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)C(C)C)c(O)c1C 10.1021/jm5000563
11648184 63063 None 0 Human Binding pEC50 = 5.9 5.9 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 454 5 1 4 5.9 CC1(C2CCCC2)Cc2cc(CCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
CHEMBL178823 63063 None 0 Human Binding pEC50 = 5.9 5.9 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 454 5 1 4 5.9 CC1(C2CCCC2)Cc2cc(CCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
71681826 90095 None 0 Human Binding pEC50 = 5.9 5.9 -4 2
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 293 4 3 4 1.3 N[C@@]1(C(=O)O)C[C@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm4000165
CHEMBL2381651 90095 None 0 Human Binding pEC50 = 5.9 5.9 -4 2
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 293 4 3 4 1.3 N[C@@]1(C(=O)O)C[C@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm4000165
162649186 183750 None 0 Rat Binding pEC50 = 5.9 5.9 - 0
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1205 32 6 12 12.5 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
CHEMBL4748285 183750 None 0 Rat Binding pEC50 = 5.9 5.9 - 0
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1205 32 6 12 12.5 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
CHEMBL4802609 183750 None 0 Rat Binding pEC50 = 5.9 5.9 - 0
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1205 32 6 12 12.5 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
1310 2315 None 61 Rat Binding pEC50 = 4.9 4.9 -13 18
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm00009a001
1369 2315 None 61 Rat Binding pEC50 = 4.9 4.9 -13 18
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm00009a001
33032 2315 None 61 Rat Binding pEC50 = 4.9 4.9 -13 18
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm00009a001
44272391 2315 None 61 Rat Binding pEC50 = 4.9 4.9 -13 18
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm00009a001
88747398 2315 None 61 Rat Binding pEC50 = 4.9 4.9 -13 18
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm00009a001
CHEMBL575060 2315 None 61 Rat Binding pEC50 = 4.9 4.9 -13 18
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm00009a001
DB00142 2315 None 61 Rat Binding pEC50 = 4.9 4.9 -13 18
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm00009a001
71681825 90089 None 0 Human Binding pEC50 = 7.9 7.9 - 0
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 226 3 3 4 -0.2 [N-]=[N+]=N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/jm4000165
CHEMBL2381645 90089 None 0 Human Binding pEC50 = 7.9 7.9 - 0
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 226 3 3 4 -0.2 [N-]=[N+]=N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/jm4000165
104766 33 None 30 Human Binding pEC50 = 4.9 4.9 -11 11
Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1021/jm00009a001
1365 33 None 30 Human Binding pEC50 = 4.9 4.9 -11 11
Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1021/jm00009a001
CHEMBL34453 33 None 30 Human Binding pEC50 = 4.9 4.9 -11 11
Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1021/jm00009a001
11583075 63510 None 0 Human Binding pEC50 = 6.9 6.9 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 442 5 1 5 5.3 O=C1c2c(cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c2Cl)CC1C1CCCC1 10.1016/j.bmcl.2005.01.077
CHEMBL179939 63510 None 0 Human Binding pEC50 = 6.9 6.9 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 442 5 1 5 5.3 O=C1c2c(cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c2Cl)CC1C1CCCC1 10.1016/j.bmcl.2005.01.077
162647509 183743 None 0 Rat Binding pEC50 = 6.9 6.9 - 0
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1134 27 6 12 10.6 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
CHEMBL4744407 183743 None 0 Rat Binding pEC50 = 6.9 6.9 - 0
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1134 27 6 12 10.6 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
CHEMBL4802513 183743 None 0 Rat Binding pEC50 = 6.9 6.9 - 0
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1134 27 6 12 10.6 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
56929215 111910 None 0 Rat Binding pEC50 = 6.9 6.9 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 400 11 2 5 4.9 Cc1c(OCCCCOc2ccc(C(=O)O)cc2)ccc(C(=O)CC(C)C)c1O 10.1021/jm5000563
CHEMBL3287671 111910 None 0 Rat Binding pEC50 = 6.9 6.9 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 400 11 2 5 4.9 Cc1c(OCCCCOc2ccc(C(=O)O)cc2)ccc(C(=O)CC(C)C)c1O 10.1021/jm5000563
90643902 111945 None 0 Rat Binding pEC50 = 6.9 6.9 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 390 10 2 5 4.4 CCC(=O)c1ccc(OCCCCOc2ccc(F)c(C(=O)O)c2)c(C)c1O 10.1021/jm5000563
CHEMBL3287711 111945 None 0 Rat Binding pEC50 = 6.9 6.9 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 390 10 2 5 4.4 CCC(=O)c1ccc(OCCCCOc2ccc(F)c(C(=O)O)c2)c(C)c1O 10.1021/jm5000563
67056056 140288 None 0 Human Binding pEC50 = 6.9 6.9 - 0
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 429 2 0 7 3.4 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CC4CCC3CN4C(=O)OC(C)(C)C)nc21 10.1021/acsmedchemlett.5b00459
CHEMBL3804910 140288 None 0 Human Binding pEC50 = 6.9 6.9 - 0
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 429 2 0 7 3.4 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CC4CCC3CN4C(=O)OC(C)(C)C)nc21 10.1021/acsmedchemlett.5b00459
46190878 1872 None 8 Human Binding pEC50 = 6.9 6.9 - 1
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 342 3 0 6 2.3 Clc1cnc(nc1)N1CCN(CC1)Cc1nc2c(n1C)cccc2 10.1016/j.bmcl.2009.11.032
6253 1872 None 8 Human Binding pEC50 = 6.9 6.9 - 1
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 342 3 0 6 2.3 Clc1cnc(nc1)N1CCN(CC1)Cc1nc2c(n1C)cccc2 10.1016/j.bmcl.2009.11.032
CHEMBL595759 1872 None 8 Human Binding pEC50 = 6.9 6.9 - 1
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 342 3 0 6 2.3 Clc1cnc(nc1)N1CCN(CC1)Cc1nc2c(n1C)cccc2 10.1016/j.bmcl.2009.11.032
46225407 202193 None 0 Human Binding pEC50 = 6.9 6.9 - 0
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 427 3 0 5 4.1 Cn1c(CN2CCN(c3nc(Cl)ccc3C(F)(F)F)CC2)nc2ccc(F)cc21 10.1016/j.bmcl.2009.11.032
CHEMBL593532 202193 None 0 Human Binding pEC50 = 6.9 6.9 - 0
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 427 3 0 5 4.1 Cn1c(CN2CCN(c3nc(Cl)ccc3C(F)(F)F)CC2)nc2ccc(F)cc21 10.1016/j.bmcl.2009.11.032
46225359 202285 None 0 Human Binding pEC50 = 6.9 6.9 - 0
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 418 5 0 6 3.9 Clc1cnc(N2CCN(Cc3nc4ccccc4n3Cc3ccccc3)CC2)nc1 10.1016/j.bmcl.2009.11.032
CHEMBL594236 202285 None 0 Human Binding pEC50 = 6.9 6.9 - 0
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 418 5 0 6 3.9 Clc1cnc(N2CCN(Cc3nc4ccccc4n3Cc3ccccc3)CC2)nc1 10.1016/j.bmcl.2009.11.032
46225334 202502 None 0 Human Binding pEC50 = 6.9 6.9 - 1
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 358 3 0 4 3.7 Cn1c(CN2CCN(c3ccc(Cl)cc3F)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL595607 202502 None 0 Human Binding pEC50 = 6.9 6.9 - 1
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 358 3 0 4 3.7 Cn1c(CN2CCN(c3ccc(Cl)cc3F)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
46225358 204319 None 0 Human Binding pEC50 = 6.9 6.9 - 0
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 485 5 0 5 5.5 FC(F)(F)c1ccc(Cl)nc1N1CCN(Cc2nc3ccccc3n2Cc2ccccc2)CC1 10.1016/j.bmcl.2009.11.032
CHEMBL607195 204319 None 0 Human Binding pEC50 = 6.9 6.9 - 0
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 485 5 0 5 5.5 FC(F)(F)c1ccc(Cl)nc1N1CCN(Cc2nc3ccccc3n2Cc2ccccc2)CC1 10.1016/j.bmcl.2009.11.032
24815439 204392 None 1 Human Binding pEC50 = 6.9 6.9 - 3
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 323 3 0 3 4.1 Cn1c(CN2CCC(c3ccccc3F)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL607689 204392 None 1 Human Binding pEC50 = 6.9 6.9 - 3
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 323 3 0 3 4.1 Cn1c(CN2CCC(c3ccccc3F)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
46225384 202353 None 3 Human Binding pEC50 = 4.9 4.9 - 0
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 328 3 1 5 2.3 Clc1cnc(N2CCN(Cc3nc4ccccc4[nH]3)CC2)nc1 10.1016/j.bmcl.2009.11.032
CHEMBL594673 202353 None 3 Human Binding pEC50 = 4.9 4.9 - 0
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 328 3 1 5 2.3 Clc1cnc(N2CCN(Cc3nc4ccccc4[nH]3)CC2)nc1 10.1016/j.bmcl.2009.11.032
46225383 202553 None 0 Human Binding pEC50 = 4.9 4.9 - 0
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 395 3 1 4 4.0 FC(F)(F)c1ccc(Cl)nc1N1CCN(Cc2nc3ccccc3[nH]2)CC1 10.1016/j.bmcl.2009.11.032
CHEMBL595991 202553 None 0 Human Binding pEC50 = 4.9 4.9 - 0
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 395 3 1 4 4.0 FC(F)(F)c1ccc(Cl)nc1N1CCN(Cc2nc3ccccc3[nH]2)CC1 10.1016/j.bmcl.2009.11.032
69929646 140406 None 0 Human Binding pEC50 = 5.9 5.9 - 0
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 329 2 1 6 1.7 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CC4CCC3CN4)nc21 10.1021/acsmedchemlett.5b00459
CHEMBL3806226 140406 None 0 Human Binding pEC50 = 5.9 5.9 - 0
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 329 2 1 6 1.7 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CC4CCC3CN4)nc21 10.1021/acsmedchemlett.5b00459
127038185 138030 None 0 Human Binding pEC50 = 4.9 4.9 - 0
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 248 2 0 4 2.4 COc1ccc2c(c1)n(C)c(=O)n2CC(C)(C)C 10.1016/j.bmcl.2016.01.021
CHEMBL3763995 138030 None 0 Human Binding pEC50 = 4.9 4.9 - 0
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 248 2 0 4 2.4 COc1ccc2c(c1)n(C)c(=O)n2CC(C)(C)C 10.1016/j.bmcl.2016.01.021
90643868 111924 None 0 Rat Binding pEC50 = 5.9 5.9 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 440 11 2 5 5.7 Cc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)CC2CCCC2)c(O)c1C 10.1021/jm5000563
CHEMBL3287690 111924 None 0 Rat Binding pEC50 = 5.9 5.9 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 440 11 2 5 5.7 Cc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)CC2CCCC2)c(O)c1C 10.1021/jm5000563
164608826 184573 None 0 Rat Binding pEC50 = 7.9 7.9 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 444 11 2 6 5.3 COc1ccc(OCCCCOc2ccc(C(=O)CC(C)(C)C)c(O)c2C)cc1C(=O)O 10.1016/j.bmcl.2021.128342
CHEMBL4846872 184573 None 0 Rat Binding pEC50 = 7.9 7.9 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 444 11 2 6 5.3 COc1ccc(OCCCCOc2ccc(C(=O)CC(C)(C)C)c(O)c2C)cc1C(=O)O 10.1016/j.bmcl.2021.128342
68108429 149767 None 0 Human Binding pEC50 = 7.9 7.9 - 0
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 448 5 0 4 5.7 FC(F)(F)c1c(CN2CCC(c3ccccc3Cl)CC2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.6b00913
CHEMBL3947590 149767 None 0 Human Binding pEC50 = 7.9 7.9 - 0
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 448 5 0 4 5.7 FC(F)(F)c1c(CN2CCC(c3ccccc3Cl)CC2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.6b00913
53390677 82720 None 0 Rat Binding pEC50 = 6.9 6.9 - 0
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 451 6 1 5 6.0 O=C(O)c1cc(-c2cccc(COc3ccc4c(=O)n(C5CC5)sc4c3)c2)ccc1Cl 10.1021/jm3005306
CHEMBL2179629 82720 None 0 Rat Binding pEC50 = 6.9 6.9 - 0
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 451 6 1 5 6.0 O=C(O)c1cc(-c2cccc(COc3ccc4c(=O)n(C5CC5)sc4c3)c2)ccc1Cl 10.1021/jm3005306
53390520 82728 None 0 Rat Binding pEC50 = 6.9 6.9 - 0
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 445 6 1 3 5.7 O=C(O)c1cc(F)cc(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)c1 10.1021/jm3005306
CHEMBL2179637 82728 None 0 Rat Binding pEC50 = 6.9 6.9 - 0
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 445 6 1 3 5.7 O=C(O)c1cc(F)cc(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)c1 10.1021/jm3005306
6604704 101455 None 23 Human Binding pEC50 = 4.9 4.9 - 0
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
ChEMBL 173 2 3 3 -0.3 N[C@@]1(C(=O)O)CC[C@H](C(=O)O)C1 10.1021/jm970719q
CHEMBL29726 101455 None 23 Human Binding pEC50 = 4.9 4.9 - 0
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
ChEMBL 173 2 3 3 -0.3 N[C@@]1(C(=O)O)CC[C@H](C(=O)O)C1 10.1021/jm970719q
49822195 146270 None 0 Human Binding pEC50 = 6.9 6.9 - 0
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 432 5 0 4 5.2 FC(F)(F)c1c(CN2CCC(F)(c3ccccc3)CC2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.6b00913
CHEMBL3919978 146270 None 0 Human Binding pEC50 = 6.9 6.9 - 0
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 432 5 0 4 5.2 FC(F)(F)c1c(CN2CCC(F)(c3ccccc3)CC2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.6b00913
162657776 183789 None 0 Rat Binding pEC50 = 6.9 6.9 - 0
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1176 30 6 12 11.7 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
CHEMBL4759458 183789 None 0 Rat Binding pEC50 = 6.9 6.9 - 0
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1176 30 6 12 11.7 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
CHEMBL4803052 183789 None 0 Rat Binding pEC50 = 6.9 6.9 - 0
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1176 30 6 12 11.7 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
25195461 2144 None 42 Human Binding pEC50 = 5.9 5.9 - 1
Positive allosteric modulation at human mGlu2 receptor L639A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor L639A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
8946 2144 None 42 Human Binding pEC50 = 5.9 5.9 - 1
Positive allosteric modulation at human mGlu2 receptor L639A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor L639A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
CHEMBL3337527 2144 None 42 Human Binding pEC50 = 5.9 5.9 - 1
Positive allosteric modulation at human mGlu2 receptor L639A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor L639A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
DB12059 2144 None 42 Human Binding pEC50 = 5.9 5.9 - 1
Positive allosteric modulation at human mGlu2 receptor L639A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor L639A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
86765132 111959 None 0 Rat Binding pEC50 = 6.9 6.9 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 428 10 2 5 5.6 Cc1c(OCCCCOc2ccc(C(=O)CC(C)(C)C)c(O)c2C)cccc1C(=O)O 10.1021/jm5000563
CHEMBL3287725 111959 None 0 Rat Binding pEC50 = 6.9 6.9 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 428 10 2 5 5.6 Cc1c(OCCCCOc2ccc(C(=O)CC(C)(C)C)c(O)c2C)cccc1C(=O)O 10.1021/jm5000563
164613604 185290 None 0 Rat Binding pEC50 = 6.9 6.9 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 430 9 2 6 4.9 COc1ccc(C(=O)O)cc1O[C@@H](C)COc1ccc(C(=O)CC(C)(C)C)c(O)c1C 10.1016/j.bmcl.2021.128342
CHEMBL4857426 185290 None 0 Rat Binding pEC50 = 6.9 6.9 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 430 9 2 6 4.9 COc1ccc(C(=O)O)cc1O[C@@H](C)COc1ccc(C(=O)CC(C)(C)C)c(O)c1C 10.1016/j.bmcl.2021.128342
11362035 42 None 1 Human Binding pEC50 = 7.9 7.9 - 1
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 416 9 0 4 4.5 CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C 10.1016/j.bmcl.2004.04.017
6328 42 None 1 Human Binding pEC50 = 7.9 7.9 - 1
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 416 9 0 4 4.5 CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C 10.1016/j.bmcl.2004.04.017
6329 42 None 1 Human Binding pEC50 = 7.9 7.9 - 1
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 416 9 0 4 4.5 CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C 10.1016/j.bmcl.2004.04.017
CHEMBL105296 42 None 1 Human Binding pEC50 = 7.9 7.9 - 1
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 416 9 0 4 4.5 CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C 10.1016/j.bmcl.2004.04.017
23521659 4848 None 0 Human Binding pEC50 = 6.9 6.9 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 414 6 0 4 3.9 O=S(=O)(CC(F)(F)F)N(Cc1cccnc1)c1cccc(OC(F)(F)F)c1 10.1016/j.bmcl.2004.04.017
CHEMBL104260 4848 None 0 Human Binding pEC50 = 6.9 6.9 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 414 6 0 4 3.9 O=S(=O)(CC(F)(F)F)N(Cc1cccnc1)c1cccc(OC(F)(F)F)c1 10.1016/j.bmcl.2004.04.017
23521713 109825 None 0 Human Binding pEC50 = 5.9 5.9 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 380 7 0 3 4.6 CCS(=O)(=O)N(Cc1cccnc1)c1ccc(C(C)c2ccccc2)cc1 10.1016/j.bmcl.2004.04.017
CHEMBL323138 109825 None 0 Human Binding pEC50 = 5.9 5.9 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 380 7 0 3 4.6 CCS(=O)(=O)N(Cc1cccnc1)c1ccc(C(C)c2ccccc2)cc1 10.1016/j.bmcl.2004.04.017
49822116 147080 None 14 Human Binding pEC50 = 5.9 5.9 - 1
Positive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 451 5 0 5 4.3 Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
CHEMBL3926416 147080 None 14 Human Binding pEC50 = 5.9 5.9 - 1
Positive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 451 5 0 5 4.3 Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
44395191 66321 None 0 Human Binding pEC50 = 5.9 5.9 - 0
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 396 10 2 7 3.6 CCCc1c(OCCCOc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2004.08.020
CHEMBL184838 66321 None 0 Human Binding pEC50 = 5.9 5.9 - 0
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 396 10 2 7 3.6 CCCc1c(OCCCOc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2004.08.020
164621278 185638 None 0 Rat Binding pEC50 = 6.9 6.9 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 418 8 2 5 5.0 Cc1c(OC[C@H](C)Oc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
CHEMBL4862801 185638 None 0 Rat Binding pEC50 = 6.9 6.9 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 418 8 2 5 5.0 Cc1c(OC[C@H](C)Oc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
25195461 2144 None 42 Human Binding pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
8946 2144 None 42 Human Binding pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
CHEMBL3337527 2144 None 42 Human Binding pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
DB12059 2144 None 42 Human Binding pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
49765871 2145 None 41 Human Binding pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of mGlu2 receptor (unknown origin)Positive allosteric modulation of mGlu2 receptor (unknown origin)
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1016/j.bmc.2022.116614
6317 2145 None 41 Human Binding pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of mGlu2 receptor (unknown origin)Positive allosteric modulation of mGlu2 receptor (unknown origin)
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1016/j.bmc.2022.116614
CHEMBL2179319 2145 None 41 Human Binding pEC50 = 6.8 6.8 - 1
Positive allosteric modulation of mGlu2 receptor (unknown origin)Positive allosteric modulation of mGlu2 receptor (unknown origin)
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1016/j.bmc.2022.116614
90643858 111929 None 0 Rat Binding pEC50 = 6.8 6.8 - 0
Agonist activity at rat mGluR2 receptor expressed in HEK293 cells assessed as thallium flux incubated for 2.5 mins prior to thallium buffer addition measured after 2.5 mins by GIRK assayAgonist activity at rat mGluR2 receptor expressed in HEK293 cells assessed as thallium flux incubated for 2.5 mins prior to thallium buffer addition measured after 2.5 mins by GIRK assay
ChEMBL 430 12 2 6 4.9 COc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)CC(C)C)c(O)c1C 10.1021/jm5000563
CHEMBL3287695 111929 None 0 Rat Binding pEC50 = 6.8 6.8 - 0
Agonist activity at rat mGluR2 receptor expressed in HEK293 cells assessed as thallium flux incubated for 2.5 mins prior to thallium buffer addition measured after 2.5 mins by GIRK assayAgonist activity at rat mGluR2 receptor expressed in HEK293 cells assessed as thallium flux incubated for 2.5 mins prior to thallium buffer addition measured after 2.5 mins by GIRK assay
ChEMBL 430 12 2 6 4.9 COc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)CC(C)C)c(O)c1C 10.1021/jm5000563
90643905 111949 None 0 Rat Binding pEC50 = 6.8 6.8 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 400 10 2 5 4.8 Cc1c(OCCCCOc2ccc(C(=O)C(C)C)c(O)c2C)cccc1C(=O)O 10.1021/jm5000563
CHEMBL3287715 111949 None 0 Rat Binding pEC50 = 6.8 6.8 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 400 10 2 5 4.8 Cc1c(OCCCCOc2ccc(C(=O)C(C)C)c(O)c2C)cccc1C(=O)O 10.1021/jm5000563
67056141 140296 None 0 Human Binding pEC50 = 6.8 6.8 - 0
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 424 4 0 8 2.9 Cc1cc(CN2CC3CCC2CN3c2ccc3c(n2)n(C)c(=O)n3CC(C)(C)C)no1 10.1021/acsmedchemlett.5b00459
CHEMBL3805017 140296 None 0 Human Binding pEC50 = 6.8 6.8 - 0
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 424 4 0 8 2.9 Cc1cc(CN2CC3CCC2CN3c2ccc3c(n2)n(C)c(=O)n3CC(C)(C)C)no1 10.1021/acsmedchemlett.5b00459
68107810 146242 None 0 Human Binding pEC50 = 7.8 7.8 - 0
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 432 5 0 4 5.2 Fc1ccccc1C1CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1 10.1021/acs.jmedchem.6b00913
CHEMBL3919807 146242 None 0 Human Binding pEC50 = 7.8 7.8 - 0
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 432 5 0 4 5.2 Fc1ccccc1C1CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1 10.1021/acs.jmedchem.6b00913
68108457 148644 None 0 Human Binding pEC50 = 7.8 7.8 - 0
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 450 5 0 4 5.4 Fc1ccc(C2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
CHEMBL3938796 148644 None 0 Human Binding pEC50 = 7.8 7.8 - 0
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 450 5 0 4 5.4 Fc1ccc(C2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
127039577 138052 None 0 Human Binding pEC50 = 7.8 7.8 - 0
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 462 6 1 5 5.5 Cn1c(=O)n(CC(C)(C)C)c2ccc(OCc3cccc(-c4cc(F)cc(C(=O)O)c4)c3)cc21 10.1016/j.bmcl.2016.01.021
CHEMBL3764173 138052 None 0 Human Binding pEC50 = 7.8 7.8 - 0
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 462 6 1 5 5.5 Cn1c(=O)n(CC(C)(C)C)c2ccc(OCc3cccc(-c4cc(F)cc(C(=O)O)c4)c3)cc21 10.1016/j.bmcl.2016.01.021
9885608 4853 None 1 Human Binding pEC50 = 5.8 5.8 - 0
Effective concentration against Metabotropic glutamate receptor 2Effective concentration against Metabotropic glutamate receptor 2
ChEMBL 368 7 0 4 4.2 CCS(=O)(=O)N(Cc1cccnc1)c1ccc(Oc2ccccc2)cc1 10.1021/jm034015u
CHEMBL104296 4853 None 1 Human Binding pEC50 = 5.8 5.8 - 0
Effective concentration against Metabotropic glutamate receptor 2Effective concentration against Metabotropic glutamate receptor 2
ChEMBL 368 7 0 4 4.2 CCS(=O)(=O)N(Cc1cccnc1)c1ccc(Oc2ccccc2)cc1 10.1021/jm034015u
9885608 4853 None 1 Human Binding pEC50 = 5.8 5.8 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 368 7 0 4 4.2 CCS(=O)(=O)N(Cc1cccnc1)c1ccc(Oc2ccccc2)cc1 10.1016/j.bmcl.2004.04.017
CHEMBL104296 4853 None 1 Human Binding pEC50 = 5.8 5.8 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 368 7 0 4 4.2 CCS(=O)(=O)N(Cc1cccnc1)c1ccc(Oc2ccccc2)cc1 10.1016/j.bmcl.2004.04.017
90643863 111919 None 0 Rat Binding pEC50 = 6.8 6.8 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 434 11 2 5 5.5 Cc1c(OCCCCOc2ccc(C(=O)O)c(Cl)c2)ccc(C(=O)CC(C)C)c1O 10.1021/jm5000563
CHEMBL3287683 111919 None 0 Rat Binding pEC50 = 6.8 6.8 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 434 11 2 5 5.5 Cc1c(OCCCCOc2ccc(C(=O)O)c(Cl)c2)ccc(C(=O)CC(C)C)c1O 10.1021/jm5000563
90643865 111921 None 0 Rat Binding pEC50 = 6.8 6.8 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 418 11 2 5 5.0 Cc1c(OCCCCOc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)C)c1O 10.1021/jm5000563
CHEMBL3287687 111921 None 0 Rat Binding pEC50 = 6.8 6.8 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 418 11 2 5 5.0 Cc1c(OCCCCOc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)C)c1O 10.1021/jm5000563
90643878 111935 None 0 Rat Binding pEC50 = 6.8 6.8 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 430 12 2 6 4.9 COc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)CC(C)C)c(O)c1C 10.1021/jm5000563
CHEMBL3287701 111935 None 0 Rat Binding pEC50 = 6.8 6.8 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 430 12 2 6 4.9 COc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)CC(C)C)c(O)c1C 10.1021/jm5000563
90668092 109593 None 0 Human Binding pEC50 = 6.8 6.8 - 0
Positive allosteric modulation of mGluR2 (unknown origin) by FLIPR assayPositive allosteric modulation of mGluR2 (unknown origin) by FLIPR assay
ChEMBL 306 6 1 3 4.1 CCCn1ccc2c(NCCc3ccccc3)cccc2c1=O 10.1039/C0MD00200C
CHEMBL3221831 109593 None 0 Human Binding pEC50 = 6.8 6.8 - 0
Positive allosteric modulation of mGluR2 (unknown origin) by FLIPR assayPositive allosteric modulation of mGluR2 (unknown origin) by FLIPR assay
ChEMBL 306 6 1 3 4.1 CCCn1ccc2c(NCCc3ccccc3)cccc2c1=O 10.1039/C0MD00200C
46225371 202279 None 0 Human Binding pEC50 = 6.8 6.8 - 0
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 453 6 0 6 4.1 COCCn1c(CN2CCN(c3nc(Cl)ccc3C(F)(F)F)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL594204 202279 None 0 Human Binding pEC50 = 6.8 6.8 - 0
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 453 6 0 6 4.1 COCCn1c(CN2CCN(c3nc(Cl)ccc3C(F)(F)F)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
46225372 203822 None 0 Human Binding pEC50 = 6.8 6.8 - 0
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 356 4 0 6 2.8 CCn1c(CN2CCN(c3ncc(Cl)cn3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL604472 203822 None 0 Human Binding pEC50 = 6.8 6.8 - 0
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 356 4 0 6 2.8 CCn1c(CN2CCN(c3ncc(Cl)cn3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
46225582 204072 None 0 Human Binding pEC50 = 6.8 6.8 - 2
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 362 3 0 5 4.6 Cn1c(CN2CCC(c3nc4ccccc4s3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL605831 204072 None 0 Human Binding pEC50 = 6.8 6.8 - 2
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 362 3 0 5 4.6 Cn1c(CN2CCC(c3nc4ccccc4s3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
3461070 117410 None 0 Human Binding pEC50 = 4.8 4.8 - 0
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 307 3 0 5 2.3 Cn1c(CN2CCN(c3ccccn3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL339714 117410 None 0 Human Binding pEC50 = 4.8 4.8 - 0
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 307 3 0 5 2.3 Cn1c(CN2CCN(c3ccccn3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
44335554 109279 None 0 Human Binding pEC50 = 7.8 7.8 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 416 9 0 4 4.5 CCC(CC)Oc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1 10.1016/j.bmcl.2004.04.017
CHEMBL321746 109279 None 0 Human Binding pEC50 = 7.8 7.8 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 416 9 0 4 4.5 CCC(CC)Oc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1 10.1016/j.bmcl.2004.04.017
71479388 140310 None 0 Human Binding pEC50 = 7.8 7.8 - 0
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 421 3 0 7 3.1 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=C[C@@H]4CC[C@H]3CN4C(=O)c3ccon3)nc21 10.1021/acsmedchemlett.5b00459
CHEMBL3805139 140310 None 0 Human Binding pEC50 = 7.8 7.8 - 0
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 421 3 0 7 3.1 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=C[C@@H]4CC[C@H]3CN4C(=O)c3ccon3)nc21 10.1021/acsmedchemlett.5b00459
23521708 4827 None 0 Human Binding pEC50 = 6.8 6.8 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 382 8 0 4 4.0 CCS(=O)(=O)N(Cc1cccnc1)c1cccc(COc2ccccc2)c1 10.1016/j.bmcl.2004.04.017
CHEMBL104191 4827 None 0 Human Binding pEC50 = 6.8 6.8 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 382 8 0 4 4.0 CCS(=O)(=O)N(Cc1cccnc1)c1cccc(COc2ccccc2)c1 10.1016/j.bmcl.2004.04.017
23521727 4904 None 0 Human Binding pEC50 = 5.8 5.8 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 366 7 0 3 4.0 CCS(=O)(=O)N(Cc1cccnc1)c1ccc(Cc2ccccc2)cc1 10.1016/j.bmcl.2004.04.017
CHEMBL104541 4904 None 0 Human Binding pEC50 = 5.8 5.8 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 366 7 0 3 4.0 CCS(=O)(=O)N(Cc1cccnc1)c1ccc(Cc2ccccc2)cc1 10.1016/j.bmcl.2004.04.017
44335514 4953 None 0 Human Binding pEC50 = 5.8 5.8 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 360 6 0 4 3.3 CCS(=O)(=O)N(Cc1cccnc1)c1cccc(OC(F)(F)F)c1 10.1016/j.bmcl.2004.04.017
CHEMBL104785 4953 None 0 Human Binding pEC50 = 5.8 5.8 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 360 6 0 4 3.3 CCS(=O)(=O)N(Cc1cccnc1)c1cccc(OC(F)(F)F)c1 10.1016/j.bmcl.2004.04.017
44404948 70578 None 0 Rat Binding pEC50 = 4.8 4.8 - 1
Effective concentration against mGluR2 receptor expressed in CHO cellsEffective concentration against mGluR2 receptor expressed in CHO cells
ChEMBL 214 2 3 5 -1.0 NC1(C(=O)O)CC2ON=C(C(=O)O)C2C1 10.1021/jm0504499
CHEMBL194787 70578 None 0 Rat Binding pEC50 = 4.8 4.8 - 1
Effective concentration against mGluR2 receptor expressed in CHO cellsEffective concentration against mGluR2 receptor expressed in CHO cells
ChEMBL 214 2 3 5 -1.0 NC1(C(=O)O)CC2ON=C(C(=O)O)C2C1 10.1021/jm0504499
1310 2315 None 61 Rat Binding pEC50 = 4.8 4.8 -13 18
Agonist activity at rat mGlu2 receptor by FRET based mGlu sensor assayAgonist activity at rat mGlu2 receptor by FRET based mGlu sensor assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
1369 2315 None 61 Rat Binding pEC50 = 4.8 4.8 -13 18
Agonist activity at rat mGlu2 receptor by FRET based mGlu sensor assayAgonist activity at rat mGlu2 receptor by FRET based mGlu sensor assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
33032 2315 None 61 Rat Binding pEC50 = 4.8 4.8 -13 18
Agonist activity at rat mGlu2 receptor by FRET based mGlu sensor assayAgonist activity at rat mGlu2 receptor by FRET based mGlu sensor assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
44272391 2315 None 61 Rat Binding pEC50 = 4.8 4.8 -13 18
Agonist activity at rat mGlu2 receptor by FRET based mGlu sensor assayAgonist activity at rat mGlu2 receptor by FRET based mGlu sensor assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
88747398 2315 None 61 Rat Binding pEC50 = 4.8 4.8 -13 18
Agonist activity at rat mGlu2 receptor by FRET based mGlu sensor assayAgonist activity at rat mGlu2 receptor by FRET based mGlu sensor assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
CHEMBL575060 2315 None 61 Rat Binding pEC50 = 4.8 4.8 -13 18
Agonist activity at rat mGlu2 receptor by FRET based mGlu sensor assayAgonist activity at rat mGlu2 receptor by FRET based mGlu sensor assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
DB00142 2315 None 61 Rat Binding pEC50 = 4.8 4.8 -13 18
Agonist activity at rat mGlu2 receptor by FRET based mGlu sensor assayAgonist activity at rat mGlu2 receptor by FRET based mGlu sensor assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
90643895 111937 None 0 Rat Binding pEC50 = 6.8 6.8 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 388 10 2 6 3.8 COc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(C)=O)c(O)c1C 10.1021/jm5000563
CHEMBL3287703 111937 None 0 Rat Binding pEC50 = 6.8 6.8 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 388 10 2 6 3.8 COc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(C)=O)c(O)c1C 10.1021/jm5000563
90643880 111943 None 0 Rat Binding pEC50 = 6.8 6.8 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 402 11 2 6 4.2 CCC(=O)c1ccc(OCCCCOc2cc(C(=O)O)ccc2OC)c(C)c1O 10.1021/jm5000563
CHEMBL3287709 111943 None 0 Rat Binding pEC50 = 6.8 6.8 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 402 11 2 6 4.2 CCC(=O)c1ccc(OCCCCOc2cc(C(=O)O)ccc2OC)c(C)c1O 10.1021/jm5000563
24905705 184128 None 0 Rat Binding pEC50 = 5.8 5.8 - 0
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay
ChEMBL 219 7 4 4 -0.6 N[C@@H](C[C@@H](CCC(=O)O)C(=O)O)C(=O)O 10.1021/acs.jmedchem.5b01333
CHEMBL482081 184128 None 0 Rat Binding pEC50 = 5.8 5.8 - 0
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay
ChEMBL 219 7 4 4 -0.6 N[C@@H](C[C@@H](CCC(=O)O)C(=O)O)C(=O)O 10.1021/acs.jmedchem.5b01333
25195461 2144 None 42 Human Binding pEC50 = 5.8 5.8 - 1
Positive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
8946 2144 None 42 Human Binding pEC50 = 5.8 5.8 - 1
Positive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
CHEMBL3337527 2144 None 42 Human Binding pEC50 = 5.8 5.8 - 1
Positive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
DB12059 2144 None 42 Human Binding pEC50 = 5.8 5.8 - 1
Positive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
164616255 185054 None 0 Rat Binding pEC50 = 6.8 6.8 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 445 10 2 5 5.1 CNC(=O)c1cc(OCCCCOc2ccc(C(=O)CC(C)(C)C)c(O)c2C)ccc1F 10.1016/j.bmcl.2021.128342
CHEMBL4853748 185054 None 0 Rat Binding pEC50 = 6.8 6.8 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 445 10 2 5 5.1 CNC(=O)c1cc(OCCCCOc2ccc(C(=O)CC(C)(C)C)c(O)c2C)ccc1F 10.1016/j.bmcl.2021.128342
11663312 63489 None 0 Human Binding pEC50 = 6.8 6.8 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 497 7 0 4 7.8 O=C1c2c(cc(OCc3cccc(CSc4ccncc4)c3)c(Cl)c2Cl)CC1C1CCCC1 10.1016/j.bmcl.2005.01.077
CHEMBL179839 63489 None 0 Human Binding pEC50 = 6.8 6.8 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 497 7 0 4 7.8 O=C1c2c(cc(OCc3cccc(CSc4ccncc4)c3)c(Cl)c2Cl)CC1C1CCCC1 10.1016/j.bmcl.2005.01.077
24905705 184128 None 0 Rat Binding pEC50 = 5.8 5.8 - 0
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay
ChEMBL 219 7 4 4 -0.6 N[C@@H](C[C@@H](CCC(=O)O)C(=O)O)C(=O)O 10.1021/acs.jmedchem.5b01333
CHEMBL482081 184128 None 0 Rat Binding pEC50 = 5.8 5.8 - 0
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay
ChEMBL 219 7 4 4 -0.6 N[C@@H](C[C@@H](CCC(=O)O)C(=O)O)C(=O)O 10.1021/acs.jmedchem.5b01333
44335555 5038 None 0 Human Binding pEC50 = 7.8 7.8 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 416 9 0 4 4.4 CCC(C)COc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1 10.1016/j.bmcl.2004.04.017
CHEMBL105193 5038 None 0 Human Binding pEC50 = 7.8 7.8 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 416 9 0 4 4.4 CCC(C)COc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1 10.1016/j.bmcl.2004.04.017
49765871 2145 None 41 Human Binding pEC50 = 7.8 7.8 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.6b00913
6317 2145 None 41 Human Binding pEC50 = 7.8 7.8 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.6b00913
CHEMBL2179319 2145 None 41 Human Binding pEC50 = 7.8 7.8 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.6b00913
134156113 150960 None 0 Human Binding pEC50 = 7.8 7.8 - 0
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 483 5 0 5 5.3 FC(F)(F)c1c(CN2CCN(c3ccc(Cl)cc3Cl)CC2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.6b00913
CHEMBL3957311 150960 None 0 Human Binding pEC50 = 7.8 7.8 - 0
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 483 5 0 5 5.3 FC(F)(F)c1c(CN2CCN(c3ccc(Cl)cc3Cl)CC2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.6b00913
71117730 144018 None 0 Human Binding pEC50 = 7.8 7.8 - 0
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 421 3 0 7 3.1 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3ncco3)nc21 nan
CHEMBL3902193 144018 None 0 Human Binding pEC50 = 7.8 7.8 - 0
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 421 3 0 7 3.1 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3ncco3)nc21 nan
46182736 989 None 0 Rat Binding pEC50 = 6.8 6.8 - 0
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 479 6 1 5 6.8 OC(=O)c1cc(ccc1Cl)c1cccc(c1)COc1ccc2c(c1)sn(c2=O)C1CCCC1 10.1021/jm3005306
6323 989 None 0 Rat Binding pEC50 = 6.8 6.8 - 0
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 479 6 1 5 6.8 OC(=O)c1cc(ccc1Cl)c1cccc(c1)COc1ccc2c(c1)sn(c2=O)C1CCCC1 10.1021/jm3005306
CHEMBL1651219 989 None 0 Rat Binding pEC50 = 6.8 6.8 - 0
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 479 6 1 5 6.8 OC(=O)c1cc(ccc1Cl)c1cccc(c1)COc1ccc2c(c1)sn(c2=O)C1CCCC1 10.1021/jm3005306
53390521 82729 None 0 Rat Binding pEC50 = 6.8 6.8 - 0
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 457 7 1 4 5.5 COc1ccc(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)cc1C(=O)O 10.1021/jm3005306
CHEMBL2179638 82729 None 0 Rat Binding pEC50 = 6.8 6.8 - 0
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 457 7 1 4 5.5 COc1ccc(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)cc1C(=O)O 10.1021/jm3005306
46182736 989 None 0 Rat Binding pEC50 = 6.8 6.8 - 0
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 479 6 1 5 6.8 OC(=O)c1cc(ccc1Cl)c1cccc(c1)COc1ccc2c(c1)sn(c2=O)C1CCCC1 10.1021/jm1012165
6323 989 None 0 Rat Binding pEC50 = 6.8 6.8 - 0
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 479 6 1 5 6.8 OC(=O)c1cc(ccc1Cl)c1cccc(c1)COc1ccc2c(c1)sn(c2=O)C1CCCC1 10.1021/jm1012165
CHEMBL1651219 989 None 0 Rat Binding pEC50 = 6.8 6.8 - 0
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 479 6 1 5 6.8 OC(=O)c1cc(ccc1Cl)c1cccc(c1)COc1ccc2c(c1)sn(c2=O)C1CCCC1 10.1021/jm1012165
1402 122 None 35 Human Binding pEC50 = 5.8 5.8 - 0
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 452 8 0 5 4.8 COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 10.1016/j.bmcl.2004.08.020
9825084 122 None 35 Human Binding pEC50 = 5.8 5.8 - 0
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 452 8 0 5 4.8 COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 10.1016/j.bmcl.2004.08.020
CHEMBL108939 122 None 35 Human Binding pEC50 = 5.8 5.8 - 0
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 452 8 0 5 4.8 COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 10.1016/j.bmcl.2004.08.020
90643882 111950 None 0 Rat Binding pEC50 = 6.8 6.8 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 404 10 2 5 4.6 Cc1c(OCCCCOc2ccc(F)c(C(=O)O)c2)ccc(C(=O)C(C)C)c1O 10.1021/jm5000563
CHEMBL3287716 111950 None 0 Rat Binding pEC50 = 6.8 6.8 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 404 10 2 5 4.6 Cc1c(OCCCCOc2ccc(F)c(C(=O)O)c2)ccc(C(=O)C(C)C)c1O 10.1021/jm5000563
90643876 111933 None 0 Rat Binding pEC50 = 6.8 6.8 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 414 11 2 5 5.2 Cc1cc(OCCCCOc2ccc(C(=O)CC(C)C)c(O)c2C)ccc1C(=O)O 10.1021/jm5000563
CHEMBL3287699 111933 None 0 Rat Binding pEC50 = 6.8 6.8 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 414 11 2 5 5.2 Cc1cc(OCCCCOc2ccc(C(=O)CC(C)C)c(O)c2C)ccc1C(=O)O 10.1021/jm5000563
44335578 109730 None 0 Human Binding pEC50 = 7.8 7.8 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 402 8 0 4 4.2 CCC(C)Oc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1 10.1016/j.bmcl.2004.04.017
CHEMBL322588 109730 None 0 Human Binding pEC50 = 7.8 7.8 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 402 8 0 4 4.2 CCC(C)Oc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1 10.1016/j.bmcl.2004.04.017
66787355 156316 None 0 Human Binding pEC50 = 7.7 7.7 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cells assessed as cellular impedance measured for 20 mins with 15 sec time interval followed by 40 mins with 5 mins time interval and subsequently measured with 15 mins time interval in presence of endogenous glutamate levels by RTCAPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cells assessed as cellular impedance measured for 20 mins with 15 sec time interval followed by 40 mins with 5 mins time interval and subsequently measured with 15 mins time interval in presence of endogenous glutamate levels by RTCA
ChEMBL 450 5 1 5 5.6 FC(F)(F)c1c(-c2ccc(NC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
CHEMBL4064589 156316 None 0 Human Binding pEC50 = 7.7 7.7 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cells assessed as cellular impedance measured for 20 mins with 15 sec time interval followed by 40 mins with 5 mins time interval and subsequently measured with 15 mins time interval in presence of endogenous glutamate levels by RTCAPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cells assessed as cellular impedance measured for 20 mins with 15 sec time interval followed by 40 mins with 5 mins time interval and subsequently measured with 15 mins time interval in presence of endogenous glutamate levels by RTCA
ChEMBL 450 5 1 5 5.6 FC(F)(F)c1c(-c2ccc(NC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
23521698 108602 None 0 Human Binding pEC50 = 6.8 6.8 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 384 7 0 3 4.5 CCS(=O)(=O)N(Cc1cccnc1)c1cccc(C(F)c2ccccc2)c1 10.1016/j.bmcl.2004.04.017
CHEMBL320151 108602 None 0 Human Binding pEC50 = 6.8 6.8 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 384 7 0 3 4.5 CCS(=O)(=O)N(Cc1cccnc1)c1cccc(C(F)c2ccccc2)c1 10.1016/j.bmcl.2004.04.017
11648824 57342 None 1 Rat Binding pEC50 = 6.8 6.8 - 0
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 488 6 1 3 7.4 Cc1c(OCc2cccc(-c3ccc(Cl)c(C(=O)O)c3)c2)cc2c(c1C)C(=O)C(C1CCCC1)C2 10.1021/jm1012165
CHEMBL1651207 57342 None 1 Rat Binding pEC50 = 6.8 6.8 - 0
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 488 6 1 3 7.4 Cc1c(OCc2cccc(-c3ccc(Cl)c(C(=O)O)c3)c2)cc2c(c1C)C(=O)C(C1CCCC1)C2 10.1021/jm1012165
1310 2315 None 61 Human Binding pEC50 = 5.8 5.8 -22 18
Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1039/C1MD00186H
1369 2315 None 61 Human Binding pEC50 = 5.8 5.8 -22 18
Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1039/C1MD00186H
33032 2315 None 61 Human Binding pEC50 = 5.8 5.8 -22 18
Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1039/C1MD00186H
44272391 2315 None 61 Human Binding pEC50 = 5.8 5.8 -22 18
Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1039/C1MD00186H
88747398 2315 None 61 Human Binding pEC50 = 5.8 5.8 -22 18
Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1039/C1MD00186H
CHEMBL575060 2315 None 61 Human Binding pEC50 = 5.8 5.8 -22 18
Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1039/C1MD00186H
DB00142 2315 None 61 Human Binding pEC50 = 5.8 5.8 -22 18
Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1039/C1MD00186H
1310 2315 None 61 Rat Binding pEC50 = 5.8 5.8 -13 18
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
1369 2315 None 61 Rat Binding pEC50 = 5.8 5.8 -13 18
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
33032 2315 None 61 Rat Binding pEC50 = 5.8 5.8 -13 18
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
44272391 2315 None 61 Rat Binding pEC50 = 5.8 5.8 -13 18
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
88747398 2315 None 61 Rat Binding pEC50 = 5.8 5.8 -13 18
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
CHEMBL575060 2315 None 61 Rat Binding pEC50 = 5.8 5.8 -13 18
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
DB00142 2315 None 61 Rat Binding pEC50 = 5.8 5.8 -13 18
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
89497771 138081 None 0 Human Binding pEC50 = 6.7 6.7 - 0
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 325 3 1 5 2.9 Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccc(CO)cc3)nc21 10.1016/j.bmcl.2016.01.021
CHEMBL3764530 138081 None 0 Human Binding pEC50 = 6.7 6.7 - 0
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 325 3 1 5 2.9 Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccc(CO)cc3)nc21 10.1016/j.bmcl.2016.01.021
1310 2315 None 61 Rat Binding pEC50 = 5.7 5.7 -13 18
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
1369 2315 None 61 Rat Binding pEC50 = 5.7 5.7 -13 18
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
33032 2315 None 61 Rat Binding pEC50 = 5.7 5.7 -13 18
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
44272391 2315 None 61 Rat Binding pEC50 = 5.7 5.7 -13 18
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
88747398 2315 None 61 Rat Binding pEC50 = 5.7 5.7 -13 18
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
CHEMBL575060 2315 None 61 Rat Binding pEC50 = 5.7 5.7 -13 18
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
DB00142 2315 None 61 Rat Binding pEC50 = 5.7 5.7 -13 18
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/acs.jmedchem.5b01333
10407808 66696 None 0 Human Binding pEC50 = 5.7 5.7 - 0
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 386 11 2 5 4.5 CCCc1c(OCCCCOc2ccc(C(=O)O)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2004.08.020
CHEMBL185419 66696 None 0 Human Binding pEC50 = 5.7 5.7 - 0
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 386 11 2 5 4.5 CCCc1c(OCCCCOc2ccc(C(=O)O)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2004.08.020
90643887 111957 None 0 Rat Binding pEC50 = 6.7 6.7 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 444 11 2 6 5.3 COc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)CC(C)(C)C)c(O)c1C 10.1021/jm5000563
CHEMBL3287723 111957 None 0 Rat Binding pEC50 = 6.7 6.7 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 444 11 2 6 5.3 COc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)CC(C)(C)C)c(O)c1C 10.1021/jm5000563
89735344 138131 None 0 Human Binding pEC50 = 6.7 6.7 - 0
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 325 3 0 5 3.5 COc1ccccc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C 10.1016/j.bmcl.2016.01.021
CHEMBL3765257 138131 None 0 Human Binding pEC50 = 6.7 6.7 - 0
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 325 3 0 5 3.5 COc1ccccc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C 10.1016/j.bmcl.2016.01.021
11213605 64486 None 3 Human Binding pEC50 = 6.7 6.7 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 471 8 0 4 7.4 CCCC1Cc2cc(OCc3cccc(CSc4ccncc4)c3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
CHEMBL181364 64486 None 3 Human Binding pEC50 = 6.7 6.7 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 471 8 0 4 7.4 CCCC1Cc2cc(OCc3cccc(CSc4ccncc4)c3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
127042771 138140 None 0 Human Binding pEC50 = 6.7 6.7 - 0
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 373 3 0 6 2.9 Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3cccc(S(C)(=O)=O)c3)nc21 10.1016/j.bmcl.2016.01.021
CHEMBL3765337 138140 None 0 Human Binding pEC50 = 6.7 6.7 - 0
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 373 3 0 6 2.9 Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3cccc(S(C)(=O)=O)c3)nc21 10.1016/j.bmcl.2016.01.021
90643869 111925 None 0 Rat Binding pEC50 = 6.7 6.7 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 414 11 2 5 5.2 Cc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)CC(C)C)c(O)c1C 10.1021/jm5000563
CHEMBL3287691 111925 None 0 Rat Binding pEC50 = 6.7 6.7 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 414 11 2 5 5.2 Cc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)CC(C)C)c(O)c1C 10.1021/jm5000563
89497792 138123 None 0 Human Binding pEC50 = 6.7 6.7 - 0
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 320 2 0 5 3.3 Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccc(C#N)cc3)nc21 10.1016/j.bmcl.2016.01.021
CHEMBL3765103 138123 None 0 Human Binding pEC50 = 6.7 6.7 - 0
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 320 2 0 5 3.3 Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccc(C#N)cc3)nc21 10.1016/j.bmcl.2016.01.021
164611067 184722 None 0 Rat Binding pEC50 = 6.7 6.7 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 444 10 2 6 5.1 COc1cc(OC[C@H](C)COc2ccc(C(=O)CC(C)(C)C)c(O)c2C)ccc1C(=O)O 10.1016/j.bmcl.2021.128342
CHEMBL4849142 184722 None 0 Rat Binding pEC50 = 6.7 6.7 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 444 10 2 6 5.1 COc1cc(OC[C@H](C)COc2ccc(C(=O)CC(C)(C)C)c(O)c2C)ccc1C(=O)O 10.1016/j.bmcl.2021.128342
11633075 65411 None 0 Human Binding pEC50 = 6.7 6.7 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 416 5 1 5 4.8 CC(C)C1Cc2cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
CHEMBL182946 65411 None 0 Human Binding pEC50 = 6.7 6.7 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 416 5 1 5 4.8 CC(C)C1Cc2cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
25125217 555 None 27 Human Binding pEC50 = 6.7 6.7 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 487 6 1 7 3.5 Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1 10.1021/acs.jmedchem.6b00913
7678 555 None 27 Human Binding pEC50 = 6.7 6.7 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 487 6 1 7 3.5 Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1 10.1021/acs.jmedchem.6b00913
CHEMBL3937907 555 None 27 Human Binding pEC50 = 6.7 6.7 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 487 6 1 7 3.5 Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1 10.1021/acs.jmedchem.6b00913
DB16073 555 None 27 Human Binding pEC50 = 6.7 6.7 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 487 6 1 7 3.5 Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1 10.1021/acs.jmedchem.6b00913
24815434 202152 None 0 Human Binding pEC50 = 6.7 6.7 - 3
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 305 3 0 3 4.0 Cn1c(CN2CCC(c3ccccc3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL593196 202152 None 0 Human Binding pEC50 = 6.7 6.7 - 3
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 305 3 0 3 4.0 Cn1c(CN2CCC(c3ccccc3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
46225335 202503 None 0 Human Binding pEC50 = 6.7 6.7 - 1
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 374 3 0 4 3.9 Cn1c(CN2CCN(c3ccc(C(F)(F)F)cc3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL595608 202503 None 0 Human Binding pEC50 = 6.7 6.7 - 1
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 374 3 0 4 3.9 Cn1c(CN2CCN(c3ccc(C(F)(F)F)cc3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
46225583 202630 None 0 Human Binding pEC50 = 6.7 6.7 - 3
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 362 3 0 5 4.6 Cn1c(CN2CCC(c3nsc4ccccc34)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL596527 202630 None 0 Human Binding pEC50 = 6.7 6.7 - 3
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 362 3 0 5 4.6 Cn1c(CN2CCC(c3nsc4ccccc34)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
46225408 204331 None 0 Human Binding pEC50 = 6.7 6.7 - 0
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 427 3 0 5 4.1 Cn1c(CN2CCN(c3nc(Cl)ccc3C(F)(F)F)CC2)nc2cc(F)ccc21 10.1016/j.bmcl.2009.11.032
CHEMBL607313 204331 None 0 Human Binding pEC50 = 6.7 6.7 - 0
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 427 3 0 5 4.1 Cn1c(CN2CCN(c3nc(Cl)ccc3C(F)(F)F)CC2)nc2cc(F)ccc21 10.1016/j.bmcl.2009.11.032
46225387 202219 None 0 Human Binding pEC50 = 5.7 5.7 - 0
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 477 3 0 5 5.0 Cn1c(CN2CCN(c3nc(Cl)ccc3C(F)(F)F)CC2)nc2cc(C(F)(F)F)ccc21 10.1016/j.bmcl.2009.11.032
CHEMBL593756 202219 None 0 Human Binding pEC50 = 5.7 5.7 - 0
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 477 3 0 5 5.0 Cn1c(CN2CCN(c3nc(Cl)ccc3C(F)(F)F)CC2)nc2cc(C(F)(F)F)ccc21 10.1016/j.bmcl.2009.11.032
56968082 143998 None 0 Human Binding pEC50 = 8.6 8.6 - 0
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 428 5 0 4 5.3 CC1(c2ccccc2)CCCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)C1 10.1021/acs.jmedchem.6b00913
CHEMBL3901998 143998 None 0 Human Binding pEC50 = 8.6 8.6 - 0
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 428 5 0 4 5.3 CC1(c2ccccc2)CCCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)C1 10.1021/acs.jmedchem.6b00913
25051025 182573 None 0 Rat Binding pEC50 = 7.7 7.7 - 0
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 402 5 0 5 3.7 Cn1c(CN2C[C@@H]3C(COc4ccc(C(F)(F)F)cc4)[C@@H]3C2)nc2ncccc21 10.1016/j.bmcl.2008.09.026
CHEMBL478646 182573 None 0 Rat Binding pEC50 = 7.7 7.7 - 0
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 402 5 0 5 3.7 Cn1c(CN2C[C@@H]3C(COc4ccc(C(F)(F)F)cc4)[C@@H]3C2)nc2ncccc21 10.1016/j.bmcl.2008.09.026
53390433 82723 None 0 Rat Binding pEC50 = 7.7 7.7 - 0
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 443 6 2 4 5.2 O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)ccc1O 10.1021/jm3005306
CHEMBL2179632 82723 None 0 Rat Binding pEC50 = 7.7 7.7 - 0
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 443 6 2 4 5.2 O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)ccc1O 10.1021/jm3005306
66799514 82735 None 0 Rat Binding pEC50 = 7.7 7.7 - 0
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 431 4 1 2 6.3 O=C(O)c1cc(-c2cccc(-c3ccc4c(c3)CN(C3CCCC3)C4=O)c2)ccc1Cl 10.1021/jm3005306
CHEMBL2179646 82735 None 0 Rat Binding pEC50 = 7.7 7.7 - 0
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 431 4 1 2 6.3 O=C(O)c1cc(-c2cccc(-c3ccc4c(c3)CN(C3CCCC3)C4=O)c2)ccc1Cl 10.1021/jm3005306
23521677 107510 None 0 Human Binding pEC50 = 6.7 6.7 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 378 7 0 3 4.5 C=C(c1ccccc1)c1cccc(N(Cc2cccnc2)S(=O)(=O)CC)c1 10.1016/j.bmcl.2004.04.017
CHEMBL318309 107510 None 0 Human Binding pEC50 = 6.7 6.7 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 378 7 0 3 4.5 C=C(c1ccccc1)c1cccc(N(Cc2cccnc2)S(=O)(=O)CC)c1 10.1016/j.bmcl.2004.04.017
53390754 82732 None 0 Rat Binding pEC50 = 6.7 6.7 - 0
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 490 7 1 7 6.0 O=C(O)c1cc(-c2cccc(COc3ccc4c(=O)n(C5CCCC5)sc4c3)c2)cc([N+](=O)[O-])c1 10.1021/jm3005306
CHEMBL2179643 82732 None 0 Rat Binding pEC50 = 6.7 6.7 - 0
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 490 7 1 7 6.0 O=C(O)c1cc(-c2cccc(COc3ccc4c(=O)n(C5CCCC5)sc4c3)c2)cc([N+](=O)[O-])c1 10.1021/jm3005306
90643897 111939 None 0 Rat Binding pEC50 = 6.7 6.7 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 372 9 2 5 4.1 CC(=O)c1ccc(OCCCCOc2cccc(C(=O)O)c2C)c(C)c1O 10.1021/jm5000563
CHEMBL3287705 111939 None 0 Rat Binding pEC50 = 6.7 6.7 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 372 9 2 5 4.1 CC(=O)c1ccc(OCCCCOc2cccc(C(=O)O)c2C)c(C)c1O 10.1021/jm5000563
104766 33 None 30 Human Binding pEC50 = 5.7 5.7 -11 11
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1021/jm970719q
1365 33 None 30 Human Binding pEC50 = 5.7 5.7 -11 11
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1021/jm970719q
CHEMBL34453 33 None 30 Human Binding pEC50 = 5.7 5.7 -11 11
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1021/jm970719q
25195461 2144 None 42 Human Binding pEC50 = 5.7 5.7 - 1
Positive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
8946 2144 None 42 Human Binding pEC50 = 5.7 5.7 - 1
Positive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
CHEMBL3337527 2144 None 42 Human Binding pEC50 = 5.7 5.7 - 1
Positive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
DB12059 2144 None 42 Human Binding pEC50 = 5.7 5.7 - 1
Positive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
10002415 166121 None 0 Human Binding pEC50 = 5.7 5.7 - 0
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 423 11 2 7 4.0 CCCc1c(OCCCCN(C)c2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2004.08.020
CHEMBL425540 166121 None 0 Human Binding pEC50 = 5.7 5.7 - 0
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 423 11 2 7 4.0 CCCc1c(OCCCCN(C)c2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2004.08.020
90643889 111960 None 0 Rat Binding pEC50 = 6.7 6.7 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 432 10 2 5 5.4 Cc1c(OCCCCOc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1021/jm5000563
CHEMBL3287726 111960 None 0 Rat Binding pEC50 = 6.7 6.7 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 432 10 2 5 5.4 Cc1c(OCCCCOc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1021/jm5000563
49822115 2146 None 24 Human Binding pEC50 = 7.7 7.7 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 414 5 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.6b00913
8947 2146 None 24 Human Binding pEC50 = 7.7 7.7 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 414 5 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.6b00913
CHEMBL3947764 2146 None 24 Human Binding pEC50 = 7.7 7.7 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 414 5 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.6b00913
11275666 90091 None 1 Human Binding pEC50 = 7.7 7.7 -15 2
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 200 2 4 4 -1.6 N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/jm4000165
CHEMBL2381647 90091 None 1 Human Binding pEC50 = 7.7 7.7 -15 2
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 200 2 4 4 -1.6 N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/jm4000165
164627946 186490 None 0 Rat Binding pEC50 = 6.7 6.7 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 428 10 2 5 5.6 Cc1ccc(OCCCCOc2ccc(C(=O)CC(C)(C)C)c(O)c2C)cc1C(=O)O 10.1016/j.bmcl.2021.128342
CHEMBL4875695 186490 None 0 Rat Binding pEC50 = 6.7 6.7 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 428 10 2 5 5.6 Cc1ccc(OCCCCOc2ccc(C(=O)CC(C)(C)C)c(O)c2C)cc1C(=O)O 10.1016/j.bmcl.2021.128342
44335500 5124 None 0 Human Binding pEC50 = 5.7 5.7 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 360 6 0 4 3.0 COc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1 10.1016/j.bmcl.2004.04.017
CHEMBL105671 5124 None 0 Human Binding pEC50 = 5.7 5.7 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 360 6 0 4 3.0 COc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1 10.1016/j.bmcl.2004.04.017
23521734 109816 None 0 Human Binding pEC50 = 5.7 5.7 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 382 8 0 4 4.0 CCS(=O)(=O)N(Cc1cccnc1)c1ccc(COc2ccccc2)cc1 10.1016/j.bmcl.2004.04.017
CHEMBL323080 109816 None 0 Human Binding pEC50 = 5.7 5.7 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 382 8 0 4 4.0 CCS(=O)(=O)N(Cc1cccnc1)c1ccc(COc2ccccc2)cc1 10.1016/j.bmcl.2004.04.017
25051018 184455 None 0 Rat Binding pEC50 = 5.7 5.7 - 0
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 334 5 0 5 2.7 Cn1c(CN2C[C@@H]3C(COc4ccccc4)[C@@H]3C2)nc2ccncc21 10.1016/j.bmcl.2008.09.026
CHEMBL484398 184455 None 0 Rat Binding pEC50 = 5.7 5.7 - 0
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 334 5 0 5 2.7 Cn1c(CN2C[C@@H]3C(COc4ccccc4)[C@@H]3C2)nc2ccncc21 10.1016/j.bmcl.2008.09.026
54761054 138168 None 0 Rat Binding pEC50 = 6.7 6.7 - 2
Positive allosteric modulation of rat mGluR2 by GTP-gamma-S binding assayPositive allosteric modulation of rat mGluR2 by GTP-gamma-S binding assay
ChEMBL 367 3 1 5 4.0 Cc1ccc(C(C)(C)O)cc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C 10.1016/j.bmcl.2016.01.021
CHEMBL3765778 138168 None 0 Rat Binding pEC50 = 6.7 6.7 - 2
Positive allosteric modulation of rat mGluR2 by GTP-gamma-S binding assayPositive allosteric modulation of rat mGluR2 by GTP-gamma-S binding assay
ChEMBL 367 3 1 5 4.0 Cc1ccc(C(C)(C)O)cc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C 10.1016/j.bmcl.2016.01.021
71136691 143708 None 0 Human Binding pEC50 = 6.7 6.7 - 0
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 394 3 0 5 3.2 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)C3CC3)nc21 nan
CHEMBL3899706 143708 None 0 Human Binding pEC50 = 6.7 6.7 - 0
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 394 3 0 5 3.2 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)C3CC3)nc21 nan
134157889 154305 None 0 Human Binding pEC50 = 7.7 7.7 - 0
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 465 5 0 5 4.7 Fc1ccc(N2CCCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
CHEMBL3985987 154305 None 0 Human Binding pEC50 = 7.7 7.7 - 0
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 465 5 0 5 4.7 Fc1ccc(N2CCCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
50993967 57348 None 0 Rat Binding pEC50 = 6.7 6.7 - 0
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 433 6 1 3 5.4 O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(C3CC3)C4=O)c2)ccc1Cl 10.1021/jm1012165
CHEMBL1651213 57348 None 0 Rat Binding pEC50 = 6.7 6.7 - 0
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 433 6 1 3 5.4 O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(C3CC3)C4=O)c2)ccc1Cl 10.1021/jm1012165
51037131 140371 None 0 Human Binding pEC50 = 5.7 5.7 - 0
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 356 2 0 5 3.9 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CCCC4CCCCC43)nc21 10.1021/acsmedchemlett.5b00459
CHEMBL3805883 140371 None 0 Human Binding pEC50 = 5.7 5.7 - 0
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 356 2 0 5 3.9 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CCCC4CCCCC43)nc21 10.1021/acsmedchemlett.5b00459
90643860 111912 None 0 Rat Binding pEC50 = 6.7 6.7 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 400 11 2 5 4.9 Cc1c(OCCCCOc2cccc(C(=O)O)c2)ccc(C(=O)CC(C)C)c1O 10.1021/jm5000563
CHEMBL3287675 111912 None 0 Rat Binding pEC50 = 6.7 6.7 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 400 11 2 5 4.9 Cc1c(OCCCCOc2cccc(C(=O)O)c2)ccc(C(=O)CC(C)C)c1O 10.1021/jm5000563
164611059 184685 None 0 Rat Binding pEC50 = 6.7 6.7 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 432 9 2 5 5.3 Cc1c(OC[C@@H](C)COc2ccc(C(=O)O)cc2F)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
CHEMBL4848600 184685 None 0 Rat Binding pEC50 = 6.7 6.7 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 432 9 2 5 5.3 Cc1c(OC[C@@H](C)COc2ccc(C(=O)O)cc2F)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
11496256 63807 None 0 Human Binding pEC50 = 6.7 6.7 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 456 5 1 5 5.7 CC1(C2CCCC2)Cc2cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
CHEMBL180186 63807 None 0 Human Binding pEC50 = 6.7 6.7 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 456 5 1 5 5.7 CC1(C2CCCC2)Cc2cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
11656483 123670 None 0 Human Binding pEC50 = 6.7 6.7 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 514 9 1 6 6.3 CC1(C2CCCC2)Cc2cc(OCCCCOc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
CHEMBL361837 123670 None 0 Human Binding pEC50 = 6.7 6.7 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 514 9 1 6 6.3 CC1(C2CCCC2)Cc2cc(OCCCCOc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
90643873 111930 None 0 Rat Binding pEC50 = 6.6 6.6 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 456 13 2 6 5.4 Cc1c(OCCCCOCOc2ccc(C(=O)O)cc2)ccc(C(=O)CC2CCCC2)c1O 10.1021/jm5000563
CHEMBL3287696 111930 None 0 Rat Binding pEC50 = 6.6 6.6 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 456 13 2 6 5.4 Cc1c(OCCCCOCOc2ccc(C(=O)O)cc2)ccc(C(=O)CC2CCCC2)c1O 10.1021/jm5000563
9979770 66359 None 0 Human Binding pEC50 = 6.6 6.6 - 0
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 424 11 2 7 4.3 Cc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.08.020
CHEMBL185054 66359 None 0 Human Binding pEC50 = 6.6 6.6 - 0
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 424 11 2 7 4.3 Cc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.08.020
49765871 2145 None 41 Human Binding pEC50 = 7.6 7.6 - 1
Positive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.6b00913
6317 2145 None 41 Human Binding pEC50 = 7.6 7.6 - 1
Positive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.6b00913
CHEMBL2179319 2145 None 41 Human Binding pEC50 = 7.6 7.6 - 1
Positive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.6b00913
44335614 5289 None 0 Human Binding pEC50 = 6.6 6.6 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 446 9 0 6 3.3 CCOC(=O)C(C)Oc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1 10.1016/j.bmcl.2004.04.017
CHEMBL106561 5289 None 0 Human Binding pEC50 = 6.6 6.6 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 446 9 0 6 3.3 CCOC(=O)C(C)Oc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1 10.1016/j.bmcl.2004.04.017
45082292 115315 None 0 Human Binding pEC50 = 4.6 4.6 -3 3
Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells
ChEMBL 159 3 3 3 -0.7 N[C@@]1(C(=O)O)C[C@@H]1CC(=O)O 10.1039/C1MD00186H
CHEMBL3347670 115315 None 0 Human Binding pEC50 = 4.6 4.6 -3 3
Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells
ChEMBL 159 3 3 3 -0.7 N[C@@]1(C(=O)O)C[C@@H]1CC(=O)O 10.1039/C1MD00186H
90643906 111951 None 0 Rat Binding pEC50 = 6.6 6.6 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 400 10 2 5 4.8 Cc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)C(C)C)c(O)c1C 10.1021/jm5000563
CHEMBL3287717 111951 None 0 Rat Binding pEC50 = 6.6 6.6 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 400 10 2 5 4.8 Cc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)C(C)C)c(O)c1C 10.1021/jm5000563
49822116 147080 None 14 Human Binding pEC50 = 5.6 5.6 - 1
Positive allosteric modulation at human mGlu2 receptor W773A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor W773A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 451 5 0 5 4.3 Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
CHEMBL3926416 147080 None 14 Human Binding pEC50 = 5.6 5.6 - 1
Positive allosteric modulation at human mGlu2 receptor W773A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor W773A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 451 5 0 5 4.3 Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
90643875 111932 None 0 Rat Binding pEC50 = 6.6 6.6 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 460 11 2 5 6.1 Cc1c(OCCCCOc2ccc(C(=O)O)cc2Cl)ccc(C(=O)CC2CCCC2)c1O 10.1021/jm5000563
CHEMBL3287698 111932 None 0 Rat Binding pEC50 = 6.6 6.6 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 460 11 2 5 6.1 Cc1c(OCCCCOc2ccc(C(=O)O)cc2Cl)ccc(C(=O)CC2CCCC2)c1O 10.1021/jm5000563
44578992 181728 None 0 Rat Binding pEC50 = 7.6 7.6 - 0
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 333 5 0 4 3.3 Cn1c(CN2C[C@@H]3C(COc4ccccc4)[C@@H]3C2)nc2ccccc21 10.1016/j.bmcl.2008.09.026
CHEMBL477376 181728 None 0 Rat Binding pEC50 = 7.6 7.6 - 0
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 333 5 0 4 3.3 Cn1c(CN2C[C@@H]3C(COc4ccccc4)[C@@H]3C2)nc2ccccc21 10.1016/j.bmcl.2008.09.026
44335556 1300 None 0 Human Binding pEC50 = 7.6 7.6 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 414 7 0 4 4.3 FC(CS(=O)(=O)N(c1cccc(c1)OC1CCCC1)Cc1cccnc1)(F)F 10.1016/j.bmcl.2004.04.017
6257 1300 None 0 Human Binding pEC50 = 7.6 7.6 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 414 7 0 4 4.3 FC(CS(=O)(=O)N(c1cccc(c1)OC1CCCC1)Cc1cccnc1)(F)F 10.1016/j.bmcl.2004.04.017
CHEMBL321968 1300 None 0 Human Binding pEC50 = 7.6 7.6 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 414 7 0 4 4.3 FC(CS(=O)(=O)N(c1cccc(c1)OC1CCCC1)Cc1cccnc1)(F)F 10.1016/j.bmcl.2004.04.017
53390753 82733 None 0 Rat Binding pEC50 = 6.6 6.6 - 0
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 463 6 1 5 6.3 O=C(O)c1cc(-c2cccc(COc3ccc4c(=O)n(C5CCCC5)sc4c3)c2)ccc1F 10.1021/jm3005306
CHEMBL2179644 82733 None 0 Rat Binding pEC50 = 6.6 6.6 - 0
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 463 6 1 5 6.3 O=C(O)c1cc(-c2cccc(COc3ccc4c(=O)n(C5CCCC5)sc4c3)c2)ccc1F 10.1021/jm3005306
44395327 66946 None 0 Human Binding pEC50 = 6.6 6.6 - 0
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 438 11 2 7 4.7 CCCc1c(OC(C)CCC(C)Oc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2004.08.020
CHEMBL186584 66946 None 0 Human Binding pEC50 = 6.6 6.6 - 0
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 438 11 2 7 4.7 CCCc1c(OC(C)CCC(C)Oc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2004.08.020
90643862 111918 None 0 Rat Binding pEC50 = 5.6 5.6 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 458 11 1 4 6.7 Cc1c(OCCCCOc2ccc(C(=O)O)c(Cl)c2)ccc(C(=O)CC2CCCC2)c1C 10.1021/jm5000563
CHEMBL3287682 111918 None 0 Rat Binding pEC50 = 5.6 5.6 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 458 11 1 4 6.7 Cc1c(OCCCCOc2ccc(C(=O)O)c(Cl)c2)ccc(C(=O)CC2CCCC2)c1C 10.1021/jm5000563
44401995 70098 None 4 Rat Binding pEC50 = 5.6 5.6 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 444 13 3 6 4.9 Cc1c(OCCCCOc2ccc(CCC(=O)O)c(O)c2)ccc(C(=O)CC(C)C)c1O 10.1021/jm5000563
CHEMBL193982 70098 None 4 Rat Binding pEC50 = 5.6 5.6 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 444 13 3 6 4.9 Cc1c(OCCCCOc2ccc(CCC(=O)O)c(O)c2)ccc(C(=O)CC(C)C)c1O 10.1021/jm5000563
71117222 146173 None 0 Human Binding pEC50 = 6.6 6.6 - 0
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 441 4 0 7 2.6 Cn1c(=O)n(CC2CC2(F)F)c2ccc(C3=CC4CN(C(=O)c5ncco5)CC4C3)nc21 nan
CHEMBL3919237 146173 None 0 Human Binding pEC50 = 6.6 6.6 - 0
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 441 4 0 7 2.6 Cn1c(=O)n(CC2CC2(F)F)c2ccc(C3=CC4CN(C(=O)c5ncco5)CC4C3)nc21 nan
53390676 82717 None 0 Rat Binding pEC50 = 5.6 5.6 - 0
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 465 7 1 5 6.1 O=C(O)c1cc(-c2cccc(COc3ccc4c(=O)n(CC5CC5)sc4c3)c2)ccc1Cl 10.1021/jm3005306
CHEMBL2179626 82717 None 0 Rat Binding pEC50 = 5.6 5.6 - 0
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 465 7 1 5 6.1 O=C(O)c1cc(-c2cccc(COc3ccc4c(=O)n(CC5CC5)sc4c3)c2)ccc1Cl 10.1021/jm3005306
54761054 138168 None 0 Rat Binding pEC50 = 7.6 7.6 - 2
Positive allosteric modulation of recombinant rat mGluR2 preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant rat mGluR2 preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 367 3 1 5 4.0 Cc1ccc(C(C)(C)O)cc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C 10.1016/j.bmcl.2016.01.021
CHEMBL3765778 138168 None 0 Rat Binding pEC50 = 7.6 7.6 - 2
Positive allosteric modulation of recombinant rat mGluR2 preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant rat mGluR2 preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 367 3 1 5 4.0 Cc1ccc(C(C)(C)O)cc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C 10.1016/j.bmcl.2016.01.021
44335650 4804 None 0 Human Binding pEC50 = 5.6 5.6 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 382 7 1 4 3.5 CCS(=O)(=O)N(Cc1cccnc1)c1cccc(C(O)c2ccccc2)c1 10.1016/j.bmcl.2004.04.017
CHEMBL104129 4804 None 0 Human Binding pEC50 = 5.6 5.6 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 382 7 1 4 3.5 CCS(=O)(=O)N(Cc1cccnc1)c1cccc(C(O)c2ccccc2)c1 10.1016/j.bmcl.2004.04.017
25050850 191897 None 0 Rat Binding pEC50 = 6.6 6.6 - 0
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 402 5 0 5 3.7 Cn1c(CN2C[C@@H]3C(COc4ccc(C(F)(F)F)cc4)[C@@H]3C2)nc2cnccc21 10.1016/j.bmcl.2008.09.026
CHEMBL519817 191897 None 0 Rat Binding pEC50 = 6.6 6.6 - 0
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 402 5 0 5 3.7 Cn1c(CN2C[C@@H]3C(COc4ccc(C(F)(F)F)cc4)[C@@H]3C2)nc2cnccc21 10.1016/j.bmcl.2008.09.026
46225385 203820 None 0 Human Binding pEC50 = 6.6 6.6 - 0
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 439 4 0 6 4.0 COc1ccc2c(c1)nc(CN1CCN(c3nc(Cl)ccc3C(F)(F)F)CC1)n2C 10.1016/j.bmcl.2009.11.032
CHEMBL604469 203820 None 0 Human Binding pEC50 = 6.6 6.6 - 0
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 439 4 0 6 4.0 COc1ccc2c(c1)nc(CN1CCN(c3nc(Cl)ccc3C(F)(F)F)CC1)n2C 10.1016/j.bmcl.2009.11.032
46225375 204330 None 0 Human Binding pEC50 = 5.6 5.6 - 0
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 437 5 0 5 4.8 CCCn1c(CN2CCN(c3nc(Cl)ccc3C(F)(F)F)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL607311 204330 None 0 Human Binding pEC50 = 5.6 5.6 - 0
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 437 5 0 5 4.8 CCCn1c(CN2CCN(c3nc(Cl)ccc3C(F)(F)F)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
60096211 90093 None 0 Human Binding pEC50 = 6.6 6.6 -5 2
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 242 3 4 4 -1.4 CC(=O)N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/jm4000165
CHEMBL2381649 90093 None 0 Human Binding pEC50 = 6.6 6.6 -5 2
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 242 3 4 4 -1.4 CC(=O)N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/jm4000165
164619969 185635 None 0 Rat Binding pEC50 = 6.6 6.6 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 418 8 2 5 5.0 Cc1c(O[C@@H](C)COc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
CHEMBL4862778 185635 None 0 Rat Binding pEC50 = 6.6 6.6 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 418 8 2 5 5.0 Cc1c(O[C@@H](C)COc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
25195461 2144 None 42 Human Binding pEC50 = 5.6 5.6 - 1
Positive allosteric modulation at human mGlu2 receptor W773A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor W773A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
8946 2144 None 42 Human Binding pEC50 = 5.6 5.6 - 1
Positive allosteric modulation at human mGlu2 receptor W773A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor W773A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
CHEMBL3337527 2144 None 42 Human Binding pEC50 = 5.6 5.6 - 1
Positive allosteric modulation at human mGlu2 receptor W773A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor W773A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
DB12059 2144 None 42 Human Binding pEC50 = 5.6 5.6 - 1
Positive allosteric modulation at human mGlu2 receptor W773A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor W773A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
90643891 111915 None 0 Rat Binding pEC50 = 5.6 5.6 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 424 11 1 4 6.0 Cc1c(OCCCCOc2ccccc2C(=O)O)ccc(C(=O)CC2CCCC2)c1C 10.1021/jm5000563
CHEMBL3287678 111915 None 0 Rat Binding pEC50 = 5.6 5.6 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 424 11 1 4 6.0 Cc1c(OCCCCOc2ccccc2C(=O)O)ccc(C(=O)CC2CCCC2)c1C 10.1021/jm5000563
90643898 111940 None 0 Rat Binding pEC50 = 6.6 6.6 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 376 9 2 5 4.0 CC(=O)c1ccc(OCCCCOc2ccc(F)c(C(=O)O)c2)c(C)c1O 10.1021/jm5000563
CHEMBL3287706 111940 None 0 Rat Binding pEC50 = 6.6 6.6 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 376 9 2 5 4.0 CC(=O)c1ccc(OCCCCOc2ccc(F)c(C(=O)O)c2)c(C)c1O 10.1021/jm5000563
44578946 181708 None 0 Rat Binding pEC50 = 7.6 7.6 - 0
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 375 6 0 4 4.5 CC(C)c1ccc(OCC2[C@H]3CN(Cc4nc5ccccc5n4C)C[C@@H]23)cc1 10.1016/j.bmcl.2008.09.026
CHEMBL477169 181708 None 0 Rat Binding pEC50 = 7.6 7.6 - 0
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 375 6 0 4 4.5 CC(C)c1ccc(OCC2[C@H]3CN(Cc4nc5ccccc5n4C)C[C@@H]23)cc1 10.1016/j.bmcl.2008.09.026
44578947 181709 None 0 Rat Binding pEC50 = 7.6 7.6 - 0
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 367 5 0 4 4.0 Cn1c(CN2C[C@@H]3C(COc4ccc(Cl)cc4)[C@@H]3C2)nc2ccccc21 10.1016/j.bmcl.2008.09.026
CHEMBL477170 181709 None 0 Rat Binding pEC50 = 7.6 7.6 - 0
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 367 5 0 4 4.0 Cn1c(CN2C[C@@H]3C(COc4ccc(Cl)cc4)[C@@H]3C2)nc2ccccc21 10.1016/j.bmcl.2008.09.026
25110722 189646 None 0 Rat Binding pEC50 = 7.6 7.6 - 0
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 368 5 0 5 3.4 Cn1c(CN2C[C@@H]3C(COc4ccc(Cl)cn4)[C@@H]3C2)nc2ccccc21 10.1016/j.bmcl.2008.09.026
CHEMBL514218 189646 None 0 Rat Binding pEC50 = 7.6 7.6 - 0
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 368 5 0 5 3.4 Cn1c(CN2C[C@@H]3C(COc4ccc(Cl)cn4)[C@@H]3C2)nc2ccccc21 10.1016/j.bmcl.2008.09.026
68108294 147375 None 0 Human Binding pEC50 = 7.6 7.6 - 0
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 444 6 0 5 4.8 COC1(c2ccccc2)CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1 10.1021/acs.jmedchem.6b00913
CHEMBL3928875 147375 None 0 Human Binding pEC50 = 7.6 7.6 - 0
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 444 6 0 5 4.8 COC1(c2ccccc2)CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1 10.1021/acs.jmedchem.6b00913
68108567 153842 None 0 Human Binding pEC50 = 7.6 7.6 - 0
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 451 5 0 5 4.3 Fc1cccc(F)c1N1CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1 10.1021/acs.jmedchem.6b00913
CHEMBL3981882 153842 None 0 Human Binding pEC50 = 7.6 7.6 - 0
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 451 5 0 5 4.3 Fc1cccc(F)c1N1CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1 10.1021/acs.jmedchem.6b00913
89735130 138037 None 0 Human Binding pEC50 = 7.6 7.6 - 0
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 320 2 0 5 3.3 Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccccc3C#N)nc21 10.1016/j.bmcl.2016.01.021
CHEMBL3764057 138037 None 0 Human Binding pEC50 = 7.6 7.6 - 0
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 320 2 0 5 3.3 Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccccc3C#N)nc21 10.1016/j.bmcl.2016.01.021
71128768 144668 None 0 Human Binding pEC50 = 7.6 7.6 - 0
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 441 4 0 7 2.7 Cn1c(=O)n(CC2CC2(F)F)c2ccc(C3=CC4CCC3CN4C(=O)c3ccon3)nc21 nan
CHEMBL3907644 144668 None 0 Human Binding pEC50 = 7.6 7.6 - 0
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 441 4 0 7 2.7 Cn1c(=O)n(CC2CC2(F)F)c2ccc(C3=CC4CCC3CN4C(=O)c3ccon3)nc21 nan
50993968 57349 None 0 Rat Binding pEC50 = 6.6 6.6 - 0
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 469 6 1 3 6.4 O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(c3ccccc3)C4=O)c2)ccc1Cl 10.1021/jm1012165
CHEMBL1651214 57349 None 0 Rat Binding pEC50 = 6.6 6.6 - 0
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 469 6 1 3 6.4 O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(c3ccccc3)C4=O)c2)ccc1Cl 10.1021/jm1012165
164619502 186306 None 0 Rat Binding pEC50 = 6.6 6.6 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 432 9 2 5 5.3 Cc1c(OC[C@@H](C)COc2ccc(C(=O)O)c(F)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
CHEMBL4872955 186306 None 0 Rat Binding pEC50 = 6.6 6.6 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 432 9 2 5 5.3 Cc1c(OC[C@@H](C)COc2ccc(C(=O)O)c(F)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
25195461 2144 None 42 Human Binding pEC50 = 6.6 6.6 - 1
Positive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
8946 2144 None 42 Human Binding pEC50 = 6.6 6.6 - 1
Positive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
CHEMBL3337527 2144 None 42 Human Binding pEC50 = 6.6 6.6 - 1
Positive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
DB12059 2144 None 42 Human Binding pEC50 = 6.6 6.6 - 1
Positive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F776A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
44335577 5884 None 1 Human Binding pEC50 = 7.6 7.6 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 402 8 0 4 4.0 CC(C)COc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1 10.1016/j.bmcl.2004.04.017
CHEMBL107948 5884 None 1 Human Binding pEC50 = 7.6 7.6 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 402 8 0 4 4.0 CC(C)COc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1 10.1016/j.bmcl.2004.04.017
49765871 2145 None 41 Human Binding pEC50 = 7.6 7.6 - 1
Positive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.6b00913
6317 2145 None 41 Human Binding pEC50 = 7.6 7.6 - 1
Positive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.6b00913
CHEMBL2179319 2145 None 41 Human Binding pEC50 = 7.6 7.6 - 1
Positive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor N735D mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.6b00913
11677757 66122 None 0 Human Binding pEC50 = 6.6 6.6 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 500 8 1 6 6.0 CC1(C2CCCC2)Cc2cc(OCCCOc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
CHEMBL183911 66122 None 0 Human Binding pEC50 = 6.6 6.6 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 500 8 1 6 6.0 CC1(C2CCCC2)Cc2cc(OCCCOc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
1402 122 None 35 Human Binding pEC50 = 6.6 6.6 - 0
Effective concentration against Metabotropic glutamate receptor 2Effective concentration against Metabotropic glutamate receptor 2
ChEMBL 452 8 0 5 4.8 COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 10.1021/jm034015u
9825084 122 None 35 Human Binding pEC50 = 6.6 6.6 - 0
Effective concentration against Metabotropic glutamate receptor 2Effective concentration against Metabotropic glutamate receptor 2
ChEMBL 452 8 0 5 4.8 COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 10.1021/jm034015u
CHEMBL108939 122 None 35 Human Binding pEC50 = 6.6 6.6 - 0
Effective concentration against Metabotropic glutamate receptor 2Effective concentration against Metabotropic glutamate receptor 2
ChEMBL 452 8 0 5 4.8 COc1ccccc1Oc1ccc(cc1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1 10.1021/jm034015u
50994049 57350 None 0 Rat Binding pEC50 = 6.6 6.6 - 0
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 475 6 1 3 6.6 O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(C3CCCCC3)C4=O)c2)ccc1Cl 10.1021/jm1012165
CHEMBL1651215 57350 None 0 Rat Binding pEC50 = 6.6 6.6 - 0
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 475 6 1 3 6.6 O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(C3CCCCC3)C4=O)c2)ccc1Cl 10.1021/jm1012165
11598292 130243 None 0 Human Binding pEC50 = 6.6 6.6 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 486 7 1 6 5.6 CC1(C2CCCC2)Cc2cc(OCCOc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
CHEMBL367823 130243 None 0 Human Binding pEC50 = 6.6 6.6 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 486 7 1 6 5.6 CC1(C2CCCC2)Cc2cc(OCCOc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
164611777 185031 None 0 Rat Binding pEC50 = 7.6 7.6 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 444 10 2 6 5.1 COc1cc(C(=O)O)ccc1OC[C@H](C)COc1ccc(C(=O)CC(C)(C)C)c(O)c1C 10.1016/j.bmcl.2021.128342
CHEMBL4853369 185031 None 0 Rat Binding pEC50 = 7.6 7.6 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 444 10 2 6 5.1 COc1cc(C(=O)O)ccc1OC[C@H](C)COc1ccc(C(=O)CC(C)(C)C)c(O)c1C 10.1016/j.bmcl.2021.128342
164621310 185671 None 0 Rat Binding pEC50 = 7.6 7.6 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 429 10 2 6 5.0 Cc1ncc(OCCCCOc2ccc(C(=O)CC(C)(C)C)c(O)c2C)cc1C(=O)O 10.1016/j.bmcl.2021.128342
CHEMBL4863303 185671 None 0 Rat Binding pEC50 = 7.6 7.6 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 429 10 2 6 5.0 Cc1ncc(OCCCCOc2ccc(C(=O)CC(C)(C)C)c(O)c2C)cc1C(=O)O 10.1016/j.bmcl.2021.128342
11344646 126844 None 0 Human Binding pEC50 = 7.5 7.5 -1 2
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 199 2 3 3 -0.2 C[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/jm4000165
CHEMBL365368 126844 None 0 Human Binding pEC50 = 7.5 7.5 -1 2
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 199 2 3 3 -0.2 C[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/jm4000165
162650303 183754 None 0 Rat Binding pEC50 = 6.6 6.6 - 0
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1064 22 6 12 8.6 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
CHEMBL4748549 183754 None 0 Rat Binding pEC50 = 6.6 6.6 - 0
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1064 22 6 12 8.6 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
CHEMBL4802664 183754 None 0 Rat Binding pEC50 = 6.6 6.6 - 0
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1064 22 6 12 8.6 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
11625861 65881 None 0 Human Binding pEC50 = 6.6 6.6 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 416 6 1 5 4.9 CCCC1Cc2cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
CHEMBL183541 65881 None 0 Human Binding pEC50 = 6.6 6.6 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 416 6 1 5 4.9 CCCC1Cc2cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
71136188 145843 None 0 Human Binding pEC50 = 5.6 5.6 - 0
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 384 3 1 6 1.6 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)CO)CC4C3)nc21 nan
CHEMBL3916627 145843 None 0 Human Binding pEC50 = 5.6 5.6 - 0
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 384 3 1 6 1.6 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)CO)CC4C3)nc21 nan
44335626 5396 None 0 Human Binding pEC50 = 7.5 7.5 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 428 7 0 4 4.7 O=S(=O)(CC(F)(F)F)N(Cc1cccnc1)c1cccc(OC2CCCCC2)c1 10.1016/j.bmcl.2004.04.017
CHEMBL107114 5396 None 0 Human Binding pEC50 = 7.5 7.5 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 428 7 0 4 4.7 O=S(=O)(CC(F)(F)F)N(Cc1cccnc1)c1cccc(OC2CCCCC2)c1 10.1016/j.bmcl.2004.04.017
51036108 140314 None 0 Human Binding pEC50 = 7.5 7.5 - 0
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 441 3 0 9 2.1 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3C[C@@H]4CC[C@H]3CN4C(=O)c3csnn3)nc21 10.1021/acsmedchemlett.5b00459
CHEMBL3805203 140314 None 0 Human Binding pEC50 = 7.5 7.5 - 0
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 441 3 0 9 2.1 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3C[C@@H]4CC[C@H]3CN4C(=O)c3csnn3)nc21 10.1021/acsmedchemlett.5b00459
127052897 140395 None 0 Human Binding pEC50 = 7.5 7.5 - 0
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 424 3 0 8 2.3 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3C[C@@H]4CC[C@H]3CN4C(=O)c3ccon3)nc21 10.1021/acsmedchemlett.5b00459
CHEMBL3806137 140395 None 0 Human Binding pEC50 = 7.5 7.5 - 0
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 424 3 0 8 2.3 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3C[C@@H]4CC[C@H]3CN4C(=O)c3ccon3)nc21 10.1021/acsmedchemlett.5b00459
1310 2315 None 61 Human Binding pEC50 = 6.5 6.5 -22 18
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm970719q
1369 2315 None 61 Human Binding pEC50 = 6.5 6.5 -22 18
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm970719q
33032 2315 None 61 Human Binding pEC50 = 6.5 6.5 -22 18
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm970719q
44272391 2315 None 61 Human Binding pEC50 = 6.5 6.5 -22 18
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm970719q
88747398 2315 None 61 Human Binding pEC50 = 6.5 6.5 -22 18
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm970719q
CHEMBL575060 2315 None 61 Human Binding pEC50 = 6.5 6.5 -22 18
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm970719q
DB00142 2315 None 61 Human Binding pEC50 = 6.5 6.5 -22 18
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm970719q
11697718 64203 None 0 Human Binding pEC50 = 6.5 6.5 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 431 8 0 4 6.7 CCCC1Cc2cc(OCc3cccc(CSc4ccncc4)c3)c(C)c(C)c2C1=O 10.1016/j.bmcl.2005.01.077
CHEMBL180871 64203 None 0 Human Binding pEC50 = 6.5 6.5 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 431 8 0 4 6.7 CCCC1Cc2cc(OCc3cccc(CSc4ccncc4)c3)c(C)c(C)c2C1=O 10.1016/j.bmcl.2005.01.077
164624801 186317 None 0 Rat Binding pEC50 = 6.5 6.5 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 432 9 2 5 5.3 Cc1c(OC[C@H](C)COc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
CHEMBL4873125 186317 None 0 Rat Binding pEC50 = 6.5 6.5 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 432 9 2 5 5.3 Cc1c(OC[C@H](C)COc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
71136186 152158 None 0 Human Binding pEC50 = 6.5 6.5 - 0
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 431 3 0 6 3.5 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3cccnc3)nc21 nan
CHEMBL3967432 152158 None 0 Human Binding pEC50 = 6.5 6.5 - 0
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 431 3 0 6 3.5 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3cccnc3)nc21 nan
25110723 189748 None 0 Rat Binding pEC50 = 7.5 7.5 - 0
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 402 5 0 5 3.7 Cn1c(CN2C[C@@H]3C(COc4ccc(C(F)(F)F)cn4)[C@@H]3C2)nc2ccccc21 10.1016/j.bmcl.2008.09.026
CHEMBL515034 189748 None 0 Rat Binding pEC50 = 7.5 7.5 - 0
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 402 5 0 5 3.7 Cn1c(CN2C[C@@H]3C(COc4ccc(C(F)(F)F)cn4)[C@@H]3C2)nc2ccccc21 10.1016/j.bmcl.2008.09.026
1377 1340 None 23 Rat Binding pEC50 = 6.5 6.5 -1 6
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 203 4 4 4 -1.6 N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O 10.1021/jm00009a001
5310979 1340 None 23 Rat Binding pEC50 = 6.5 6.5 -1 6
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 203 4 4 4 -1.6 N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O 10.1021/jm00009a001
CHEMBL284193 1340 None 23 Rat Binding pEC50 = 6.5 6.5 -1 6
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 203 4 4 4 -1.6 N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O 10.1021/jm00009a001
50994823 57354 None 0 Rat Binding pEC50 = 6.5 6.5 - 0
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 475 6 1 3 6.2 O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CCN(C3CCCC3)C4=O)c2)ccc1Cl 10.1021/jm1012165
CHEMBL1651221 57354 None 0 Rat Binding pEC50 = 6.5 6.5 - 0
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 475 6 1 3 6.2 O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CCN(C3CCCC3)C4=O)c2)ccc1Cl 10.1021/jm1012165
44578996 181691 None 0 Rat Binding pEC50 = 5.5 5.5 - 0
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 359 6 0 4 4.1 c1ccc(OCC2[C@H]3CN(Cc4nc5ccccc5n4C4CC4)C[C@@H]23)cc1 10.1016/j.bmcl.2008.09.026
CHEMBL476965 181691 None 0 Rat Binding pEC50 = 5.5 5.5 - 0
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 359 6 0 4 4.1 c1ccc(OCC2[C@H]3CN(Cc4nc5ccccc5n4C4CC4)C[C@@H]23)cc1 10.1016/j.bmcl.2008.09.026
10251009 66802 None 0 Human Binding pEC50 = 6.5 6.5 - 0
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 410 11 2 7 4.1 CCCC(=O)c1ccc(OCCCCOc2ccc(-c3nn[nH]n3)cc2)c(C)c1O 10.1016/j.bmcl.2004.08.020
CHEMBL185911 66802 None 0 Human Binding pEC50 = 6.5 6.5 - 0
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 410 11 2 7 4.1 CCCC(=O)c1ccc(OCCCCOc2ccc(-c3nn[nH]n3)cc2)c(C)c1O 10.1016/j.bmcl.2004.08.020
164611874 185220 None 0 Rat Binding pEC50 = 6.5 6.5 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 428 9 2 5 5.4 Cc1cc(OC[C@H](C)COc2ccc(C(=O)CC(C)(C)C)c(O)c2C)ccc1C(=O)O 10.1016/j.bmcl.2021.128342
CHEMBL4856242 185220 None 0 Rat Binding pEC50 = 6.5 6.5 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 428 9 2 5 5.4 Cc1cc(OC[C@H](C)COc2ccc(C(=O)CC(C)(C)C)c(O)c2C)ccc1C(=O)O 10.1016/j.bmcl.2021.128342
56651050 138045 None 0 Human Binding pEC50 = 7.5 7.5 - 0
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 294 2 0 3 4.1 Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccccc3)cc21 10.1016/j.bmcl.2016.01.021
CHEMBL3764108 138045 None 0 Human Binding pEC50 = 7.5 7.5 - 0
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 294 2 0 3 4.1 Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccccc3)cc21 10.1016/j.bmcl.2016.01.021
44335670 4965 None 0 Human Binding pEC50 = 6.5 6.5 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 366 7 0 3 4.0 CCS(=O)(=O)N(Cc1cccnc1)c1cccc(Cc2ccccc2)c1 10.1016/j.bmcl.2004.04.017
CHEMBL104818 4965 None 0 Human Binding pEC50 = 6.5 6.5 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 366 7 0 3 4.0 CCS(=O)(=O)N(Cc1cccnc1)c1cccc(Cc2ccccc2)c1 10.1016/j.bmcl.2004.04.017
50994757 57353 None 0 Rat Binding pEC50 = 6.5 6.5 - 0
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 463 6 1 5 6.3 O=C(O)c1cc(-c2cccc(COc3ccc4c(=O)n(C5CCCC5)oc4c3)c2)ccc1Cl 10.1021/jm1012165
CHEMBL1651220 57353 None 0 Rat Binding pEC50 = 6.5 6.5 - 0
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 463 6 1 5 6.3 O=C(O)c1cc(-c2cccc(COc3ccc4c(=O)n(C5CCCC5)oc4c3)c2)ccc1Cl 10.1021/jm1012165
89735684 138113 None 0 Human Binding pEC50 = 6.5 6.5 - 0
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 309 2 0 4 3.8 Cc1ccc(-c2ccc3c(n2)n(C)c(=O)n3CC(C)(C)C)cc1 10.1016/j.bmcl.2016.01.021
CHEMBL3764850 138113 None 0 Human Binding pEC50 = 6.5 6.5 - 0
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 309 2 0 4 3.8 Cc1ccc(-c2ccc3c(n2)n(C)c(=O)n3CC(C)(C)C)cc1 10.1016/j.bmcl.2016.01.021
46225336 202504 None 0 Human Binding pEC50 = 6.5 6.5 - 1
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 363 3 0 6 3.5 Cn1c(CN2CCN(c3nc4ccccc4s3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL595609 202504 None 0 Human Binding pEC50 = 6.5 6.5 - 1
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 363 3 0 6 3.5 Cn1c(CN2CCN(c3nc4ccccc4s3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
46225320 203640 None 0 Human Binding pEC50 = 6.5 6.5 - 1
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 374 3 0 4 3.9 Cn1c(CN2CCN(c3ccccc3C(F)(F)F)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL603443 203640 None 0 Human Binding pEC50 = 6.5 6.5 - 1
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 374 3 0 4 3.9 Cn1c(CN2CCN(c3ccccc3C(F)(F)F)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
46225569 203819 None 0 Human Binding pEC50 = 6.5 6.5 - 1
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 373 3 0 3 5.0 Cn1c(CN2CCC(c3ccccc3C(F)(F)F)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL604467 203819 None 0 Human Binding pEC50 = 6.5 6.5 - 1
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 373 3 0 3 5.0 Cn1c(CN2CCC(c3ccccc3C(F)(F)F)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
44335573 4826 None 0 Human Binding pEC50 = 7.5 7.5 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 388 7 0 4 3.8 CC(C)Oc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1 10.1016/j.bmcl.2004.04.017
CHEMBL104190 4826 None 0 Human Binding pEC50 = 7.5 7.5 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 388 7 0 4 3.8 CC(C)Oc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1 10.1016/j.bmcl.2004.04.017
10846649 101285 None 2 Human Binding pEC50 = 6.5 6.5 - 0
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
ChEMBL 185 2 3 3 -0.5 N[C@@]1(C(=O)O)C[C@@H]2C[C@H]1[C@H]2C(=O)O 10.1021/jm970719q
CHEMBL296054 101285 None 2 Human Binding pEC50 = 6.5 6.5 - 0
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
ChEMBL 185 2 3 3 -0.5 N[C@@]1(C(=O)O)C[C@@H]2C[C@H]1[C@H]2C(=O)O 10.1021/jm970719q
11743092 64611 None 0 Human Binding pEC50 = 5.5 5.5 - 0
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 424 12 2 7 4.4 CCCc1c(OCCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2004.08.020
CHEMBL181648 64611 None 0 Human Binding pEC50 = 5.5 5.5 - 0
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 424 12 2 7 4.4 CCCc1c(OCCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2004.08.020
51036916 140400 None 0 Human Binding pEC50 = 6.5 6.5 - 0
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 350 2 0 5 3.9 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CCCc4ccccc43)nc21 10.1021/acsmedchemlett.5b00459
CHEMBL3806176 140400 None 0 Human Binding pEC50 = 6.5 6.5 - 0
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 350 2 0 5 3.9 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CCCc4ccccc43)nc21 10.1021/acsmedchemlett.5b00459
90643893 111917 None 0 Rat Binding pEC50 = 6.5 6.5 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 426 11 2 5 5.4 Cc1c(OCCCCOc2ccccc2C(=O)O)ccc(C(=O)CC2CCCC2)c1O 10.1021/jm5000563
CHEMBL3287680 111917 None 0 Rat Binding pEC50 = 6.5 6.5 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 426 11 2 5 5.4 Cc1c(OCCCCOc2ccccc2C(=O)O)ccc(C(=O)CC2CCCC2)c1O 10.1021/jm5000563
9999945 67159 None 0 Human Binding pEC50 = 5.5 5.5 - 0
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 382 9 2 7 3.3 CC(=O)c1ccc(OCCCCOc2ccc(-c3nn[nH]n3)cc2)c(C)c1O 10.1016/j.bmcl.2004.08.020
CHEMBL187537 67159 None 0 Human Binding pEC50 = 5.5 5.5 - 0
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 382 9 2 7 3.3 CC(=O)c1ccc(OCCCCOc2ccc(-c3nn[nH]n3)cc2)c(C)c1O 10.1016/j.bmcl.2004.08.020
90643883 111952 None 0 Rat Binding pEC50 = 7.5 7.5 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 416 12 2 6 4.6 CCCC(=O)c1ccc(OCCCCOc2c(OC)cccc2C(=O)O)c(C)c1O 10.1021/jm5000563
CHEMBL3287718 111952 None 0 Rat Binding pEC50 = 7.5 7.5 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 416 12 2 6 4.6 CCCC(=O)c1ccc(OCCCCOc2c(OC)cccc2C(=O)O)c(C)c1O 10.1021/jm5000563
10047169 3224 None 0 Human Binding pEC50 = 6.5 6.5 - 0
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 410 11 2 7 4.0 CCCc1c(OCCCCOc2ccc(cc2)c2n[nH]nn2)ccc(c1O)C(=O)C 10.1016/j.bmcl.2004.08.020
1403 3224 None 0 Human Binding pEC50 = 6.5 6.5 - 0
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 410 11 2 7 4.0 CCCc1c(OCCCCOc2ccc(cc2)c2n[nH]nn2)ccc(c1O)C(=O)C 10.1016/j.bmcl.2004.08.020
CHEMBL182371 3224 None 0 Human Binding pEC50 = 6.5 6.5 - 0
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 410 11 2 7 4.0 CCCc1c(OCCCCOc2ccc(cc2)c2n[nH]nn2)ccc(c1O)C(=O)C 10.1016/j.bmcl.2004.08.020
1377 1340 None 23 Rat Binding pEC50 = 6.5 6.5 -1 6
Agonist activity at rat mGlu2 receptor by FRET based mGlu sensor assayAgonist activity at rat mGlu2 receptor by FRET based mGlu sensor assay
ChEMBL 203 4 4 4 -1.6 N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O 10.1021/acs.jmedchem.5b01333
5310979 1340 None 23 Rat Binding pEC50 = 6.5 6.5 -1 6
Agonist activity at rat mGlu2 receptor by FRET based mGlu sensor assayAgonist activity at rat mGlu2 receptor by FRET based mGlu sensor assay
ChEMBL 203 4 4 4 -1.6 N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O 10.1021/acs.jmedchem.5b01333
CHEMBL284193 1340 None 23 Rat Binding pEC50 = 6.5 6.5 -1 6
Agonist activity at rat mGlu2 receptor by FRET based mGlu sensor assayAgonist activity at rat mGlu2 receptor by FRET based mGlu sensor assay
ChEMBL 203 4 4 4 -1.6 N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O 10.1021/acs.jmedchem.5b01333
53321382 57351 None 0 Rat Binding pEC50 = 6.5 6.5 - 0
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 551 7 1 3 7.5 O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(Cc3ccc(C(F)(F)F)cc3)C4=O)c2)ccc1Cl 10.1021/jm1012165
CHEMBL1651216 57351 None 0 Rat Binding pEC50 = 6.5 6.5 - 0
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 551 7 1 3 7.5 O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(Cc3ccc(C(F)(F)F)cc3)C4=O)c2)ccc1Cl 10.1021/jm1012165
59066632 209028 None 52 Rat Binding pEC50 = 4.5 4.5 - 1
Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2
ChEMBL 161 5 3 3 -0.3 N[C@@H](CCCC(=O)O)C(=O)O 10.1021/jm020122x
92136 209028 None 52 Rat Binding pEC50 = 4.5 4.5 - 1
Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2
ChEMBL 161 5 3 3 -0.3 N[C@@H](CCCC(=O)O)C(=O)O 10.1021/jm020122x
CHEMBL88804 209028 None 52 Rat Binding pEC50 = 4.5 4.5 - 1
Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2
ChEMBL 161 5 3 3 -0.3 N[C@@H](CCCC(=O)O)C(=O)O 10.1021/jm020122x
6603885 102256 None 18 Rat Binding pEC50 = 4.5 4.5 - 0
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 158 2 3 5 -0.5 N[C@H](C(=O)O)c1cc(O)no1 10.1021/jm00009a001
6971208 102256 None 18 Rat Binding pEC50 = 4.5 4.5 - 0
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 158 2 3 5 -0.5 N[C@H](C(=O)O)c1cc(O)no1 10.1021/jm00009a001
CHEMBL30285 102256 None 18 Rat Binding pEC50 = 4.5 4.5 - 0
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 158 2 3 5 -0.5 N[C@H](C(=O)O)c1cc(O)no1 10.1021/jm00009a001
59066632 209028 None 52 Rat Binding pEC50 = 4.5 4.5 - 1
Effect on Metabotropic glutamate receptor 2Effect on Metabotropic glutamate receptor 2
ChEMBL 161 5 3 3 -0.3 N[C@@H](CCCC(=O)O)C(=O)O 10.1021/jm9703597
92136 209028 None 52 Rat Binding pEC50 = 4.5 4.5 - 1
Effect on Metabotropic glutamate receptor 2Effect on Metabotropic glutamate receptor 2
ChEMBL 161 5 3 3 -0.3 N[C@@H](CCCC(=O)O)C(=O)O 10.1021/jm9703597
CHEMBL88804 209028 None 52 Rat Binding pEC50 = 4.5 4.5 - 1
Effect on Metabotropic glutamate receptor 2Effect on Metabotropic glutamate receptor 2
ChEMBL 161 5 3 3 -0.3 N[C@@H](CCCC(=O)O)C(=O)O 10.1021/jm9703597
23521697 5029 None 0 Human Binding pEC50 = 7.4 7.4 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 400 7 0 4 3.9 O=S(=O)(CC(F)(F)F)N(Cc1cccnc1)c1cccc(OC2CCC2)c1 10.1016/j.bmcl.2004.04.017
CHEMBL105151 5029 None 0 Human Binding pEC50 = 7.4 7.4 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 400 7 0 4 3.9 O=S(=O)(CC(F)(F)F)N(Cc1cccnc1)c1cccc(OC2CCC2)c1 10.1016/j.bmcl.2004.04.017
69930179 140359 None 0 Human Binding pEC50 = 7.4 7.4 - 0
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 433 3 0 6 3.3 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CC4CCC3CN4C(=O)c3ccccc3)nc21 10.1021/acsmedchemlett.5b00459
CHEMBL3805718 140359 None 0 Human Binding pEC50 = 7.4 7.4 - 0
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 433 3 0 6 3.3 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CC4CCC3CN4C(=O)c3ccccc3)nc21 10.1021/acsmedchemlett.5b00459
23521709 164560 None 0 Human Binding pEC50 = 6.4 6.4 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 368 7 0 4 4.2 CCS(=O)(=O)N(Cc1cccnc1)c1cccc(Oc2ccccc2)c1 10.1016/j.bmcl.2004.04.017
CHEMBL421406 164560 None 0 Human Binding pEC50 = 6.4 6.4 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 368 7 0 4 4.2 CCS(=O)(=O)N(Cc1cccnc1)c1cccc(Oc2ccccc2)c1 10.1016/j.bmcl.2004.04.017
44404948 70578 None 0 Rat Binding pEC50 = 4.4 4.4 - 1
Effective concentration against mGluR2 receptor expressed in CHO cellsEffective concentration against mGluR2 receptor expressed in CHO cells
ChEMBL 214 2 3 5 -1.0 NC1(C(=O)O)CC2ON=C(C(=O)O)C2C1 10.1021/jm0504499
CHEMBL194787 70578 None 0 Rat Binding pEC50 = 4.4 4.4 - 1
Effective concentration against mGluR2 receptor expressed in CHO cellsEffective concentration against mGluR2 receptor expressed in CHO cells
ChEMBL 214 2 3 5 -1.0 NC1(C(=O)O)CC2ON=C(C(=O)O)C2C1 10.1021/jm0504499
69929785 140282 None 0 Human Binding pEC50 = 7.4 7.4 - 0
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 407 3 0 8 2.4 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CC4CCC3CN4c3ncccn3)nc21 10.1021/acsmedchemlett.5b00459
CHEMBL3804845 140282 None 0 Human Binding pEC50 = 7.4 7.4 - 0
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 407 3 0 8 2.4 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CC4CCC3CN4c3ncccn3)nc21 10.1021/acsmedchemlett.5b00459
9837114 115329 None 0 Human Binding pEC50 = 4.4 4.4 - 0
Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells
ChEMBL 203 4 3 6 -0.4 N[C@H](CCc1nsnc1O)C(=O)O 10.1039/C1MD00186H
CHEMBL334842 115329 None 0 Human Binding pEC50 = 4.4 4.4 - 0
Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells
ChEMBL 203 4 3 6 -0.4 N[C@H](CCc1nsnc1O)C(=O)O 10.1039/C1MD00186H
9837114 115329 None 0 Rat Binding pEC50 = 4.4 4.4 - 0
Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2
ChEMBL 203 4 3 6 -0.4 N[C@H](CCc1nsnc1O)C(=O)O 10.1021/jm020122x
CHEMBL334842 115329 None 0 Rat Binding pEC50 = 4.4 4.4 - 0
Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2
ChEMBL 203 4 3 6 -0.4 N[C@H](CCc1nsnc1O)C(=O)O 10.1021/jm020122x
11691077 64715 None 0 Human Binding pEC50 = 6.4 6.4 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 456 5 1 5 5.7 CC1(C2CCCC2)Cc2cc(OCc3cccc(-c4nn[nH]n4)c3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
CHEMBL181869 64715 None 0 Human Binding pEC50 = 6.4 6.4 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 456 5 1 5 5.7 CC1(C2CCCC2)Cc2cc(OCc3cccc(-c4nn[nH]n4)c3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
164624284 186135 None 0 Rat Binding pEC50 = 6.4 6.4 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 448 9 2 5 5.8 Cc1c(OC[C@@H](C)COc2ccc(Cl)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
CHEMBL4870631 186135 None 0 Rat Binding pEC50 = 6.4 6.4 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 448 9 2 5 5.8 Cc1c(OC[C@@H](C)COc2ccc(Cl)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
54761055 137974 None 0 Human Binding pEC50 = 6.4 6.4 - 0
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 373 3 0 6 2.9 Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccc(S(C)(=O)=O)cc3)nc21 10.1016/j.bmcl.2016.01.021
CHEMBL3763172 137974 None 0 Human Binding pEC50 = 6.4 6.4 - 0
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 373 3 0 6 2.9 Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccc(S(C)(=O)=O)cc3)nc21 10.1016/j.bmcl.2016.01.021
69092138 142882 None 0 Human Binding pEC50 = 7.4 7.4 - 0
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 464 6 1 4 5.8 Fc1ccc([C@H]2CC[C@@H](NCc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
CHEMBL3892865 142882 None 0 Human Binding pEC50 = 7.4 7.4 - 0
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 464 6 1 4 5.8 Fc1ccc([C@H]2CC[C@@H](NCc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
1368 2290 None 30 Human Binding pEC50 = 6.4 6.4 -3 11
Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human
ChEMBL 159 3 3 3 -0.9 N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O 10.1021/jm00009a001
5310956 2290 None 30 Human Binding pEC50 = 6.4 6.4 -3 11
Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human
ChEMBL 159 3 3 3 -0.9 N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O 10.1021/jm00009a001
CHEMBL280563 2290 None 30 Human Binding pEC50 = 6.4 6.4 -3 11
Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human
ChEMBL 159 3 3 3 -0.9 N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O 10.1021/jm00009a001
10318576 66734 None 0 Human Binding pEC50 = 6.4 6.4 - 0
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 396 10 2 7 3.7 CCC(=O)c1ccc(OCCCCOc2ccc(-c3nn[nH]n3)cc2)c(C)c1O 10.1016/j.bmcl.2004.08.020
CHEMBL185602 66734 None 0 Human Binding pEC50 = 6.4 6.4 - 0
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 396 10 2 7 3.7 CCC(=O)c1ccc(OCCCCOc2ccc(-c3nn[nH]n3)cc2)c(C)c1O 10.1016/j.bmcl.2004.08.020
3954 664 None 44 Rat Binding pEC50 = 6.4 6.4 - 2
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 454 6 1 3 6.8 Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1 10.1021/jm3005306
9868580 664 None 44 Rat Binding pEC50 = 6.4 6.4 - 2
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 454 6 1 3 6.8 Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1 10.1021/jm3005306
CHEMBL593013 664 None 44 Rat Binding pEC50 = 6.4 6.4 - 2
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 454 6 1 3 6.8 Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1 10.1021/jm3005306
3954 664 None 44 Rat Binding pEC50 = 6.4 6.4 - 2
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 454 6 1 3 6.8 Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1 10.1021/jm1012165
9868580 664 None 44 Rat Binding pEC50 = 6.4 6.4 - 2
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 454 6 1 3 6.8 Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1 10.1021/jm1012165
CHEMBL593013 664 None 44 Rat Binding pEC50 = 6.4 6.4 - 2
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 454 6 1 3 6.8 Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1 10.1021/jm1012165
10560963 164612 None 1 Human Binding pEC50 = 4.4 4.4 - 0
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
ChEMBL 185 2 3 3 -0.5 N[C@@]1(C(=O)O)C[C@@H]2C[C@H]1[C@@H]2C(=O)O 10.1021/jm970719q
CHEMBL42148 164612 None 1 Human Binding pEC50 = 4.4 4.4 - 0
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
ChEMBL 185 2 3 3 -0.5 N[C@@]1(C(=O)O)C[C@@H]2C[C@H]1[C@@H]2C(=O)O 10.1021/jm970719q
164610692 185008 None 0 Rat Binding pEC50 = 5.4 5.4 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 459 10 1 5 5.4 Cc1c(OCCCCOc2ccc(F)c(C(=O)N(C)C)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
CHEMBL4853089 185008 None 0 Rat Binding pEC50 = 5.4 5.4 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 459 10 1 5 5.4 Cc1c(OCCCCOc2ccc(F)c(C(=O)N(C)C)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
49765871 2145 None 41 Human Binding pEC50 = 6.4 6.4 - 1
Positive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.6b00913
6317 2145 None 41 Human Binding pEC50 = 6.4 6.4 - 1
Positive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.6b00913
CHEMBL2179319 2145 None 41 Human Binding pEC50 = 6.4 6.4 - 1
Positive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.6b00913
46225584 202131 None 0 Human Binding pEC50 = 7.4 7.4 - 3
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 408 3 0 4 5.0 Cn1c(CN2CCC(c3ncc(C(F)(F)F)cc3Cl)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL593056 202131 None 0 Human Binding pEC50 = 7.4 7.4 - 3
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 408 3 0 4 5.0 Cn1c(CN2CCC(c3ncc(C(F)(F)F)cc3Cl)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
49765871 2145 None 41 Human Binding pEC50 = 8.3 8.3 - 1
Positive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.6b00913
6317 2145 None 41 Human Binding pEC50 = 8.3 8.3 - 1
Positive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.6b00913
CHEMBL2179319 2145 None 41 Human Binding pEC50 = 8.3 8.3 - 1
Positive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.6b00913
90643858 111929 None 0 Rat Binding pEC50 = 7.4 7.4 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 430 12 2 6 4.9 COc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)CC(C)C)c(O)c1C 10.1021/jm5000563
CHEMBL3287695 111929 None 0 Rat Binding pEC50 = 7.4 7.4 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 430 12 2 6 4.9 COc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)CC(C)C)c(O)c1C 10.1021/jm5000563
71116701 144947 None 0 Human Binding pEC50 = 7.4 7.4 - 0
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 387 4 1 4 2.4 CC1C(c2ccc3c(n2)N(C)S(=O)(=O)N3CC2CC2(F)F)C1C(C)(C)O nan
CHEMBL3909811 144947 None 0 Human Binding pEC50 = 7.4 7.4 - 0
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 387 4 1 4 2.4 CC1C(c2ccc3c(n2)N(C)S(=O)(=O)N3CC2CC2(F)F)C1C(C)(C)O nan
1310 2315 None 61 Rat Binding pEC50 = 5.4 5.4 -13 18
Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm020122x
1369 2315 None 61 Rat Binding pEC50 = 5.4 5.4 -13 18
Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm020122x
33032 2315 None 61 Rat Binding pEC50 = 5.4 5.4 -13 18
Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm020122x
44272391 2315 None 61 Rat Binding pEC50 = 5.4 5.4 -13 18
Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm020122x
88747398 2315 None 61 Rat Binding pEC50 = 5.4 5.4 -13 18
Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm020122x
CHEMBL575060 2315 None 61 Rat Binding pEC50 = 5.4 5.4 -13 18
Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm020122x
DB00142 2315 None 61 Rat Binding pEC50 = 5.4 5.4 -13 18
Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm020122x
1310 2315 None 61 Rat Binding pEC50 = 5.4 5.4 -13 18
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm00009a001
1369 2315 None 61 Rat Binding pEC50 = 5.4 5.4 -13 18
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm00009a001
33032 2315 None 61 Rat Binding pEC50 = 5.4 5.4 -13 18
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm00009a001
44272391 2315 None 61 Rat Binding pEC50 = 5.4 5.4 -13 18
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm00009a001
88747398 2315 None 61 Rat Binding pEC50 = 5.4 5.4 -13 18
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm00009a001
CHEMBL575060 2315 None 61 Rat Binding pEC50 = 5.4 5.4 -13 18
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm00009a001
DB00142 2315 None 61 Rat Binding pEC50 = 5.4 5.4 -13 18
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm00009a001
139054390 207381 None 56 Rat Binding pEC50 = 5.4 5.4 -1 5
Effect on Metabotropic glutamate receptor 2Effect on Metabotropic glutamate receptor 2
ChEMBL 147 4 3 3 -0.7 N[C@H](CCC(=O)O)C(=O)O 10.1021/jm9703597
23327 207381 None 56 Rat Binding pEC50 = 5.4 5.4 -1 5
Effect on Metabotropic glutamate receptor 2Effect on Metabotropic glutamate receptor 2
ChEMBL 147 4 3 3 -0.7 N[C@H](CCC(=O)O)C(=O)O 10.1021/jm9703597
CHEMBL76232 207381 None 56 Rat Binding pEC50 = 5.4 5.4 -1 5
Effect on Metabotropic glutamate receptor 2Effect on Metabotropic glutamate receptor 2
ChEMBL 147 4 3 3 -0.7 N[C@H](CCC(=O)O)C(=O)O 10.1021/jm9703597
10465478 21792 None 0 Human Binding pEC50 = 4.4 4.4 - 0
Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells
ChEMBL 203 4 3 6 -0.4 N[C@@H](CCc1nsnc1O)C(=O)O 10.1039/C1MD00186H
CHEMBL131922 21792 None 0 Human Binding pEC50 = 4.4 4.4 - 0
Agonist activity at human mGluR2 receptor expressed in HEK cellsAgonist activity at human mGluR2 receptor expressed in HEK cells
ChEMBL 203 4 3 6 -0.4 N[C@@H](CCc1nsnc1O)C(=O)O 10.1039/C1MD00186H
10465478 21792 None 0 Rat Binding pEC50 = 4.4 4.4 - 0
Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2
ChEMBL 203 4 3 6 -0.4 N[C@@H](CCc1nsnc1O)C(=O)O 10.1021/jm020122x
CHEMBL131922 21792 None 0 Rat Binding pEC50 = 4.4 4.4 - 0
Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2Compound was evaluated for the inhibitory activity against cloned Metabotropic glutamate receptor 2
ChEMBL 203 4 3 6 -0.4 N[C@@H](CCc1nsnc1O)C(=O)O 10.1021/jm020122x
90643892 111916 None 0 Rat Binding pEC50 = 6.4 6.4 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 400 11 2 5 4.9 Cc1c(OCCCCOc2ccccc2C(=O)O)ccc(C(=O)CC(C)C)c1O 10.1021/jm5000563
CHEMBL3287679 111916 None 0 Rat Binding pEC50 = 6.4 6.4 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 400 11 2 5 4.9 Cc1c(OCCCCOc2ccccc2C(=O)O)ccc(C(=O)CC(C)C)c1O 10.1021/jm5000563
25050849 184348 None 0 Rat Binding pEC50 = 6.4 6.4 - 0
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 402 5 0 5 3.7 Cn1c(CN2C[C@@H]3C(COc4ccc(C(F)(F)F)cc4)[C@@H]3C2)nc2cccnc21 10.1016/j.bmcl.2008.09.026
CHEMBL483569 184348 None 0 Rat Binding pEC50 = 6.4 6.4 - 0
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 402 5 0 5 3.7 Cn1c(CN2C[C@@H]3C(COc4ccc(C(F)(F)F)cc4)[C@@H]3C2)nc2cccnc21 10.1016/j.bmcl.2008.09.026
23521725 5702 None 0 Human Binding pEC50 = 5.4 5.4 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 380 7 0 4 3.7 CCS(=O)(=O)N(Cc1cccnc1)c1ccc(C(=O)c2ccccc2)cc1 10.1016/j.bmcl.2004.04.017
CHEMBL107806 5702 None 0 Human Binding pEC50 = 5.4 5.4 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 380 7 0 4 3.7 CCS(=O)(=O)N(Cc1cccnc1)c1ccc(C(=O)c2ccccc2)cc1 10.1016/j.bmcl.2004.04.017
10026879 67050 None 0 Human Binding pEC50 = 6.4 6.4 - 0
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 452 13 2 7 5.0 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.08.020
CHEMBL187077 67050 None 0 Human Binding pEC50 = 6.4 6.4 - 0
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 452 13 2 7 5.0 CCCc1c(OCCCCOc2ccc(-c3nn[nH]n3)cc2)ccc(C(=O)CC(C)C)c1O 10.1016/j.bmcl.2004.08.020
90643879 111936 None 0 Rat Binding pEC50 = 6.4 6.4 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 456 12 2 6 5.4 COc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)CC2CCCC2)c(O)c1C 10.1021/jm5000563
CHEMBL3287702 111936 None 0 Rat Binding pEC50 = 6.4 6.4 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 456 12 2 6 5.4 COc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)CC2CCCC2)c(O)c1C 10.1021/jm5000563
51036701 140286 None 0 Human Binding pEC50 = 6.4 6.4 - 0
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 302 2 0 5 2.8 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CCCCC3)nc21 10.1021/acsmedchemlett.5b00459
CHEMBL3804903 140286 None 0 Human Binding pEC50 = 6.4 6.4 - 0
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 302 2 0 5 2.8 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3CCCCC3)nc21 10.1021/acsmedchemlett.5b00459
71116772 147757 None 0 Human Binding pEC50 = 7.4 7.4 - 0
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 456 4 1 8 3.7 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3CCC(C)(C)C(NC(=O)c4cnsn4)C3)nc21 nan
CHEMBL3931730 147757 None 0 Human Binding pEC50 = 7.4 7.4 - 0
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 456 4 1 8 3.7 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3CCC(C)(C)C(NC(=O)c4cnsn4)C3)nc21 nan
23521693 5357 None 0 Human Binding pEC50 = 6.4 6.4 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 382 8 0 4 4.0 CCS(=O)(=O)N(Cc1cccnc1)c1cccc(OCc2ccccc2)c1 10.1016/j.bmcl.2004.04.017
CHEMBL106909 5357 None 0 Human Binding pEC50 = 6.4 6.4 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 382 8 0 4 4.0 CCS(=O)(=O)N(Cc1cccnc1)c1cccc(OCc2ccccc2)c1 10.1016/j.bmcl.2004.04.017
11496550 63912 None 0 Human Binding pEC50 = 6.4 6.4 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 473 5 1 4 5.8 CC(=O)NC(=O)c1ccc(COc2cc3c(c(Cl)c2Cl)C(=O)C(C)(C2CCCC2)C3)cc1 10.1016/j.bmcl.2005.01.077
CHEMBL180455 63912 None 0 Human Binding pEC50 = 6.4 6.4 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 473 5 1 4 5.8 CC(=O)NC(=O)c1ccc(COc2cc3c(c(Cl)c2Cl)C(=O)C(C)(C2CCCC2)C3)cc1 10.1016/j.bmcl.2005.01.077
164615875 185550 None 0 Rat Binding pEC50 = 6.4 6.4 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 428 9 2 5 5.4 Cc1cc(C(=O)O)ccc1OC[C@H](C)COc1ccc(C(=O)CC(C)(C)C)c(O)c1C 10.1016/j.bmcl.2021.128342
CHEMBL4861618 185550 None 0 Rat Binding pEC50 = 6.4 6.4 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 428 9 2 5 5.4 Cc1cc(C(=O)O)ccc1OC[C@H](C)COc1ccc(C(=O)CC(C)(C)C)c(O)c1C 10.1016/j.bmcl.2021.128342
49822116 147080 None 14 Human Binding pEC50 = 7.3 7.3 - 1
Positive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 451 5 0 5 4.3 Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
CHEMBL3926416 147080 None 14 Human Binding pEC50 = 7.3 7.3 - 1
Positive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 451 5 0 5 4.3 Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
90643861 111913 None 0 Rat Binding pEC50 = 6.4 6.4 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 426 11 2 5 5.4 Cc1c(OCCCCOc2cccc(C(=O)O)c2)ccc(C(=O)CC2CCCC2)c1O 10.1021/jm5000563
CHEMBL3287676 111913 None 0 Rat Binding pEC50 = 6.4 6.4 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 426 11 2 5 5.4 Cc1c(OCCCCOc2cccc(C(=O)O)c2)ccc(C(=O)CC2CCCC2)c1O 10.1021/jm5000563
90643867 111923 None 0 Rat Binding pEC50 = 6.3 6.3 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 414 11 2 5 5.2 Cc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)CC(C)C)c(O)c1C 10.1021/jm5000563
CHEMBL3287689 111923 None 0 Rat Binding pEC50 = 6.3 6.3 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 414 11 2 5 5.2 Cc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)CC(C)C)c(O)c1C 10.1021/jm5000563
49765871 2145 None 41 Human Binding pEC50 = 7.3 7.3 - 1
Positive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assayPositive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assay
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.6b00913
6317 2145 None 41 Human Binding pEC50 = 7.3 7.3 - 1
Positive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assayPositive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assay
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.6b00913
CHEMBL2179319 2145 None 41 Human Binding pEC50 = 7.3 7.3 - 1
Positive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assayPositive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assay
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.6b00913
127038550 138150 None 0 Human Binding pEC50 = 5.3 5.3 - 0
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 373 3 0 6 2.9 Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccccc3S(C)(=O)=O)nc21 10.1016/j.bmcl.2016.01.021
CHEMBL3765412 138150 None 0 Human Binding pEC50 = 5.3 5.3 - 0
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 373 3 0 6 2.9 Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccccc3S(C)(=O)=O)nc21 10.1016/j.bmcl.2016.01.021
90643888 111958 None 0 Rat Binding pEC50 = 7.3 7.3 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 444 11 2 6 5.3 COc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)CC(C)(C)C)c(O)c1C 10.1021/jm5000563
CHEMBL3287724 111958 None 0 Rat Binding pEC50 = 7.3 7.3 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 444 11 2 6 5.3 COc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)CC(C)(C)C)c(O)c1C 10.1021/jm5000563
71681824 90090 None 0 Human Binding pEC50 = 7.3 7.3 - 0
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 200 2 4 4 -1.6 N[C@@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]21 10.1021/jm4000165
CHEMBL2381646 90090 None 0 Human Binding pEC50 = 7.3 7.3 - 0
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 200 2 4 4 -1.6 N[C@@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]21 10.1021/jm4000165
53390605 82719 None 0 Rat Binding pEC50 = 6.3 6.3 - 0
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 467 7 1 5 6.3 CC(C)Cn1sc2cc(OCc3cccc(-c4ccc(Cl)c(C(=O)O)c4)c3)ccc2c1=O 10.1021/jm3005306
CHEMBL2179628 82719 None 0 Rat Binding pEC50 = 6.3 6.3 - 0
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 467 7 1 5 6.3 CC(C)Cn1sc2cc(OCc3cccc(-c4ccc(Cl)c(C(=O)O)c4)c3)ccc2c1=O 10.1021/jm3005306
1310 2315 None 61 Human Binding pEC50 = 5.3 5.3 -22 18
Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm00009a001
1369 2315 None 61 Human Binding pEC50 = 5.3 5.3 -22 18
Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm00009a001
33032 2315 None 61 Human Binding pEC50 = 5.3 5.3 -22 18
Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm00009a001
44272391 2315 None 61 Human Binding pEC50 = 5.3 5.3 -22 18
Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm00009a001
88747398 2315 None 61 Human Binding pEC50 = 5.3 5.3 -22 18
Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm00009a001
CHEMBL575060 2315 None 61 Human Binding pEC50 = 5.3 5.3 -22 18
Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm00009a001
DB00142 2315 None 61 Human Binding pEC50 = 5.3 5.3 -22 18
Concentration for half maximal activation of metabotropic glutamate mGluR2 in humanConcentration for half maximal activation of metabotropic glutamate mGluR2 in human
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm00009a001
164623088 185591 None 0 Rat Binding pEC50 = 6.3 6.3 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 448 9 2 5 5.8 Cc1c(OC[C@@H](C)COc2ccc(C(=O)O)cc2Cl)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
CHEMBL4862244 185591 None 0 Rat Binding pEC50 = 6.3 6.3 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 448 9 2 5 5.8 Cc1c(OC[C@@H](C)COc2ccc(C(=O)O)cc2Cl)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
71574840 86305 None 0 Rat Binding pEC50 = 5.3 5.3 - 0
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay
ChEMBL 204 7 4 4 -0.8 NCCC[C@H](C[C@H](N)C(=O)O)C(=O)O 10.1021/acs.jmedchem.5b01333
CHEMBL2312685 86305 None 0 Rat Binding pEC50 = 5.3 5.3 - 0
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay
ChEMBL 204 7 4 4 -0.8 NCCC[C@H](C[C@H](N)C(=O)O)C(=O)O 10.1021/acs.jmedchem.5b01333
89497505 138015 None 0 Human Binding pEC50 = 7.3 7.3 - 0
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 378 3 1 6 3.5 Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3cc(C(C)(C)O)ccc3C#N)nc21 10.1016/j.bmcl.2016.01.021
CHEMBL3763754 138015 None 0 Human Binding pEC50 = 7.3 7.3 - 0
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 378 3 1 6 3.5 Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3cc(C(C)(C)O)ccc3C#N)nc21 10.1016/j.bmcl.2016.01.021
164610947 185357 None 0 Rat Binding pEC50 = 6.3 6.3 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 415 10 2 6 4.7 Cc1c(OCCCCOc2cncc(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
CHEMBL4858387 185357 None 0 Rat Binding pEC50 = 6.3 6.3 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 415 10 2 6 4.7 Cc1c(OCCCCOc2cncc(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
71574840 86305 None 0 Rat Binding pEC50 = 4.3 4.3 - 0
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay
ChEMBL 204 7 4 4 -0.8 NCCC[C@H](C[C@H](N)C(=O)O)C(=O)O 10.1021/acs.jmedchem.5b01333
CHEMBL2312685 86305 None 0 Rat Binding pEC50 = 4.3 4.3 - 0
Agonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assayAgonist activity at rat mGlu2 receptor expressed in HEK293 cells by [35S]GTP-gamma binding assay
ChEMBL 204 7 4 4 -0.8 NCCC[C@H](C[C@H](N)C(=O)O)C(=O)O 10.1021/acs.jmedchem.5b01333
44395282 123224 None 0 Human Binding pEC50 = 6.3 6.3 - 0
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 424 11 2 7 4.4 CCCc1c(OCCCC(C)Oc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2004.08.020
CHEMBL361248 123224 None 0 Human Binding pEC50 = 6.3 6.3 - 0
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 424 11 2 7 4.4 CCCc1c(OCCCC(C)Oc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2004.08.020
46182745 57343 None 0 Rat Binding pEC50 = 7.3 7.3 - 0
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 461 6 1 3 6.2 O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)ccc1Cl 10.1021/jm3005306
CHEMBL1651208 57343 None 0 Rat Binding pEC50 = 7.3 7.3 - 0
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 461 6 1 3 6.2 O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)ccc1Cl 10.1021/jm3005306
46182745 57343 None 0 Rat Binding pEC50 = 7.3 7.3 - 0
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 461 6 1 3 6.2 O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)ccc1Cl 10.1021/jm1012165
CHEMBL1651208 57343 None 0 Rat Binding pEC50 = 7.3 7.3 - 0
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 461 6 1 3 6.2 O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)ccc1Cl 10.1021/jm1012165
90643899 111941 None 0 Rat Binding pEC50 = 7.3 7.3 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 372 9 2 5 4.1 CC(=O)c1ccc(OCCCCOc2ccc(C(=O)O)cc2C)c(C)c1O 10.1021/jm5000563
CHEMBL3287707 111941 None 0 Rat Binding pEC50 = 7.3 7.3 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 372 9 2 5 4.1 CC(=O)c1ccc(OCCCCOc2ccc(C(=O)O)cc2C)c(C)c1O 10.1021/jm5000563
164620553 185875 None 0 Rat Binding pEC50 = 7.3 7.3 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 448 9 2 5 5.8 Cc1c(OC[C@@H](C)COc2ccc(C(=O)O)c(Cl)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
CHEMBL4866466 185875 None 0 Rat Binding pEC50 = 7.3 7.3 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 448 9 2 5 5.8 Cc1c(OC[C@@H](C)COc2ccc(C(=O)O)c(Cl)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
46225386 202218 None 0 Human Binding pEC50 = 7.3 7.3 - 0
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 434 3 0 6 3.8 Cn1c(CN2CCN(c3nc(Cl)ccc3C(F)(F)F)CC2)nc2cc(C#N)ccc21 10.1016/j.bmcl.2009.11.032
CHEMBL593755 202218 None 0 Human Binding pEC50 = 7.3 7.3 - 0
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 434 3 0 6 3.8 Cn1c(CN2CCN(c3nc(Cl)ccc3C(F)(F)F)CC2)nc2cc(C#N)ccc21 10.1016/j.bmcl.2009.11.032
11690041 64889 None 0 Human Binding pEC50 = 5.3 5.3 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 408 6 1 5 4.5 CC1(C2CCCC2)Cc2cc(OCCCc3nn[nH]n3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
CHEMBL182138 64889 None 0 Human Binding pEC50 = 5.3 5.3 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 408 6 1 5 4.5 CC1(C2CCCC2)Cc2cc(OCCCc3nn[nH]n3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
104766 33 None 30 Rat Binding pEC50 = 5.3 5.3 -3 11
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1021/jm00009a001
1365 33 None 30 Rat Binding pEC50 = 5.3 5.3 -3 11
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1021/jm00009a001
CHEMBL34453 33 None 30 Rat Binding pEC50 = 5.3 5.3 -3 11
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1021/jm00009a001
46225373 202280 None 0 Human Binding pEC50 = 6.3 6.3 - 0
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 386 6 0 7 2.4 COCCn1c(CN2CCN(c3ncc(Cl)cn3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL594205 202280 None 0 Human Binding pEC50 = 6.3 6.3 - 0
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 386 6 0 7 2.4 COCCn1c(CN2CCN(c3ncc(Cl)cn3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
46225337 202433 None 0 Human Binding pEC50 = 6.3 6.3 - 1
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 375 3 0 5 3.3 Cn1c(CN2CCN(c3ccc(C(F)(F)F)cn3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL595151 202433 None 0 Human Binding pEC50 = 6.3 6.3 - 1
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 375 3 0 5 3.3 Cn1c(CN2CCN(c3ccc(C(F)(F)F)cn3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
851990 202161 None 4 Human Binding pEC50 = 5.3 5.3 - 0
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 306 3 0 4 2.9 Cn1c(CN2CCN(c3ccccc3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL593300 202161 None 4 Human Binding pEC50 = 5.3 5.3 - 0
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 306 3 0 4 2.9 Cn1c(CN2CCN(c3ccccc3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
164618046 185568 None 0 Rat Binding pEC50 = 5.3 5.3 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 471 10 1 6 5.1 COc1ccc(C(=O)N(C)C)cc1OC[C@H](C)COc1ccc(C(=O)CC(C)(C)C)c(O)c1C 10.1016/j.bmcl.2021.128342
CHEMBL4861837 185568 None 0 Rat Binding pEC50 = 5.3 5.3 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 471 10 1 6 5.1 COc1ccc(C(=O)N(C)C)cc1OC[C@H](C)COc1ccc(C(=O)CC(C)(C)C)c(O)c1C 10.1016/j.bmcl.2021.128342
71116730 149150 None 0 Human Binding pEC50 = 7.3 7.3 - 0
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 424 3 1 6 2.6 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)C5(O)CCC5)CC4C3)nc21 nan
CHEMBL3942904 149150 None 0 Human Binding pEC50 = 7.3 7.3 - 0
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 424 3 1 6 2.6 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)C5(O)CCC5)CC4C3)nc21 nan
90643864 111920 None 0 Rat Binding pEC50 = 6.3 6.3 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 460 11 2 5 6.1 Cc1c(OCCCCOc2ccc(C(=O)O)c(Cl)c2)ccc(C(=O)CC2CCCC2)c1O 10.1021/jm5000563
CHEMBL3287684 111920 None 0 Rat Binding pEC50 = 6.3 6.3 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 460 11 2 5 6.1 Cc1c(OCCCCOc2ccc(C(=O)O)c(Cl)c2)ccc(C(=O)CC2CCCC2)c1O 10.1021/jm5000563
44578997 181692 None 0 Rat Binding pEC50 = 6.3 6.3 - 0
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 368 5 0 5 3.4 Cn1c(CN2C[C@@H]3C(COc4ccc(Cl)nc4)[C@@H]3C2)nc2ccccc21 10.1016/j.bmcl.2008.09.026
CHEMBL476966 181692 None 0 Rat Binding pEC50 = 6.3 6.3 - 0
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 368 5 0 5 3.4 Cn1c(CN2C[C@@H]3C(COc4ccc(Cl)nc4)[C@@H]3C2)nc2ccccc21 10.1016/j.bmcl.2008.09.026
164625596 185848 None 0 Rat Binding pEC50 = 6.3 6.3 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 428 10 2 5 5.6 Cc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)CC(C)(C)C)c(O)c1C 10.1016/j.bmcl.2021.128342
CHEMBL4866163 185848 None 0 Rat Binding pEC50 = 6.3 6.3 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 428 10 2 5 5.6 Cc1ccc(C(=O)O)cc1OCCCCOc1ccc(C(=O)CC(C)(C)C)c(O)c1C 10.1016/j.bmcl.2021.128342
11699129 132033 None 0 Human Binding pEC50 = 6.3 6.3 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 509 6 1 5 5.2 CC1(C2CCCC2)Cc2cc(OCc3ccc(C(=O)NS(C)(=O)=O)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
CHEMBL369526 132033 None 0 Human Binding pEC50 = 6.3 6.3 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 509 6 1 5 5.2 CC1(C2CCCC2)Cc2cc(OCc3ccc(C(=O)NS(C)(=O)=O)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
90643885 111954 None 0 Rat Binding pEC50 = 7.3 7.3 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 400 11 2 5 4.9 CCCC(=O)c1ccc(OCCCCOc2cccc(C(=O)O)c2C)c(C)c1O 10.1021/jm5000563
CHEMBL3287720 111954 None 0 Rat Binding pEC50 = 7.3 7.3 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 400 11 2 5 4.9 CCCC(=O)c1ccc(OCCCCOc2cccc(C(=O)O)c2C)c(C)c1O 10.1021/jm5000563
117972250 142399 None 4 Human Binding pEC50 = 6.3 6.3 - 1
Agonist activity at humanized monkey mGlu2 receptor expressed in HEK293 cells co-expressing Gqi5 measured for 3 mins by Fluo-4 dye based FLIPR assayAgonist activity at humanized monkey mGlu2 receptor expressed in HEK293 cells co-expressing Gqi5 measured for 3 mins by Fluo-4 dye based FLIPR assay
ChEMBL 421 6 0 4 5.5 FC(F)(F)c1c(OC[C@H]2C[C@@H]2c2ccc(Cl)cc2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
CHEMBL3885379 142399 None 4 Human Binding pEC50 = 6.3 6.3 - 1
Agonist activity at humanized monkey mGlu2 receptor expressed in HEK293 cells co-expressing Gqi5 measured for 3 mins by Fluo-4 dye based FLIPR assayAgonist activity at humanized monkey mGlu2 receptor expressed in HEK293 cells co-expressing Gqi5 measured for 3 mins by Fluo-4 dye based FLIPR assay
ChEMBL 421 6 0 4 5.5 FC(F)(F)c1c(OC[C@H]2C[C@@H]2c2ccc(Cl)cc2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
71128783 140295 None 0 Human Binding pEC50 = 6.3 6.3 - 0
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 397 3 0 7 2.8 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3CCN(C(=O)c4ccon4)CC3)nc21 10.1021/acsmedchemlett.5b00459
CHEMBL3805005 140295 None 0 Human Binding pEC50 = 6.3 6.3 - 0
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 397 3 0 7 2.8 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3CCN(C(=O)c4ccon4)CC3)nc21 10.1021/acsmedchemlett.5b00459
162677305 183899 None 0 Rat Binding pEC50 = 7.3 7.3 - 0
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1078 23 6 12 9.0 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
CHEMBL4800093 183899 None 0 Rat Binding pEC50 = 7.3 7.3 - 0
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1078 23 6 12 9.0 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
CHEMBL4804159 183899 None 0 Rat Binding pEC50 = 7.3 7.3 - 0
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1078 23 6 12 9.0 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
71116952 147402 None 0 Human Binding pEC50 = 7.3 7.3 - 0
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 421 3 0 7 2.9 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)c5ncco5)CC4C3)nc21 nan
CHEMBL3929070 147402 None 0 Human Binding pEC50 = 7.3 7.3 - 0
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 421 3 0 7 2.9 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CN(C(=O)c5ncco5)CC4C3)nc21 nan
10775369 178470 None 1 Human Binding pEC50 = 4.3 4.3 - 0
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
ChEMBL 185 2 3 3 -0.5 N[C@@]1(C(=O)O)C[C@H]2C[C@@H]1[C@@H]2C(=O)O 10.1021/jm970719q
CHEMBL46527 178470 None 1 Human Binding pEC50 = 4.3 4.3 - 0
Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).Compound was tested for the inhibition of metabotropic glutamate receptor 2 (mGluR2).
ChEMBL 185 2 3 3 -0.5 N[C@@]1(C(=O)O)C[C@H]2C[C@@H]1[C@@H]2C(=O)O 10.1021/jm970719q
11684927 63496 None 0 Human Binding pEC50 = 6.3 6.3 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 511 7 0 4 8.2 CC1(C2CCCC2)Cc2cc(OCc3cccc(CSc4ccncc4)c3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
CHEMBL179876 63496 None 0 Human Binding pEC50 = 6.3 6.3 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 511 7 0 4 8.2 CC1(C2CCCC2)Cc2cc(OCc3cccc(CSc4ccncc4)c3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
90643877 111934 None 0 Rat Binding pEC50 = 6.3 6.3 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 440 11 2 5 5.7 Cc1cc(OCCCCOc2ccc(C(=O)CC3CCCC3)c(O)c2C)ccc1C(=O)O 10.1021/jm5000563
CHEMBL3287700 111934 None 0 Rat Binding pEC50 = 6.3 6.3 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 440 11 2 5 5.7 Cc1cc(OCCCCOc2ccc(C(=O)CC3CCCC3)c(O)c2C)ccc1C(=O)O 10.1021/jm5000563
68108604 147492 None 0 Human Binding pEC50 = 7.2 7.2 - 0
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 480 7 0 5 5.2 Fc1ccc(COC2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
CHEMBL3929786 147492 None 0 Human Binding pEC50 = 7.2 7.2 - 0
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 480 7 0 5 5.2 Fc1ccc(COC2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
68107740 151632 None 0 Human Binding pEC50 = 7.2 7.2 - 0
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 466 6 0 5 5.0 Fc1ccc(OC2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
CHEMBL3963034 151632 None 0 Human Binding pEC50 = 7.2 7.2 - 0
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 466 6 0 5 5.0 Fc1ccc(OC2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
89735006 138032 None 0 Human Binding pEC50 = 7.2 7.2 - 0
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 309 2 0 4 3.8 Cc1ccccc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C 10.1016/j.bmcl.2016.01.021
CHEMBL3764005 138032 None 0 Human Binding pEC50 = 7.2 7.2 - 0
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 309 2 0 4 3.8 Cc1ccccc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C 10.1016/j.bmcl.2016.01.021
88593167 150847 None 0 Human Binding pEC50 = 7.2 7.2 - 0
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 482 5 0 4 5.8 FC(F)(F)c1c(CN2CCC(c3ccccc3)(C(F)(F)F)CC2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.6b00913
CHEMBL3956434 150847 None 0 Human Binding pEC50 = 7.2 7.2 - 0
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 482 5 0 4 5.8 FC(F)(F)c1c(CN2CCC(c3ccccc3)(C(F)(F)F)CC2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.6b00913
53390675 82718 None 0 Rat Binding pEC50 = 6.2 6.2 - 0
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 465 6 1 5 6.4 O=C(O)c1cc(-c2cccc(COc3ccc4c(=O)n(C5CCC5)sc4c3)c2)ccc1Cl 10.1021/jm3005306
CHEMBL2179627 82718 None 0 Rat Binding pEC50 = 6.2 6.2 - 0
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 465 6 1 5 6.4 O=C(O)c1cc(-c2cccc(COc3ccc4c(=O)n(C5CCC5)sc4c3)c2)ccc1Cl 10.1021/jm3005306
11676185 65611 None 0 Human Binding pEC50 = 6.2 6.2 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 422 7 1 5 4.8 CC1(C2CCCC2)Cc2cc(OCCCCc3nn[nH]n3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
CHEMBL183234 65611 None 0 Human Binding pEC50 = 6.2 6.2 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 422 7 1 5 4.8 CC1(C2CCCC2)Cc2cc(OCCCCc3nn[nH]n3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
44390403 122402 None 0 Human Binding pEC50 = 6.2 6.2 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 457 7 0 4 7.1 Cc1c(OCc2cccc(CSc3ccncc3)c2)cc2c(c1C)C(=O)C(C1CCCC1)C2 10.1016/j.bmcl.2005.01.077
CHEMBL359909 122402 None 0 Human Binding pEC50 = 6.2 6.2 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 457 7 0 4 7.1 Cc1c(OCc2cccc(CSc3ccncc3)c2)cc2c(c1C)C(=O)C(C1CCCC1)C2 10.1016/j.bmcl.2005.01.077
50994051 57352 None 0 Rat Binding pEC50 = 7.2 7.2 - 0
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 463 8 1 3 6.3 CC(C)CCN1Cc2cc(OCc3cccc(-c4ccc(Cl)c(C(=O)O)c4)c3)ccc2C1=O 10.1021/jm1012165
CHEMBL1651217 57352 None 0 Rat Binding pEC50 = 7.2 7.2 - 0
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 463 8 1 3 6.3 CC(C)CCN1Cc2cc(OCc3cccc(-c4ccc(Cl)c(C(=O)O)c4)c3)ccc2C1=O 10.1021/jm1012165
11663353 123305 None 1 Human Binding pEC50 = 6.2 6.2 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 499 6 2 6 5.1 CC1(C2CCCC2)Cc2cc(OCC(=O)Nc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
CHEMBL361358 123305 None 1 Human Binding pEC50 = 6.2 6.2 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 499 6 2 6 5.1 CC1(C2CCCC2)Cc2cc(OCC(=O)Nc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
54761054 138168 None 0 Human Binding pEC50 = 6.2 6.2 - 2
Positive allosteric modulation of human mGluR2 by GTP-gamma-S binding assayPositive allosteric modulation of human mGluR2 by GTP-gamma-S binding assay
ChEMBL 367 3 1 5 4.0 Cc1ccc(C(C)(C)O)cc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C 10.1016/j.bmcl.2016.01.021
CHEMBL3765778 138168 None 0 Human Binding pEC50 = 6.2 6.2 - 2
Positive allosteric modulation of human mGluR2 by GTP-gamma-S binding assayPositive allosteric modulation of human mGluR2 by GTP-gamma-S binding assay
ChEMBL 367 3 1 5 4.0 Cc1ccc(C(C)(C)O)cc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C 10.1016/j.bmcl.2016.01.021
90643870 111926 None 0 Rat Binding pEC50 = 6.2 6.2 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 440 11 2 5 5.7 Cc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)CC2CCCC2)c(O)c1C 10.1021/jm5000563
CHEMBL3287692 111926 None 0 Rat Binding pEC50 = 6.2 6.2 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 440 11 2 5 5.7 Cc1cc(C(=O)O)ccc1OCCCCOc1ccc(C(=O)CC2CCCC2)c(O)c1C 10.1021/jm5000563
54761054 138168 None 0 Human Binding pEC50 = 7.2 7.2 - 2
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 367 3 1 5 4.0 Cc1ccc(C(C)(C)O)cc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C 10.1016/j.bmcl.2016.01.021
CHEMBL3765778 138168 None 0 Human Binding pEC50 = 7.2 7.2 - 2
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 367 3 1 5 4.0 Cc1ccc(C(C)(C)O)cc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C 10.1016/j.bmcl.2016.01.021
11691314 182006 None 0 Rat Binding pEC50 = 7.2 7.2 - 0
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 470 6 2 4 6.5 Cc1c(OCc2cccc(-c3ccc(O)c(C(=O)O)c3)c2)cc2c(c1C)C(=O)C(C1CCCC1)C2 10.1016/j.bmcl.2020.127212
CHEMBL4779278 182006 None 0 Rat Binding pEC50 = 7.2 7.2 - 0
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 470 6 2 4 6.5 Cc1c(OCc2cccc(-c3ccc(O)c(C(=O)O)c3)c2)cc2c(c1C)C(=O)C(C1CCCC1)C2 10.1016/j.bmcl.2020.127212
162660656 183812 None 0 Rat Binding pEC50 = 7.2 7.2 - 0
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1120 26 6 12 10.2 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
CHEMBL4762369 183812 None 0 Rat Binding pEC50 = 7.2 7.2 - 0
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1120 26 6 12 10.2 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
CHEMBL4803219 183812 None 0 Rat Binding pEC50 = 7.2 7.2 - 0
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1120 26 6 12 10.2 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
90643901 111944 None 0 Rat Binding pEC50 = 7.2 7.2 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 386 10 2 5 4.5 CCC(=O)c1ccc(OCCCCOc2cccc(C(=O)O)c2C)c(C)c1O 10.1021/jm5000563
CHEMBL3287710 111944 None 0 Rat Binding pEC50 = 7.2 7.2 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 386 10 2 5 4.5 CCC(=O)c1ccc(OCCCCOc2cccc(C(=O)O)c2C)c(C)c1O 10.1021/jm5000563
23521692 108629 None 0 Human Binding pEC50 = 6.2 6.2 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 436 8 0 4 4.6 O=S(=O)(CC(F)(F)F)N(Cc1cccnc1)c1cccc(OCc2ccccc2)c1 10.1016/j.bmcl.2004.04.017
CHEMBL320292 108629 None 0 Human Binding pEC50 = 6.2 6.2 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 436 8 0 4 4.6 O=S(=O)(CC(F)(F)F)N(Cc1cccnc1)c1cccc(OCc2ccccc2)c1 10.1016/j.bmcl.2004.04.017
11691221 123394 None 0 Human Binding pEC50 = 6.2 6.2 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 464 5 1 5 5.4 CC1(c2ccccc2)Cc2cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
CHEMBL361633 123394 None 0 Human Binding pEC50 = 6.2 6.2 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 464 5 1 5 5.4 CC1(c2ccccc2)Cc2cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
54761054 138168 None 0 Human Binding pEC50 = 7.2 7.2 - 2
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 367 3 1 5 4.0 Cc1ccc(C(C)(C)O)cc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C 10.1021/acsmedchemlett.5b00459
CHEMBL3765778 138168 None 0 Human Binding pEC50 = 7.2 7.2 - 2
Positive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 367 3 1 5 4.0 Cc1ccc(C(C)(C)O)cc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C 10.1021/acsmedchemlett.5b00459
164616933 185171 None 0 Rat Binding pEC50 = 7.2 7.2 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 444 10 2 6 5.1 COc1ccc(C(=O)O)cc1OC[C@H](C)COc1ccc(C(=O)CC(C)(C)C)c(O)c1C 10.1016/j.bmcl.2021.128342
CHEMBL4855540 185171 None 0 Rat Binding pEC50 = 7.2 7.2 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 444 10 2 6 5.1 COc1ccc(C(=O)O)cc1OC[C@H](C)COc1ccc(C(=O)CC(C)(C)C)c(O)c1C 10.1016/j.bmcl.2021.128342
46225357 202253 None 0 Human Binding pEC50 = 7.2 7.2 - 0
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 423 4 0 5 4.4 CCn1c(CN2CCN(c3nc(C(F)(F)F)ccc3Cl)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL594011 202253 None 0 Human Binding pEC50 = 7.2 7.2 - 0
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 423 4 0 5 4.4 CCn1c(CN2CCN(c3nc(C(F)(F)F)ccc3Cl)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
11310142 2422 None 14 Human Binding pEC50 = 7.2 7.2 1 2
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 199 2 3 3 -0.2 C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O 10.1021/jm4000165
11614 2422 None 14 Human Binding pEC50 = 7.2 7.2 1 2
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 199 2 3 3 -0.2 C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O 10.1021/jm4000165
CHEMBL192051 2422 None 14 Human Binding pEC50 = 7.2 7.2 1 2
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 199 2 3 3 -0.2 C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O 10.1021/jm4000165
51036108 140314 None 0 Human Binding pEC50 = 6.2 6.2 - 0
Agonist activity at recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayAgonist activity at recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 441 3 0 9 2.1 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3C[C@@H]4CC[C@H]3CN4C(=O)c3csnn3)nc21 10.1021/acsmedchemlett.5b00459
CHEMBL3805203 140314 None 0 Human Binding pEC50 = 6.2 6.2 - 0
Agonist activity at recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayAgonist activity at recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 441 3 0 9 2.1 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3C[C@@H]4CC[C@H]3CN4C(=O)c3csnn3)nc21 10.1021/acsmedchemlett.5b00459
90643872 111928 None 0 Rat Binding pEC50 = 6.2 6.2 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 444 11 2 5 5.5 Cc1c(OCCCCOc2ccc(C(=O)O)cc2F)ccc(C(=O)CC2CCCC2)c1O 10.1021/jm5000563
CHEMBL3287694 111928 None 0 Rat Binding pEC50 = 6.2 6.2 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 444 11 2 5 5.5 Cc1c(OCCCCOc2ccc(C(=O)O)cc2F)ccc(C(=O)CC2CCCC2)c1O 10.1021/jm5000563
25050844 184349 None 0 Rat Binding pEC50 = 7.2 7.2 - 0
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 368 5 0 5 3.4 Cn1c(CN2C[C@@H]3C(COc4cccc(Cl)c4)[C@@H]3C2)nc2ncccc21 10.1016/j.bmcl.2008.09.026
CHEMBL483570 184349 None 0 Rat Binding pEC50 = 7.2 7.2 - 0
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 368 5 0 5 3.4 Cn1c(CN2C[C@@H]3C(COc4cccc(Cl)c4)[C@@H]3C2)nc2ncccc21 10.1016/j.bmcl.2008.09.026
44335613 169243 None 0 Human Binding pEC50 = 6.2 6.2 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 432 9 0 6 2.9 CCOC(=O)COc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1 10.1016/j.bmcl.2004.04.017
CHEMBL440328 169243 None 0 Human Binding pEC50 = 6.2 6.2 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 432 9 0 6 2.9 CCOC(=O)COc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1 10.1016/j.bmcl.2004.04.017
53390678 82716 None 0 Rat Binding pEC50 = 6.2 6.2 - 0
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 425 5 1 5 5.2 Cn1sc2cc(OCc3cccc(-c4ccc(Cl)c(C(=O)O)c4)c3)ccc2c1=O 10.1021/jm3005306
CHEMBL2179625 82716 None 0 Rat Binding pEC50 = 6.2 6.2 - 0
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 425 5 1 5 5.2 Cn1sc2cc(OCc3cccc(-c4ccc(Cl)c(C(=O)O)c4)c3)ccc2c1=O 10.1021/jm3005306
69093542 147515 None 0 Human Binding pEC50 = 7.2 7.2 - 0
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 414 5 0 4 5.1 FC(F)(F)c1c(CN2CCCC(c3ccccc3)C2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.6b00913
CHEMBL3929950 147515 None 0 Human Binding pEC50 = 7.2 7.2 - 0
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 414 5 0 4 5.1 FC(F)(F)c1c(CN2CCCC(c3ccccc3)C2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.6b00913
25195461 2144 None 42 Human Binding pEC50 = 7.2 7.2 - 1
Positive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
8946 2144 None 42 Human Binding pEC50 = 7.2 7.2 - 1
Positive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
CHEMBL3337527 2144 None 42 Human Binding pEC50 = 7.2 7.2 - 1
Positive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
DB12059 2144 None 42 Human Binding pEC50 = 7.2 7.2 - 1
Positive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of wild-type human mGlu2 receptor expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
53390604 82721 None 0 Rat Binding pEC50 = 6.2 6.2 - 0
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 481 8 1 5 6.7 CC(C)CCn1sc2cc(OCc3cccc(-c4ccc(Cl)c(C(=O)O)c4)c3)ccc2c1=O 10.1021/jm3005306
CHEMBL2179630 82721 None 0 Rat Binding pEC50 = 6.2 6.2 - 0
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 481 8 1 5 6.7 CC(C)CCn1sc2cc(OCc3cccc(-c4ccc(Cl)c(C(=O)O)c4)c3)ccc2c1=O 10.1021/jm3005306
49822116 147080 None 14 Human Binding pEC50 = 5.2 5.2 - 1
Positive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 451 5 0 5 4.3 Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
CHEMBL3926416 147080 None 14 Human Binding pEC50 = 5.2 5.2 - 1
Positive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation at human mGlu2 receptor F643A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 451 5 0 5 4.3 Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
127052897 140395 None 0 Human Binding pEC50 = 6.2 6.2 - 0
Agonist activity at recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayAgonist activity at recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 424 3 0 8 2.3 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3C[C@@H]4CC[C@H]3CN4C(=O)c3ccon3)nc21 10.1021/acsmedchemlett.5b00459
CHEMBL3806137 140395 None 0 Human Binding pEC50 = 6.2 6.2 - 0
Agonist activity at recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assayAgonist activity at recombinant human mGlu2 receptor expressed in CHO cells assessed as potentiation of glutamate-induced effect preincubated for 5 mins followed by glutamate stimulation for 3 mins by Fluo-4AM staining-based FLIPR assay
ChEMBL 424 3 0 8 2.3 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3C[C@@H]4CC[C@H]3CN4C(=O)c3ccon3)nc21 10.1021/acsmedchemlett.5b00459
11568710 180526 None 0 Rat Binding pEC50 = 7.2 7.2 - 0
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 454 6 1 3 6.8 Cc1c(OCc2cccc(-c3cccc(C(=O)O)c3)c2)cc2c(c1C)C(=O)C(C1CCCC1)C2 10.1016/j.bmcl.2020.127212
CHEMBL4752318 180526 None 0 Rat Binding pEC50 = 7.2 7.2 - 0
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 454 6 1 3 6.8 Cc1c(OCc2cccc(-c3cccc(C(=O)O)c3)c2)cc2c(c1C)C(=O)C(C1CCCC1)C2 10.1016/j.bmcl.2020.127212
71116726 145364 None 0 Human Binding pEC50 = 7.2 7.2 - 0
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 438 3 0 8 3.0 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3csnn3)nc21 nan
CHEMBL3912982 145364 None 0 Human Binding pEC50 = 7.2 7.2 - 0
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 438 3 0 8 3.0 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3csnn3)nc21 nan
90643866 111922 None 0 Rat Binding pEC50 = 6.2 6.2 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 444 11 2 5 5.5 Cc1c(OCCCCOc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC2CCCC2)c1O 10.1021/jm5000563
CHEMBL3287688 111922 None 0 Rat Binding pEC50 = 6.2 6.2 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 444 11 2 5 5.5 Cc1c(OCCCCOc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC2CCCC2)c1O 10.1021/jm5000563
44578905 181694 None 0 Rat Binding pEC50 = 8.2 8.2 - 0
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 369 5 0 4 3.6 Cn1c(CN2C[C@@H]3C(COc4cc(F)ccc4F)[C@@H]3C2)nc2ccccc21 10.1016/j.bmcl.2008.09.026
CHEMBL476998 181694 None 0 Rat Binding pEC50 = 8.2 8.2 - 0
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 369 5 0 4 3.6 Cn1c(CN2C[C@@H]3C(COc4cc(F)ccc4F)[C@@H]3C2)nc2ccccc21 10.1016/j.bmcl.2008.09.026
11084869 90087 None 1 Human Binding pEC50 = 8.1 8.1 - 1
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 201 2 4 4 -1.5 N[C@@]1(C(=O)O)C[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/jm4000165
CHEMBL2381643 90087 None 1 Human Binding pEC50 = 8.1 8.1 - 1
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 201 2 4 4 -1.5 N[C@@]1(C(=O)O)C[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/jm4000165
70052526 90086 None 1 Human Binding pEC50 = 8.1 8.1 - 1
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 201 2 4 4 -1.5 N[C@@]1(C(=O)O)C[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/jm4000165
CHEMBL2381642 90086 None 1 Human Binding pEC50 = 8.1 8.1 - 1
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 201 2 4 4 -1.5 N[C@@]1(C(=O)O)C[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/jm4000165
50993963 57344 None 0 Rat Binding pEC50 = 7.2 7.2 - 0
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 435 6 1 3 5.6 CC(C)N1Cc2cc(OCc3cccc(-c4ccc(Cl)c(C(=O)O)c4)c3)ccc2C1=O 10.1021/jm1012165
CHEMBL1651209 57344 None 0 Rat Binding pEC50 = 7.2 7.2 - 0
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 435 6 1 3 5.6 CC(C)N1Cc2cc(OCc3cccc(-c4ccc(Cl)c(C(=O)O)c4)c3)ccc2C1=O 10.1021/jm1012165
89735186 137989 None 0 Human Binding pEC50 = 7.2 7.2 - 0
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 295 2 0 4 3.4 Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccccc3)nc21 10.1016/j.bmcl.2016.01.021
CHEMBL3763395 137989 None 0 Human Binding pEC50 = 7.2 7.2 - 0
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 295 2 0 4 3.4 Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccccc3)nc21 10.1016/j.bmcl.2016.01.021
10249222 5013 None 0 Human Binding pEC50 = 7.1 7.1 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 380 7 0 3 4.6 CCS(=O)(=O)N(Cc1cccnc1)c1cccc(C(C)c2ccccc2)c1 10.1016/j.bmcl.2004.04.017
CHEMBL105065 5013 None 0 Human Binding pEC50 = 7.1 7.1 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 380 7 0 3 4.6 CCS(=O)(=O)N(Cc1cccnc1)c1cccc(C(C)c2ccccc2)c1 10.1016/j.bmcl.2004.04.017
90643886 111955 None 0 Rat Binding pEC50 = 7.1 7.1 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 404 11 2 5 4.8 CCCC(=O)c1ccc(OCCCCOc2ccc(F)c(C(=O)O)c2)c(C)c1O 10.1021/jm5000563
CHEMBL3287721 111955 None 0 Rat Binding pEC50 = 7.1 7.1 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 404 11 2 5 4.8 CCCC(=O)c1ccc(OCCCCOc2ccc(F)c(C(=O)O)c2)c(C)c1O 10.1021/jm5000563
53390680 82731 None 0 Rat Binding pEC50 = 6.1 6.1 - 0
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 459 6 1 5 6.4 Cc1ccc(C(=O)O)cc1-c1cccc(COc2ccc3c(=O)n(C4CCCC4)sc3c2)c1 10.1021/jm3005306
CHEMBL2179642 82731 None 0 Rat Binding pEC50 = 6.1 6.1 - 0
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 459 6 1 5 6.4 Cc1ccc(C(=O)O)cc1-c1cccc(COc2ccc3c(=O)n(C4CCCC4)sc3c2)c1 10.1021/jm3005306
1310 2315 None 61 Human Binding pEC50 = 5.1 5.1 -22 18
Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/s0960-894x(01)00656-4
1369 2315 None 61 Human Binding pEC50 = 5.1 5.1 -22 18
Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/s0960-894x(01)00656-4
33032 2315 None 61 Human Binding pEC50 = 5.1 5.1 -22 18
Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/s0960-894x(01)00656-4
44272391 2315 None 61 Human Binding pEC50 = 5.1 5.1 -22 18
Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/s0960-894x(01)00656-4
88747398 2315 None 61 Human Binding pEC50 = 5.1 5.1 -22 18
Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/s0960-894x(01)00656-4
CHEMBL575060 2315 None 61 Human Binding pEC50 = 5.1 5.1 -22 18
Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/s0960-894x(01)00656-4
DB00142 2315 None 61 Human Binding pEC50 = 5.1 5.1 -22 18
Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/s0960-894x(01)00656-4
127052897 140395 None 0 Rat Binding pEC50 = 7.1 7.1 - 0
Positive allosteric modulation of rat mGlu2 receptor assessed as potentiation of glutamate-induced effect by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of rat mGlu2 receptor assessed as potentiation of glutamate-induced effect by Fluo-4AM staining-based FLIPR assay
ChEMBL 424 3 0 8 2.3 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3C[C@@H]4CC[C@H]3CN4C(=O)c3ccon3)nc21 10.1021/acsmedchemlett.5b00459
CHEMBL3806137 140395 None 0 Rat Binding pEC50 = 7.1 7.1 - 0
Positive allosteric modulation of rat mGlu2 receptor assessed as potentiation of glutamate-induced effect by Fluo-4AM staining-based FLIPR assayPositive allosteric modulation of rat mGlu2 receptor assessed as potentiation of glutamate-induced effect by Fluo-4AM staining-based FLIPR assay
ChEMBL 424 3 0 8 2.3 Cn1c(=O)n(CC(C)(C)C)c2ccc(N3C[C@@H]4CC[C@H]3CN4C(=O)c3ccon3)nc21 10.1021/acsmedchemlett.5b00459
164614107 185236 None 0 Rat Binding pEC50 = 7.1 7.1 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 432 10 2 5 5.4 Cc1c(OCCCCOc2ccc(C(=O)O)cc2F)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
CHEMBL4856556 185236 None 0 Rat Binding pEC50 = 7.1 7.1 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 432 10 2 5 5.4 Cc1c(OCCCCOc2ccc(C(=O)O)cc2F)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
1368 2290 None 30 Rat Binding pEC50 = 6.1 6.1 1 11
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 159 3 3 3 -0.9 N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O 10.1021/jm00009a001
5310956 2290 None 30 Rat Binding pEC50 = 6.1 6.1 1 11
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 159 3 3 3 -0.9 N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O 10.1021/jm00009a001
CHEMBL280563 2290 None 30 Rat Binding pEC50 = 6.1 6.1 1 11
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 159 3 3 3 -0.9 N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O 10.1021/jm00009a001
44395381 66160 None 0 Human Binding pEC50 = 5.1 5.1 - 0
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 424 10 2 8 3.5 CCCc1c(OCCCC(=O)Oc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2004.08.020
CHEMBL184098 66160 None 0 Human Binding pEC50 = 5.1 5.1 - 0
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 424 10 2 8 3.5 CCCc1c(OCCCC(=O)Oc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2004.08.020
11539379 65619 None 0 Human Binding pEC50 = 6.1 6.1 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 436 8 1 5 5.2 CC1(C2CCCC2)Cc2cc(OCCCCCc3nn[nH]n3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
CHEMBL183286 65619 None 0 Human Binding pEC50 = 6.1 6.1 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 436 8 1 5 5.2 CC1(C2CCCC2)Cc2cc(OCCCCCc3nn[nH]n3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
25195461 2144 None 42 Human Binding pEC50 = 7.1 7.1 - 1
Positive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assayPositive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assay
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
8946 2144 None 42 Human Binding pEC50 = 7.1 7.1 - 1
Positive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assayPositive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assay
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
CHEMBL3337527 2144 None 42 Human Binding pEC50 = 7.1 7.1 - 1
Positive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assayPositive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assay
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
DB12059 2144 None 42 Human Binding pEC50 = 7.1 7.1 - 1
Positive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assayPositive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assay
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
104766 33 None 30 Rat Binding pEC50 = 5.1 5.1 -3 11
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1021/jm00009a001
1365 33 None 30 Rat Binding pEC50 = 5.1 5.1 -3 11
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1021/jm00009a001
CHEMBL34453 33 None 30 Rat Binding pEC50 = 5.1 5.1 -3 11
Concentration for half maximal activation of metabotropic glutamate mGluR2 in ratConcentration for half maximal activation of metabotropic glutamate mGluR2 in rat
ChEMBL 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10.1021/jm00009a001
49822116 147080 None 14 Human Binding pEC50 = 7.1 7.1 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 451 5 0 5 4.3 Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
CHEMBL3926416 147080 None 14 Human Binding pEC50 = 7.1 7.1 - 1
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 451 5 0 5 4.3 Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
168278157 190468 None 0 Human Binding pEC50 = 7.1 7.1 - 0
Positive allosteric modulation of mGlu2 receptor (unknown origin)Positive allosteric modulation of mGlu2 receptor (unknown origin)
ChEMBL 435 4 0 3 6.4 Fc1ccc(C2CCC(c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1016/j.bmc.2022.116614
CHEMBL5177038 190468 None 0 Human Binding pEC50 = 7.1 7.1 - 0
Positive allosteric modulation of mGlu2 receptor (unknown origin)Positive allosteric modulation of mGlu2 receptor (unknown origin)
ChEMBL 435 4 0 3 6.4 Fc1ccc(C2CCC(c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1016/j.bmc.2022.116614
164616491 185497 None 0 Rat Binding pEC50 = 7.1 7.1 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 430 9 2 6 4.9 COc1ccc(C(=O)O)cc1OC[C@@H](C)Oc1ccc(C(=O)CC(C)(C)C)c(O)c1C 10.1016/j.bmcl.2021.128342
CHEMBL4860693 185497 None 0 Rat Binding pEC50 = 7.1 7.1 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 430 9 2 6 4.9 COc1ccc(C(=O)O)cc1OC[C@@H](C)Oc1ccc(C(=O)CC(C)(C)C)c(O)c1C 10.1016/j.bmcl.2021.128342
23521714 4808 None 0 Human Binding pEC50 = 6.1 6.1 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 378 7 0 3 4.5 C=C(c1ccccc1)c1ccc(N(Cc2cccnc2)S(=O)(=O)CC)cc1 10.1016/j.bmcl.2004.04.017
CHEMBL104140 4808 None 0 Human Binding pEC50 = 6.1 6.1 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 378 7 0 3 4.5 C=C(c1ccccc1)c1ccc(N(Cc2cccnc2)S(=O)(=O)CC)cc1 10.1016/j.bmcl.2004.04.017
11516962 63918 None 0 Human Binding pEC50 = 6.1 6.1 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 402 4 1 5 4.5 CC1(C)Cc2cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
CHEMBL180488 63918 None 0 Human Binding pEC50 = 6.1 6.1 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 402 4 1 5 4.5 CC1(C)Cc2cc(OCc3ccc(-c4nn[nH]n4)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
46190877 1871 None 8 Human Binding pEC50 = 7.1 7.1 - 3
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 409 3 0 5 4.0 Clc1cc(cnc1N1CCN(CC1)Cc1nc2c(n1C)cccc2)C(F)(F)F 10.1016/j.bmcl.2009.11.032
6252 1871 None 8 Human Binding pEC50 = 7.1 7.1 - 3
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 409 3 0 5 4.0 Clc1cc(cnc1N1CCN(CC1)Cc1nc2c(n1C)cccc2)C(F)(F)F 10.1016/j.bmcl.2009.11.032
CHEMBL605836 1871 None 8 Human Binding pEC50 = 7.1 7.1 - 3
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 409 3 0 5 4.0 Clc1cc(cnc1N1CCN(CC1)Cc1nc2c(n1C)cccc2)C(F)(F)F 10.1016/j.bmcl.2009.11.032
24849462 202214 None 0 Human Binding pEC50 = 7.1 7.1 - 3
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 339 3 0 3 4.6 Cn1c(CN2CCC(c3ccc(Cl)cc3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL593744 202214 None 0 Human Binding pEC50 = 7.1 7.1 - 3
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 339 3 0 3 4.6 Cn1c(CN2CCC(c3ccc(Cl)cc3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
46225374 202310 None 0 Human Binding pEC50 = 6.1 6.1 - 0
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 370 5 0 6 3.2 CCCn1c(CN2CCN(c3ncc(Cl)cn3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL594428 202310 None 0 Human Binding pEC50 = 6.1 6.1 - 0
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 370 5 0 6 3.2 CCCn1c(CN2CCN(c3ncc(Cl)cn3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
24849789 202590 None 0 Human Binding pEC50 = 6.1 6.1 - 0
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 324 3 0 4 3.0 Cn1c(CN2CCN(c3ccccc3F)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL596270 202590 None 0 Human Binding pEC50 = 6.1 6.1 - 0
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 324 3 0 4 3.0 Cn1c(CN2CCN(c3ccccc3F)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
798232 202591 None 6 Human Binding pEC50 = 6.1 6.1 - 1
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 340 3 0 4 3.5 Cn1c(CN2CCN(c3ccc(Cl)cc3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
CHEMBL596271 202591 None 6 Human Binding pEC50 = 6.1 6.1 - 1
Positive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assayPositive modulation of human mGluR2 expressed in CHO cells co-expressing Ga16 G-protein assessed as glutamate-induced response by FLIPR assay
ChEMBL 340 3 0 4 3.5 Cn1c(CN2CCN(c3ccc(Cl)cc3)CC2)nc2ccccc21 10.1016/j.bmcl.2009.11.032
44578948 181727 None 0 Rat Binding pEC50 = 8.1 8.1 - 0
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 385 5 0 4 4.1 Cn1c(CN2C[C@@H]3C(COc4ccc(Cl)cc4F)[C@@H]3C2)nc2ccccc21 10.1016/j.bmcl.2008.09.026
CHEMBL477375 181727 None 0 Rat Binding pEC50 = 8.1 8.1 - 0
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 385 5 0 4 4.1 Cn1c(CN2C[C@@H]3C(COc4ccc(Cl)cc4F)[C@@H]3C2)nc2ccccc21 10.1016/j.bmcl.2008.09.026
71681823 90088 None 0 Human Binding pEC50 = 8.1 8.1 - 0
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 226 3 3 4 -0.2 [N-]=[N+]=N[C@@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]21 10.1021/jm4000165
CHEMBL2381644 90088 None 0 Human Binding pEC50 = 8.1 8.1 - 0
Agonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assayAgonist activity at human mGlu2 receptor expressed in golden Syrian hamster AV12 cells coexpressing EAAT1 after 20 mins by HTRF assay
ChEMBL 226 3 3 4 -0.2 [N-]=[N+]=N[C@@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]21 10.1021/jm4000165
66799669 82722 None 0 Rat Binding pEC50 = 7.1 7.1 - 0
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 457 7 1 4 5.5 COc1ccc(C(=O)O)cc1-c1cccc(COc2ccc3c(c2)CN(C2CCCC2)C3=O)c1 10.1021/jm3005306
CHEMBL2179631 82722 None 0 Rat Binding pEC50 = 7.1 7.1 - 0
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 457 7 1 4 5.5 COc1ccc(C(=O)O)cc1-c1cccc(COc2ccc3c(c2)CN(C2CCCC2)C3=O)c1 10.1021/jm3005306
53390432 82724 None 0 Rat Binding pEC50 = 7.1 7.1 - 0
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 487 8 1 5 5.5 COc1cc(C(=O)O)cc(OC)c1-c1cccc(COc2ccc3c(c2)CN(C2CCCC2)C3=O)c1 10.1021/jm3005306
CHEMBL2179633 82724 None 0 Rat Binding pEC50 = 7.1 7.1 - 0
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 487 8 1 5 5.5 COc1cc(C(=O)O)cc(OC)c1-c1cccc(COc2ccc3c(c2)CN(C2CCCC2)C3=O)c1 10.1021/jm3005306
50993964 57345 None 0 Rat Binding pEC50 = 7.1 7.1 - 0
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 447 7 1 3 5.7 O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(CC3CC3)C4=O)c2)ccc1Cl 10.1021/jm1012165
CHEMBL1651210 57345 None 0 Rat Binding pEC50 = 7.1 7.1 - 0
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 447 7 1 3 5.7 O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(CC3CC3)C4=O)c2)ccc1Cl 10.1021/jm1012165
89735530 138110 None 0 Human Binding pEC50 = 7.1 7.1 - 0
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 320 2 0 5 3.3 Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3cccc(C#N)c3)nc21 10.1016/j.bmcl.2016.01.021
CHEMBL3764820 138110 None 0 Human Binding pEC50 = 7.1 7.1 - 0
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 320 2 0 5 3.3 Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3cccc(C#N)c3)nc21 10.1016/j.bmcl.2016.01.021
164620998 185979 None 0 Rat Binding pEC50 = 7.1 7.1 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 432 10 2 5 5.4 Cc1c(OCCCCOc2ccc(C(=O)O)c(F)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
CHEMBL4868114 185979 None 0 Rat Binding pEC50 = 7.1 7.1 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 432 10 2 5 5.4 Cc1c(OCCCCOc2ccc(C(=O)O)c(F)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
89735654 138035 None 0 Human Binding pEC50 = 7.1 7.1 - 0
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 313 2 0 4 3.6 Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccccc3F)nc21 10.1016/j.bmcl.2016.01.021
CHEMBL3764024 138035 None 0 Human Binding pEC50 = 7.1 7.1 - 0
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 313 2 0 4 3.6 Cn1c(=O)n(CC(C)(C)C)c2ccc(-c3ccccc3F)nc21 10.1016/j.bmcl.2016.01.021
90643903 111946 None 0 Rat Binding pEC50 = 7.1 7.1 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 386 10 2 5 4.5 CCC(=O)c1ccc(OCCCCOc2ccc(C(=O)O)cc2C)c(C)c1O 10.1021/jm5000563
CHEMBL3287712 111946 None 0 Rat Binding pEC50 = 7.1 7.1 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 386 10 2 5 4.5 CCC(=O)c1ccc(OCCCCOc2ccc(C(=O)O)cc2C)c(C)c1O 10.1021/jm5000563
90643859 111911 None 0 Rat Binding pEC50 = 6.1 6.1 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 426 11 2 5 5.4 Cc1c(OCCCCOc2ccc(C(=O)O)cc2)ccc(C(=O)CC2CCCC2)c1O 10.1021/jm5000563
CHEMBL3287672 111911 None 0 Rat Binding pEC50 = 6.1 6.1 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 426 11 2 5 5.4 Cc1c(OCCCCOc2ccc(C(=O)O)cc2)ccc(C(=O)CC2CCCC2)c1O 10.1021/jm5000563
69092138 148823 None 0 Human Binding pEC50 = 7.1 7.1 - 0
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 464 6 1 4 5.8 Fc1ccc([C@H]2CC[C@H](NCc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
CHEMBL3940264 148823 None 0 Human Binding pEC50 = 7.1 7.1 - 0
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 464 6 1 4 5.8 Fc1ccc([C@H]2CC[C@H](NCc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
164612248 184996 None 0 Rat Binding pEC50 = 7.1 7.1 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 418 8 2 5 5.0 Cc1c(O[C@H](C)COc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
CHEMBL4852903 184996 None 0 Rat Binding pEC50 = 7.1 7.1 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 418 8 2 5 5.0 Cc1c(O[C@H](C)COc2ccc(F)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
11648510 63288 None 0 Human Binding pEC50 = 6.1 6.1 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 471 7 0 4 7.3 CC(C)C1Cc2cc(OCc3cccc(CSc4ccncc4)c3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
CHEMBL179171 63288 None 0 Human Binding pEC50 = 6.1 6.1 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 471 7 0 4 7.3 CC(C)C1Cc2cc(OCc3cccc(CSc4ccncc4)c3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
11712790 181362 None 0 Rat Binding pEC50 = 7.1 7.1 - 0
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 484 7 1 4 6.8 COc1ccc(-c2cccc(COc3cc4c(c(C)c3C)C(=O)C(C3CCCC3)C4)c2)cc1C(=O)O 10.1016/j.bmcl.2020.127212
CHEMBL4761801 181362 None 0 Rat Binding pEC50 = 7.1 7.1 - 0
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 484 7 1 4 6.8 COc1ccc(-c2cccc(COc3cc4c(c(C)c3C)C(=O)C(C3CCCC3)C4)c2)cc1C(=O)O 10.1016/j.bmcl.2020.127212
44578949 181649 None 0 Rat Binding pEC50 = 7.1 7.1 - 0
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 401 5 0 4 4.3 Cn1c(CN2C[C@@H]3C(COc4ccc(C(F)(F)F)cc4)[C@@H]3C2)nc2ccccc21 10.1016/j.bmcl.2008.09.026
CHEMBL476551 181649 None 0 Rat Binding pEC50 = 7.1 7.1 - 0
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 401 5 0 4 4.3 Cn1c(CN2C[C@@H]3C(COc4ccc(C(F)(F)F)cc4)[C@@H]3C2)nc2ccccc21 10.1016/j.bmcl.2008.09.026
25050845 184494 None 0 Rat Binding pEC50 = 7.1 7.1 - 0
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 368 5 0 5 3.4 Cn1c(CN2C[C@@H]3C(COc4cccc(Cl)c4)[C@@H]3C2)nc2cnccc21 10.1016/j.bmcl.2008.09.026
CHEMBL484578 184494 None 0 Rat Binding pEC50 = 7.1 7.1 - 0
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 368 5 0 5 3.4 Cn1c(CN2C[C@@H]3C(COc4cccc(Cl)c4)[C@@H]3C2)nc2cnccc21 10.1016/j.bmcl.2008.09.026
86691853 138161 None 0 Human Binding pEC50 = 7.1 7.1 - 0
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 339 3 1 5 3.2 Cc1ccc(CO)cc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C 10.1016/j.bmcl.2016.01.021
CHEMBL3765537 138161 None 0 Human Binding pEC50 = 7.1 7.1 - 0
Positive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assayPositive allosteric modulation of recombinant human mGluR2 expressed in CHO cells preincubated for 5 mins followed by stimulation with EC20 concentration of glutamate for 3 mins by FLIPR assay
ChEMBL 339 3 1 5 3.2 Cc1ccc(CO)cc1-c1ccc2c(n1)n(C)c(=O)n2CC(C)(C)C 10.1016/j.bmcl.2016.01.021
164609025 184547 None 0 Rat Binding pEC50 = 7.1 7.1 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 448 10 2 5 5.9 Cc1c(OCCCCOc2ccc(Cl)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
CHEMBL4846460 184547 None 0 Rat Binding pEC50 = 7.1 7.1 - 0
Positive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assayPositive allosteric modulator activity at rat mGlu2 receptor transfected in GIRK channel overexpressing cells assessed as potentiation of glutamate-induced response by thallium mobilization assay
ChEMBL 448 10 2 5 5.9 Cc1c(OCCCCOc2ccc(Cl)c(C(=O)O)c2)ccc(C(=O)CC(C)(C)C)c1O 10.1016/j.bmcl.2021.128342
10343566 66721 None 0 Human Binding pEC50 = 6.1 6.1 - 0
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 446 9 2 7 3.8 CC(=O)c1ccc(OCCCCOc2ccc(-c3nn[nH]n3)cc2)c(Br)c1O 10.1016/j.bmcl.2004.08.020
CHEMBL185529 66721 None 0 Human Binding pEC50 = 6.1 6.1 - 0
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 446 9 2 7 3.8 CC(=O)c1ccc(OCCCCOc2ccc(-c3nn[nH]n3)cc2)c(Br)c1O 10.1016/j.bmcl.2004.08.020
44335615 110122 None 0 Human Binding pEC50 = 7.1 7.1 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 460 9 0 6 3.7 CCOC(=O)C(C)(C)Oc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1 10.1016/j.bmcl.2004.04.017
CHEMBL323541 110122 None 0 Human Binding pEC50 = 7.1 7.1 - 0
Effective concentration against metabotropic glutamate receptor 2Effective concentration against metabotropic glutamate receptor 2
ChEMBL 460 9 0 6 3.7 CCOC(=O)C(C)(C)Oc1cccc(N(Cc2cccnc2)S(=O)(=O)CC(F)(F)F)c1 10.1016/j.bmcl.2004.04.017
71119170 148860 None 0 Human Binding pEC50 = 7.1 7.1 - 0
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 468 4 1 5 1.9 CN1c2nc(C3=CC4CN(C(=O)C(C)(C)O)CC4C3)ccc2N(CC2CC2(F)F)S1(=O)=O nan
CHEMBL3940610 148860 None 0 Human Binding pEC50 = 7.1 7.1 - 0
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 468 4 1 5 1.9 CN1c2nc(C3=CC4CN(C(=O)C(C)(C)O)CC4C3)ccc2N(CC2CC2(F)F)S1(=O)=O nan
66786069 156552 None 0 Human Binding pEC50 = 7.1 7.1 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cells assessed as cellular impedance measured for 20 mins with 15 sec time interval followed by 40 mins with 5 mins time interval and subsequently measured with 15 mins time interval in presence of endogenous glutamate levels by RTCAPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cells assessed as cellular impedance measured for 20 mins with 15 sec time interval followed by 40 mins with 5 mins time interval and subsequently measured with 15 mins time interval in presence of endogenous glutamate levels by RTCA
ChEMBL 451 5 0 5 5.6 FC(F)(F)c1c(-c2ccc(OC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
CHEMBL4067290 156552 None 0 Human Binding pEC50 = 7.1 7.1 - 1
Positive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cells assessed as cellular impedance measured for 20 mins with 15 sec time interval followed by 40 mins with 5 mins time interval and subsequently measured with 15 mins time interval in presence of endogenous glutamate levels by RTCAPositive allosteric modulation of human metabotropic glutamate receptor 2 expressed in CHOK1 cells assessed as cellular impedance measured for 20 mins with 15 sec time interval followed by 40 mins with 5 mins time interval and subsequently measured with 15 mins time interval in presence of endogenous glutamate levels by RTCA
ChEMBL 451 5 0 5 5.6 FC(F)(F)c1c(-c2ccc(OC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
11654949 47485 None 0 Human Binding pEC50 = 6.1 6.1 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 432 5 1 3 6.2 CC1(C2CCCC2)Cc2cc(OCc3ccc(C(=O)O)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
CHEMBL154542 47485 None 0 Human Binding pEC50 = 6.1 6.1 - 0
Binding affinity against metabotropic glutamate receptor 2Binding affinity against metabotropic glutamate receptor 2
ChEMBL 432 5 1 3 6.2 CC1(C2CCCC2)Cc2cc(OCc3ccc(C(=O)O)cc3)c(Cl)c(Cl)c2C1=O 10.1016/j.bmcl.2005.01.077
71136746 148688 None 0 Human Binding pEC50 = 8.0 8.0 - 0
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 421 3 0 7 3.1 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3ccon3)nc21 nan
CHEMBL3939174 148688 None 0 Human Binding pEC50 = 8.0 8.0 - 0
[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).[35S]-GTPγS Assay: The stimulation of [35S]-GTPγS binding is a common functional assay to monitor Gαi-coupled receptor in native and recombinant receptor membrane preparation. Membrane from cells stably expressing hmGlu2 CHO-K1 (50 μg) are incubated in a 96 well plate for 1 hour in the presence of GTPγS35 (0.05 nM), GDP (5 μM) and compounds. The reaction is stopped by rapid filtration over Unifilter GF/B plate (Packard, Bioscience, Meriden Conn.) using a 96-well cell harvester (Brandel Gaithersburg, Md.). The filter plates are counted using Topcount counter (Packard, Bioscience, Meriden Conn., USA). When compounds are evaluated as potentiators they are tested in the presence of glutamate (1 μM).
ChEMBL 421 3 0 7 3.1 Cn1c(=O)n(CC(C)(C)C)c2ccc(C3=CC4CCC3CN4C(=O)c3ccon3)nc21 nan
68107813 145079 None 0 Human Binding pEC50 = 8.0 8.0 - 0
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 450 5 0 4 5.4 Fc1cccc(F)c1C1CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1 10.1021/acs.jmedchem.6b00913
CHEMBL3910866 145079 None 0 Human Binding pEC50 = 8.0 8.0 - 0
Positive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting methodPositive allosteric modulation of human mGlu2 receptor expressed in CHO cell membranes assessed as potentiation of glutamate-induced effect incubated for 30 mins prior to [35S]GTPgamma addition measured after 30 mins by scintillation counting method
ChEMBL 450 5 0 4 5.4 Fc1cccc(F)c1C1CCN(Cc2ccn3c(CC4CC4)nnc3c2C(F)(F)F)CC1 10.1021/acs.jmedchem.6b00913
53390517 82725 None 0 Rat Binding pEC50 = 7.1 7.1 - 0
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 461 6 1 3 6.2 O=C(O)c1ccc(Cl)c(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)c1 10.1021/jm3005306
CHEMBL2179634 82725 None 0 Rat Binding pEC50 = 7.1 7.1 - 0
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 461 6 1 3 6.2 O=C(O)c1ccc(Cl)c(-c2cccc(COc3ccc4c(c3)CN(C3CCCC3)C4=O)c2)c1 10.1021/jm3005306
50993965 57346 None 0 Rat Binding pEC50 = 7.1 7.1 - 0
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 447 6 1 3 5.8 O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(C3CCC3)C4=O)c2)ccc1Cl 10.1021/jm1012165
CHEMBL1651211 57346 None 0 Rat Binding pEC50 = 7.1 7.1 - 0
Positive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channelsPositive allosteric modulation of rat mGluR2 expressed in HEK-293 cells assessed as thallium flux through GIRK channels
ChEMBL 447 6 1 3 5.8 O=C(O)c1cc(-c2cccc(COc3ccc4c(c3)CN(C3CCC3)C4=O)c2)ccc1Cl 10.1021/jm1012165
44395299 67071 None 0 Human Binding pEC50 = 6.0 6.0 - 0
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 424 11 2 7 4.4 CCCc1c(OC(C)CCCOc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2004.08.020
CHEMBL187151 67071 None 0 Human Binding pEC50 = 6.0 6.0 - 0
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 424 11 2 7 4.4 CCCc1c(OC(C)CCCOc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2004.08.020
162644103 183725 None 0 Rat Binding pEC50 = 7.0 7.0 - 0
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1106 25 6 12 9.8 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
CHEMBL4777845 183725 None 0 Rat Binding pEC50 = 7.0 7.0 - 0
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1106 25 6 12 9.8 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
CHEMBL4802343 183725 None 0 Rat Binding pEC50 = 7.0 7.0 - 0
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1106 25 6 12 9.8 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
10413231 125104 None 0 Human Binding pEC50 = 7.0 7.0 - 0
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 488 11 2 7 4.8 CC(C)CC(=O)c1ccc(OCCCCOc2ccc(-c3nn[nH]n3)cc2)c(Br)c1O 10.1016/j.bmcl.2004.08.020
CHEMBL364324 125104 None 0 Human Binding pEC50 = 7.0 7.0 - 0
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 488 11 2 7 4.8 CC(C)CC(=O)c1ccc(OCCCCOc2ccc(-c3nn[nH]n3)cc2)c(Br)c1O 10.1016/j.bmcl.2004.08.020
10070087 67258 None 0 Human Binding pEC50 = 6.0 6.0 - 0
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 409 11 3 7 4.0 CCCc1c(OCCCCNc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2004.08.020
CHEMBL187959 67258 None 0 Human Binding pEC50 = 6.0 6.0 - 0
Effective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assayEffective concentration for binding to human metabotropic glutamate receptor 2 as determined by GTPgammaS assay
ChEMBL 409 11 3 7 4.0 CCCc1c(OCCCCNc2ccc(-c3nn[nH]n3)cc2)ccc(C(C)=O)c1O 10.1016/j.bmcl.2004.08.020
162646759 183738 None 0 Rat Binding pEC50 = 7.0 7.0 - 0
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1148 28 6 12 11.0 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
CHEMBL4740929 183738 None 0 Rat Binding pEC50 = 7.0 7.0 - 0
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1148 28 6 12 11.0 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
CHEMBL4802473 183738 None 0 Rat Binding pEC50 = 7.0 7.0 - 0
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1148 28 6 12 11.0 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
90643874 111931 None 0 Rat Binding pEC50 = 7.0 7.0 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 434 11 2 5 5.5 Cc1c(OCCCCOc2ccc(C(=O)O)cc2Cl)ccc(C(=O)CC(C)C)c1O 10.1021/jm5000563
CHEMBL3287697 111931 None 0 Rat Binding pEC50 = 7.0 7.0 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 434 11 2 5 5.5 Cc1c(OCCCCOc2ccc(C(=O)O)cc2Cl)ccc(C(=O)CC(C)C)c1O 10.1021/jm5000563
44578903 181674 None 0 Rat Binding pEC50 = 6.0 6.0 - 0
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 359 5 0 4 3.7 c1ccc(OCC2[C@H]3CN(Cc4nc5cccc6c5n4CCC6)C[C@@H]23)cc1 10.1016/j.bmcl.2008.09.026
CHEMBL476790 181674 None 0 Rat Binding pEC50 = 6.0 6.0 - 0
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 359 5 0 4 3.7 c1ccc(OCC2[C@H]3CN(Cc4nc5cccc6c5n4CCC6)C[C@@H]23)cc1 10.1016/j.bmcl.2008.09.026
44578995 181672 None 0 Rat Binding pEC50 = 5.0 5.0 - 0
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 330 5 0 3 4.0 c1ccc(OCC2[C@H]3CN(Cc4cnc5ccccc5c4)C[C@@H]23)cc1 10.1016/j.bmcl.2008.09.026
CHEMBL476756 181672 None 0 Rat Binding pEC50 = 5.0 5.0 - 0
Activity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamateActivity at rat mGluR2 receptor expressed in HEK cells by FLIPR assay in presence of glutamate
ChEMBL 330 5 0 3 4.0 c1ccc(OCC2[C@H]3CN(Cc4cnc5ccccc5c4)C[C@@H]23)cc1 10.1016/j.bmcl.2008.09.026
90643890 111914 None 0 Rat Binding pEC50 = 6.0 6.0 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 398 11 1 4 5.5 Cc1c(OCCCCOc2ccccc2C(=O)O)ccc(C(=O)CC(C)C)c1C 10.1021/jm5000563
CHEMBL3287677 111914 None 0 Rat Binding pEC50 = 6.0 6.0 - 0
Positive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assayPositive allosteric modulation of rat mGluR2 receptor expressed in HEK293 cells assessed as potentiation of glutamate-induced thallium flux incubated for 2.5 mins prior to glutamate addition measured after 2.5 mins by GIRK assay
ChEMBL 398 11 1 4 5.5 Cc1c(OCCCCOc2ccccc2C(=O)O)ccc(C(=O)CC(C)C)c1C 10.1021/jm5000563
49822116 147080 None 14 Human Binding pEC50 = 6.0 6.0 - 1
Positive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assayPositive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assay
ChEMBL 451 5 0 5 4.3 Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
CHEMBL3926416 147080 None 14 Human Binding pEC50 = 6.0 6.0 - 1
Positive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assayPositive allosteric modulation at wild type human mGlu2 receptor L732A mutant expressed in CHO-K1 cells assessed as potentiation of glutamate-induced effect preincubated for 30 mins prior to glutamate challenge measured after 30 mins by [35S]GTP-gammaS binding assay
ChEMBL 451 5 0 5 4.3 Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
162666879 183839 None 0 Rat Binding pEC50 = 7.0 7.0 - 0
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1092 24 6 12 9.4 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
CHEMBL4786847 183839 None 0 Rat Binding pEC50 = 7.0 7.0 - 0
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1092 24 6 12 9.4 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
CHEMBL4803552 183839 None 0 Rat Binding pEC50 = 7.0 7.0 - 0
Positive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assayPositive allosteric modulation of rat mGlu2 receptor expressed in HEK293 cells coexpressing GIRK assessed as thallium influx in presence of EC20 glutamate by CODA-RET assay
ChEMBL 1092 24 6 12 9.4 COc1cc(NC(=O)c2ccccn2)ccc1NC(=O)c1ccc(NC(=O)COCC(=O)NCCCCNC(=O)COc2ccc(-c3cccc(COc4cc5c(c(C)c4C)C(=O)C(C4CCCC4)C5)c3)cc2C(=O)O)cc1Cl 10.1016/j.bmcl.2020.127212
53390837 82734 None 0 Rat Binding pEC50 = 6.0 6.0 - 0
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 506 6 0 5 6.8 CN(C)C(=O)c1cc(-c2cccc(COc3ccc4c(=O)n(C5CCCC5)sc4c3)c2)ccc1Cl 10.1021/jm3005306
CHEMBL2179645 82734 None 0 Rat Binding pEC50 = 6.0 6.0 - 0
Positive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assayPositive allosteric modulation activity at rat mGlu2R expressed in HEK293 cells co-expressing GIRK channels by thallium flux assay
ChEMBL 506 6 0 5 6.8 CN(C)C(=O)c1cc(-c2cccc(COc3ccc4c(=O)n(C5CCCC5)sc4c3)c2)ccc1Cl 10.1021/jm3005306
89554832 142888 None 0 Human Binding pIC50 = 8 8.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 484 7 2 6 4.4 CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)cc4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F nan
CHEMBL3892899 142888 None 0 Human Binding pIC50 = 8 8.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 484 7 2 6 4.4 CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)cc4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F nan
71565964 144338 None 0 Human Binding pIC50 = 8 8.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 429 7 1 4 5.2 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4ccc(CF)nc4)ccc23)cc1 nan
CHEMBL3904730 144338 None 0 Human Binding pIC50 = 8 8.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 429 7 1 4 5.2 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4ccc(CF)nc4)ccc23)cc1 nan
124201729 146650 None 0 Human Binding pIC50 = 8 8.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 421 5 2 4 4.5 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc([C@@H](O)Cc3ccc(Cl)nc3)cc2n1 nan
CHEMBL3922857 146650 None 0 Human Binding pIC50 = 8 8.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 421 5 2 4 4.5 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc([C@@H](O)Cc3ccc(Cl)nc3)cc2n1 nan
89554927 146970 None 0 Human Binding pIC50 = 8 8.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 406 5 1 5 3.7 COc1ncc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2F)cn1 nan
CHEMBL3925389 146970 None 0 Human Binding pIC50 = 8 8.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 406 5 1 5 3.7 COc1ncc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2F)cn1 nan
71566125 147138 None 0 Human Binding pIC50 = 8 8.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 411 6 1 4 5.1 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4ccc(C)nc4)ccc23)cc1 nan
CHEMBL3926942 147138 None 0 Human Binding pIC50 = 8 8.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 411 6 1 4 5.1 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4ccc(C)nc4)ccc23)cc1 nan
89554857 148186 None 0 Human Binding pIC50 = 8 8.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 520 7 2 6 4.7 CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)c(F)c4)cc(C(N)=O)nc3c2F)cn1)C(F)(F)F nan
CHEMBL3935153 148186 None 0 Human Binding pIC50 = 8 8.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 520 7 2 6 4.7 CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)c(F)c4)cc(C(N)=O)nc3c2F)cn1)C(F)(F)F nan
71565965 148372 None 0 Human Binding pIC50 = 8 8.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 447 7 1 4 5.4 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4ccc(CF)nc4)ccc23)c(F)c1 nan
CHEMBL3936681 148372 None 0 Human Binding pIC50 = 8 8.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 447 7 1 4 5.4 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4ccc(CF)nc4)ccc23)c(F)c1 nan
71566127 148725 None 0 Human Binding pIC50 = 8 8.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 415 6 1 4 4.9 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4)ccc23)c(F)c1 nan
CHEMBL3939455 148725 None 0 Human Binding pIC50 = 8 8.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 415 6 1 4 4.9 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4)ccc23)c(F)c1 nan
89554768 149539 None 0 Human Binding pIC50 = 8 8.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 397 6 1 4 4.8 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4)ccc23)cc1 nan
CHEMBL3946016 149539 None 0 Human Binding pIC50 = 8 8.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 397 6 1 4 4.8 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4)ccc23)cc1 nan
71566207 150442 None 0 Human Binding pIC50 = 8 8.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 388 5 1 5 3.5 COc1ncc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 nan
CHEMBL3953157 150442 None 0 Human Binding pIC50 = 8 8.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 388 5 1 5 3.5 COc1ncc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 nan
89554874 153560 None 0 Human Binding pIC50 = 8 8.0 - 1
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 371 5 1 3 4.3 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3cccnc3)cc2n1 nan
CHEMBL3979547 153560 None 0 Human Binding pIC50 = 8 8.0 - 1
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 371 5 1 3 4.3 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3cccnc3)cc2n1 nan
89554726 160805 None 0 Human Binding pIC50 = 8 8.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 446 4 2 4 3.9 C[C@@H]1CNC(C(F)(F)F)CN1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
CHEMBL4113710 160805 None 0 Human Binding pIC50 = 8 8.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 446 4 2 4 3.9 C[C@@H]1CNC(C(F)(F)F)CN1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
156012009 177462 None 0 Human Binding pIC50 = 8 8.0 - 0
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 472 6 2 5 4.5 CC[C@@](O)(c1cnn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)c1)C(F)(F)F 10.1016/j.bmcl.2020.127066
CHEMBL4637618 177462 None 0 Human Binding pIC50 = 8 8.0 - 0
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 472 6 2 5 4.5 CC[C@@](O)(c1cnn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)c1)C(F)(F)F 10.1016/j.bmcl.2020.127066
22317767 56306 None 0 Rat Binding pIC50 = 8 8.0 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 437 3 1 3 6.7 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(C(C)C)nc3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1629847 56306 None 0 Rat Binding pIC50 = 8 8.0 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 437 3 1 3 6.7 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(C(C)C)nc3)c1)=N2 10.1016/j.bmcl.2010.09.125
11269030 56320 None 0 Rat Binding pIC50 = 8 8.0 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 381 2 1 3 5.2 O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(C(F)(F)F)cc2N1 10.1016/j.bmcl.2010.09.125
CHEMBL1629861 56320 None 0 Rat Binding pIC50 = 8 8.0 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 381 2 1 3 5.2 O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(C(F)(F)F)cc2N1 10.1016/j.bmcl.2010.09.125
22317741 56428 None 0 Rat Binding pIC50 = 8 8.0 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 435 3 1 3 6.4 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C4CC4)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631863 56428 None 0 Rat Binding pIC50 = 8 8.0 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 435 3 1 3 6.4 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C4CC4)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
22317279 56430 None 0 Rat Binding pIC50 = 8 8.0 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 463 3 1 3 7.2 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C4CCCC4)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631865 56430 None 0 Rat Binding pIC50 = 8 8.0 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 463 3 1 3 7.2 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C4CCCC4)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
71566440 143729 None 0 Human Binding pIC50 = 7 7.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 300 2 1 2 3.8 NC(=O)c1cc(-c2ccc(F)cc2Cl)c2ccccc2n1 nan
CHEMBL3899883 143729 None 0 Human Binding pIC50 = 7 7.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 300 2 1 2 3.8 NC(=O)c1cc(-c2ccc(F)cc2Cl)c2ccccc2n1 nan
22224818 146766 None 0 Rat Binding pIC50 = 6.0 6.0 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 462 2 1 4 3.9 CN1CCN(C(=O)c2cccc(C3=Nc4ccc(C#Cc5ccccc5)cc4NC(=O)C3)c2)CC1 10.1016/j.bmcl.2007.10.026
CHEMBL392381 146766 None 0 Rat Binding pIC50 = 6.0 6.0 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 462 2 1 4 3.9 CN1CCN(C(=O)c2cccc(C3=Nc4ccc(C#Cc5ccccc5)cc4NC(=O)C3)c2)CC1 10.1016/j.bmcl.2007.10.026
71565597 154045 None 0 Human Binding pIC50 = 7.0 7.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 399 4 1 4 2.7 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCS3(=O)=O)cc2n1 nan
CHEMBL3983624 154045 None 0 Human Binding pIC50 = 7.0 7.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 399 4 1 4 2.7 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCS3(=O)=O)cc2n1 nan
9905849 206511 None 0 Rat Binding pIC50 = 6.0 6.0 - 0
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 337 4 0 4 4.9 Clc1ccc(/C(=C/n2cncn2)OC2CCCCC2)c(Cl)c1 10.1016/s0960-894x(99)00346-7
CHEMBL69970 206511 None 0 Rat Binding pIC50 = 6.0 6.0 - 0
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 337 4 0 4 4.9 Clc1ccc(/C(=C/n2cncn2)OC2CCCCC2)c(Cl)c1 10.1016/s0960-894x(99)00346-7
71565672 151353 None 0 Human Binding pIC50 = 7.0 7.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 378 4 1 3 3.0 CN1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O nan
CHEMBL3960294 151353 None 0 Human Binding pIC50 = 7.0 7.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 378 4 1 3 3.0 CN1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O nan
89554824 152626 None 0 Human Binding pIC50 = 6.0 6.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 464 5 1 6 4.3 CC(C)c1ncc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)s1 nan
CHEMBL3971590 152626 None 0 Human Binding pIC50 = 6.0 6.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 464 5 1 6 4.3 CC(C)c1ncc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)s1 nan
89554770 144178 None 0 Human Binding pIC50 = 8.0 8.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 446 4 2 4 3.9 C[C@H]1CNC(C(F)(F)F)CN1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
CHEMBL3903459 144178 None 0 Human Binding pIC50 = 8.0 8.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 446 4 2 4 3.9 C[C@H]1CNC(C(F)(F)F)CN1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
89554787 149997 None 0 Human Binding pIC50 = 8.0 8.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 455 5 1 6 3.4 NC(=O)c1cc(-c2cnn(C(F)F)c2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1 nan
CHEMBL3949371 149997 None 0 Human Binding pIC50 = 8.0 8.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 455 5 1 6 3.4 NC(=O)c1cc(-c2cnn(C(F)F)c2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1 nan
89554900 151245 None 0 Human Binding pIC50 = 8.0 8.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 434 6 1 5 4.2 COc1c(F)cc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)cc1F nan
CHEMBL3959588 151245 None 0 Human Binding pIC50 = 8.0 8.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 434 6 1 5 4.2 COc1c(F)cc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)cc1F nan
89554749 152094 None 0 Human Binding pIC50 = 8.0 8.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 433 6 2 5 4.3 COc1ccc(-c2cc(C(N)=O)nc3cc(C(O)Cc4ccc(Cl)nc4)ccc23)cc1 nan
CHEMBL3966866 152094 None 0 Human Binding pIC50 = 8.0 8.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 433 6 2 5 4.3 COc1ccc(-c2cc(C(N)=O)nc3cc(C(O)Cc4ccc(Cl)nc4)ccc23)cc1 nan
89554828 160311 None 0 Human Binding pIC50 = 8.0 8.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 447 4 1 6 3.3 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4C[C@H](C(F)(F)F)OC(C)(C)C4)ccc23)cn1 nan
CHEMBL4109697 160311 None 0 Human Binding pIC50 = 8.0 8.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 447 4 1 6 3.3 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4C[C@H](C(F)(F)F)OC(C)(C)C4)ccc23)cn1 nan
89545222 160472 None 4 Human Binding pIC50 = 8.0 8.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 433 4 1 6 2.9 C[C@@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1 nan
CHEMBL4111091 160472 None 4 Human Binding pIC50 = 8.0 8.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 433 4 1 6 2.9 C[C@@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1 nan
10115228 96226 None 0 Rat Binding pIC50 = 8.0 8.0 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 456 5 1 6 4.8 CC(C)CN(C)c1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
CHEMBL260642 96226 None 0 Rat Binding pIC50 = 8.0 8.0 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 456 5 1 6 4.8 CC(C)CN(C)c1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
57459488 83937 None 0 Human Binding pIC50 = 8.0 8.0 - 0
Displacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation countingDisplacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation counting
ChEMBL 414 5 0 5 4.9 COc1ccc(F)cc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm300912k
CHEMBL2206441 83937 None 0 Human Binding pIC50 = 8.0 8.0 - 0
Displacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation countingDisplacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation counting
ChEMBL 414 5 0 5 4.9 COc1ccc(F)cc1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm300912k
57459494 83938 None 0 Human Binding pIC50 = 8.0 8.0 - 0
Displacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation countingDisplacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation counting
ChEMBL 414 5 0 5 4.9 COc1cccc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm300912k
CHEMBL2206442 83938 None 0 Human Binding pIC50 = 8.0 8.0 - 0
Displacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation countingDisplacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation counting
ChEMBL 414 5 0 5 4.9 COc1cccc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm300912k
10428048 3361 None 25 Rat Binding pIC50 = 7.0 7.0 - 1
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 351 4 0 4 5.3 Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl 10.1016/s0960-894x(99)00346-7
3955 3361 None 25 Rat Binding pIC50 = 7.0 7.0 - 1
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 351 4 0 4 5.3 Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl 10.1016/s0960-894x(99)00346-7
CHEMBL305406 3361 None 25 Rat Binding pIC50 = 7.0 7.0 - 1
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 351 4 0 4 5.3 Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl 10.1016/s0960-894x(99)00346-7
71566276 144512 None 0 Human Binding pIC50 = 7.0 7.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 381 5 1 5 3.1 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCCCC4CF)ccc23)cn1 nan
CHEMBL3906311 144512 None 0 Human Binding pIC50 = 7.0 7.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 381 5 1 5 3.1 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCCCC4CF)ccc23)cn1 nan
117642007 145819 None 0 Human Binding pIC50 = 7.0 7.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 474 6 2 7 3.3 CC[C@](O)(c1cn(Cc2ccc3c(-c4cccnc4F)cc(C(N)=O)nc3c2)nn1)C(F)(F)F nan
CHEMBL3916486 145819 None 0 Human Binding pIC50 = 7.0 7.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 474 6 2 7 3.3 CC[C@](O)(c1cn(Cc2ccc3c(-c4cccnc4F)cc(C(N)=O)nc3c2)nn1)C(F)(F)F nan
89554827 153417 None 0 Human Binding pIC50 = 6.9 6.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 417 4 1 5 3.5 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCC(C(F)(F)F)CC4)ccc23)cn1 nan
CHEMBL3978247 153417 None 0 Human Binding pIC50 = 6.9 6.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 417 4 1 5 3.5 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCC(C(F)(F)F)CC4)ccc23)cn1 nan
89554725 160919 None 0 Human Binding pIC50 = 6.9 6.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 378 4 2 4 2.9 C[C@@H]1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CCN1 nan
CHEMBL4114602 160919 None 0 Human Binding pIC50 = 6.9 6.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 378 4 2 4 2.9 C[C@@H]1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CCN1 nan
44309100 102686 None 0 Rat Binding pIC50 = 4.9 4.9 - 0
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 297 4 0 4 4.0 CC(C)O/C(=C\n1cncn1)c1ccc(Cl)cc1Cl 10.1016/s0960-894x(99)00346-7
CHEMBL304285 102686 None 0 Rat Binding pIC50 = 4.9 4.9 - 0
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 297 4 0 4 4.0 CC(C)O/C(=C\n1cncn1)c1ccc(Cl)cc1Cl 10.1016/s0960-894x(99)00346-7
89554830 151959 None 0 Human Binding pIC50 = 5.9 5.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 405 4 2 5 2.5 NC(=O)c1cc(-c2cn[nH]c2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1 nan
CHEMBL3965612 151959 None 0 Human Binding pIC50 = 5.9 5.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 405 4 2 5 2.5 NC(=O)c1cc(-c2cn[nH]c2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1 nan
89554917 143223 None 0 Human Binding pIC50 = 6.9 6.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 406 5 2 4 3.6 CC(C)C1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CCN1 nan
CHEMBL3895775 143223 None 0 Human Binding pIC50 = 6.9 6.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 406 5 2 4 3.6 CC(C)C1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CCN1 nan
89554812 144664 None 0 Human Binding pIC50 = 6.9 6.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 395 4 3 5 2.4 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC(O)(O)CC3)cc2n1 nan
CHEMBL3907626 144664 None 0 Human Binding pIC50 = 6.9 6.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 395 4 3 5 2.4 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC(O)(O)CC3)cc2n1 nan
89554781 160087 None 0 Human Binding pIC50 = 6.9 6.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 367 4 1 3 3.7 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CC[C@@H](F)C3)cc2n1 nan
CHEMBL4107730 160087 None 0 Human Binding pIC50 = 6.9 6.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 367 4 1 3 3.7 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CC[C@@H](F)C3)cc2n1 nan
53320741 56431 None 0 Rat Binding pIC50 = 6.9 6.9 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 471 3 1 3 7.2 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(-c4ccccc4)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631866 56431 None 0 Rat Binding pIC50 = 6.9 6.9 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 471 3 1 3 7.2 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(-c4ccccc4)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
71566277 142852 None 0 Human Binding pIC50 = 7.9 7.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 451 5 1 5 4.6 Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cc(C5CC5)nc(C(F)(F)F)c4)ccc23)cn1 nan
CHEMBL3892604 142852 None 0 Human Binding pIC50 = 7.9 7.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 451 5 1 5 4.6 Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cc(C5CC5)nc(C(F)(F)F)c4)ccc23)cn1 nan
71566125 147138 None 0 Human Binding pIC50 = 7.9 7.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 411 6 1 4 5.1 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4ccc(C)nc4)ccc23)cc1 nan
CHEMBL3926942 147138 None 0 Human Binding pIC50 = 7.9 7.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 411 6 1 4 5.1 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4ccc(C)nc4)ccc23)cc1 nan
89554755 151957 None 0 Human Binding pIC50 = 7.9 7.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 411 4 1 4 3.4 NC(=O)c1cc(-c2ccc(F)cc2Cl)c2ccc(CN3C(=O)CCC3=O)cc2n1 nan
CHEMBL3965606 151957 None 0 Human Binding pIC50 = 7.9 7.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 411 4 1 4 3.4 NC(=O)c1cc(-c2ccc(F)cc2Cl)c2ccc(CN3C(=O)CCC3=O)cc2n1 nan
89554749 152094 None 0 Human Binding pIC50 = 7.9 7.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 433 6 2 5 4.3 COc1ccc(-c2cc(C(N)=O)nc3cc(C(O)Cc4ccc(Cl)nc4)ccc23)cc1 nan
CHEMBL3966866 152094 None 0 Human Binding pIC50 = 7.9 7.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 433 6 2 5 4.3 COc1ccc(-c2cc(C(N)=O)nc3cc(C(O)Cc4ccc(Cl)nc4)ccc23)cc1 nan
89554734 160255 None 0 Human Binding pIC50 = 7.9 7.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 419 4 1 6 2.5 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCO[C@@H](C(F)(F)F)C4)ccc23)cn1 nan
CHEMBL4109210 160255 None 0 Human Binding pIC50 = 7.9 7.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 419 4 1 6 2.5 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCO[C@@H](C(F)(F)F)C4)ccc23)cn1 nan
22224657 96225 None 0 Rat Binding pIC50 = 7.9 7.9 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 396 3 1 4 5.1 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccccc3F)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL260636 96225 None 0 Rat Binding pIC50 = 7.9 7.9 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 396 3 1 4 5.1 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccccc3F)cc2N1 10.1016/j.bmcl.2008.02.076
18548739 160459 None 0 Rat Binding pIC50 = 7.9 7.9 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 384 2 1 4 4.7 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2008.02.076
CHEMBL411095 160459 None 0 Rat Binding pIC50 = 7.9 7.9 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 384 2 1 4 4.7 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2008.02.076
156016312 177838 None 0 Human Binding pIC50 = 7.9 7.9 - 0
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 487 6 2 6 4.5 CC[C@@](O)(c1cn(C(C)c2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
CHEMBL4642428 177838 None 0 Human Binding pIC50 = 7.9 7.9 - 0
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 487 6 2 6 4.5 CC[C@@](O)(c1cn(C(C)c2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
22317847 56426 None 0 Rat Binding pIC50 = 7.9 7.9 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 420 2 1 4 5.4 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C#N)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631861 56426 None 0 Rat Binding pIC50 = 7.9 7.9 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 420 2 1 4 5.4 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C#N)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
9952648 96361 None 0 Rat Binding pIC50 = 7.9 7.9 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 397 3 1 5 4.5 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1 10.1016/j.bmcl.2010.09.125
CHEMBL261288 96361 None 0 Rat Binding pIC50 = 7.9 7.9 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 397 3 1 5 4.5 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1 10.1016/j.bmcl.2010.09.125
18548739 160459 None 0 Rat Binding pIC50 = 7.9 7.9 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 384 2 1 4 4.7 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL411095 160459 None 0 Rat Binding pIC50 = 7.9 7.9 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 384 2 1 4 4.7 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2010.09.125
89554801 142951 None 0 Human Binding pIC50 = 6.9 6.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 378 4 2 4 2.9 C[C@H]1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CCN1 nan
CHEMBL3893351 142951 None 0 Human Binding pIC50 = 6.9 6.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 378 4 2 4 2.9 C[C@H]1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CCN1 nan
18548785 56422 None 0 Rat Binding pIC50 = 6.9 6.9 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 415 3 2 6 3.6 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3nncc3CO)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631857 56422 None 0 Rat Binding pIC50 = 6.9 6.9 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 415 3 2 6 3.6 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3nncc3CO)c1)=N2 10.1016/j.bmcl.2010.09.125
44309123 206328 None 0 Rat Binding pIC50 = 5.9 5.9 - 0
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 365 4 0 4 5.7 Clc1ccc(/C(=C/n2cncn2)OC2CCCCCCC2)c(Cl)c1 10.1016/s0960-894x(99)00346-7
CHEMBL68739 206328 None 0 Rat Binding pIC50 = 5.9 5.9 - 0
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 365 4 0 4 5.7 Clc1ccc(/C(=C/n2cncn2)OC2CCCCCCC2)c(Cl)c1 10.1016/s0960-894x(99)00346-7
71565668 150507 None 0 Human Binding pIC50 = 6.9 6.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 365 4 1 4 3.1 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCOC3=O)cc2n1 nan
CHEMBL3953821 150507 None 0 Human Binding pIC50 = 6.9 6.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 365 4 1 4 3.1 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCOC3=O)cc2n1 nan
71566518 152377 None 0 Human Binding pIC50 = 6.9 6.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 280 2 1 2 3.4 Cc1ccc(-c2cc(C(N)=O)nc3ccccc23)c(F)c1 nan
CHEMBL3969392 152377 None 0 Human Binding pIC50 = 6.9 6.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 280 2 1 2 3.4 Cc1ccc(-c2cc(C(N)=O)nc3ccccc23)c(F)c1 nan
71566202 152458 None 0 Human Binding pIC50 = 6.9 6.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 377 3 1 3 3.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(C(=O)N3CCCCC3)cc2n1 nan
CHEMBL3970177 152458 None 0 Human Binding pIC50 = 6.9 6.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 377 3 1 3 3.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(C(=O)N3CCCCC3)cc2n1 nan
53323293 56310 None 0 Rat Binding pIC50 = 6.9 6.9 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 396 2 1 4 4.9 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cccnn3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1629851 56310 None 0 Rat Binding pIC50 = 6.9 6.9 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 396 2 1 4 4.9 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cccnn3)c1)=N2 10.1016/j.bmcl.2010.09.125
71565594 143114 None 0 Human Binding pIC50 = 6.9 6.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 395 4 2 4 4.2 CC(C)(C)OC(=O)NCc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
CHEMBL3894815 143114 None 0 Human Binding pIC50 = 6.9 6.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 395 4 2 4 4.2 CC(C)(C)OC(=O)NCc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
123632099 143489 None 0 Human Binding pIC50 = 7.9 7.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 426 6 1 4 4.9 [C-]#[N+]c1ccc(CCc2ccc3c(-c4ccc(OC)cc4F)cc(C(N)=O)nc3c2)cn1 nan
CHEMBL3897968 143489 None 0 Human Binding pIC50 = 7.9 7.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 426 6 1 4 4.9 [C-]#[N+]c1ccc(CCc2ccc3c(-c4ccc(OC)cc4F)cc(C(N)=O)nc3c2)cn1 nan
89554871 143663 None 0 Human Binding pIC50 = 7.9 7.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 435 4 1 5 3.6 Cn1cc(-c2cc(C(N)=O)nc3c(F)c(CN4CCCC(C(F)(F)F)C4)ccc23)cn1 nan
CHEMBL3899261 143663 None 0 Human Binding pIC50 = 7.9 7.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 435 4 1 5 3.6 Cn1cc(-c2cc(C(N)=O)nc3c(F)c(CN4CCCC(C(F)(F)F)C4)ccc23)cn1 nan
71565883 147655 None 0 Human Binding pIC50 = 7.9 7.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 407 5 1 6 3.1 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCSC(C5CC5)C4)ccc23)cn1 nan
CHEMBL3930893 147655 None 0 Human Binding pIC50 = 7.9 7.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 407 5 1 6 3.1 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCSC(C5CC5)C4)ccc23)cn1 nan
89554967 148767 None 0 Human Binding pIC50 = 7.9 7.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 410 4 0 5 3.6 COC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)c(F)c2n1 nan
CHEMBL3939827 148767 None 0 Human Binding pIC50 = 7.9 7.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 410 4 0 5 3.6 COC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)c(F)c2n1 nan
89554841 148984 None 0 Human Binding pIC50 = 7.9 7.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 382 4 1 4 4.0 N#Cc1ccc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 nan
CHEMBL3941663 148984 None 0 Human Binding pIC50 = 7.9 7.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 382 4 1 4 4.0 N#Cc1ccc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 nan
89554833 160889 None 0 Human Binding pIC50 = 7.9 7.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 450 4 1 6 3.9 Cc1cc(-c2cc(C(N)=O)nc3cc(CN4C[C@@H](C)O[C@@H](C(F)(F)F)C4)ccc23)sn1 nan
CHEMBL4114374 160889 None 0 Human Binding pIC50 = 7.9 7.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 450 4 1 6 3.9 Cc1cc(-c2cc(C(N)=O)nc3cc(CN4C[C@@H](C)O[C@@H](C(F)(F)F)C4)ccc23)sn1 nan
89554925 160905 None 0 Human Binding pIC50 = 7.9 7.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 469 5 1 6 3.7 C[C@@H]1CN(Cc2ccc3c(-c4cnn(C(F)F)c4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1 nan
CHEMBL4114497 160905 None 0 Human Binding pIC50 = 7.9 7.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 469 5 1 6 3.7 C[C@@H]1CN(Cc2ccc3c(-c4cnn(C(F)F)c4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1 nan
9909080 155372 None 0 Rat Binding pIC50 = 7.9 7.9 - 0
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 402 2 1 4 4.7 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C#Cc3ccccc3)cc2N1 10.1016/j.bmcl.2007.12.005
CHEMBL402886 155372 None 0 Rat Binding pIC50 = 7.9 7.9 - 0
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 402 2 1 4 4.7 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C#Cc3ccccc3)cc2N1 10.1016/j.bmcl.2007.12.005
156015264 177647 None 0 Human Binding pIC50 = 7.9 7.9 - 0
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 473 6 2 6 3.9 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
CHEMBL4640203 177647 None 0 Human Binding pIC50 = 7.9 7.9 - 0
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 473 6 2 6 3.9 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
22317724 56304 None 0 Rat Binding pIC50 = 7.9 7.9 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 409 2 1 3 5.8 Cc1ccc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cn1 10.1016/j.bmcl.2010.09.125
CHEMBL1629845 56304 None 0 Rat Binding pIC50 = 7.9 7.9 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 409 2 1 3 5.8 Cc1ccc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cn1 10.1016/j.bmcl.2010.09.125
11212447 56433 None 0 Rat Binding pIC50 = 7.9 7.9 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 425 3 2 4 5.0 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(CO)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631868 56433 None 0 Rat Binding pIC50 = 7.9 7.9 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 425 3 2 4 5.0 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(CO)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
22317620 56434 None 0 Rat Binding pIC50 = 7.9 7.9 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 439 4 1 4 5.7 COCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
CHEMBL1631869 56434 None 0 Rat Binding pIC50 = 7.9 7.9 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 439 4 1 4 5.7 COCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
53326017 56437 None 0 Rat Binding pIC50 = 7.9 7.9 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 425 3 1 4 5.5 COc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
CHEMBL1631872 56437 None 0 Rat Binding pIC50 = 7.9 7.9 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 425 3 1 4 5.5 COc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
44450454 96173 None 0 Rat Binding pIC50 = 6.9 6.9 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 381 2 1 5 3.5 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(Br)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL260343 96173 None 0 Rat Binding pIC50 = 6.9 6.9 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 381 2 1 5 3.5 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(Br)cc2N1 10.1016/j.bmcl.2008.02.076
11347391 66873 None 0 Rat Binding pIC50 = 6.9 6.9 2 2
Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells
ChEMBL 309 5 3 4 0.8 N[C@@]1(C(=O)O)[C@H](OCc2ccccc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL186214 66873 None 0 Rat Binding pIC50 = 6.9 6.9 2 2
Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells
ChEMBL 309 5 3 4 0.8 N[C@@]1(C(=O)O)[C@H](OCc2ccccc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
71566520 144636 None 0 Human Binding pIC50 = 6.9 6.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 287 2 1 3 3.2 Cc1ccc(-c2cc(C(N)=O)nc3ccccc23)c(C#N)c1 nan
CHEMBL3907349 144636 None 0 Human Binding pIC50 = 6.9 6.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 287 2 1 3 3.2 Cc1ccc(-c2cc(C(N)=O)nc3ccccc23)c(C#N)c1 nan
89554899 147608 None 0 Human Binding pIC50 = 6.9 6.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 364 4 2 4 2.5 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNCC3)cc2n1 nan
CHEMBL3930631 147608 None 0 Human Binding pIC50 = 6.9 6.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 364 4 2 4 2.5 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNCC3)cc2n1 nan
89554784 142838 None 0 Human Binding pIC50 = 6.9 6.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 407 5 1 5 3.3 COC(=O)[C@@H]1CCCN1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
CHEMBL3892501 142838 None 0 Human Binding pIC50 = 6.9 6.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 407 5 1 5 3.3 COC(=O)[C@@H]1CCCN1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
156010547 177269 None 0 Human Binding pIC50 = 5.9 5.9 - 0
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 280 1 1 4 2.4 O=c1[nH]nc2nc(-c3ccc(F)cc3)c3ccccc3n12 10.1016/j.bmcl.2020.127066
CHEMBL4634351 177269 None 0 Human Binding pIC50 = 5.9 5.9 - 0
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 280 1 1 4 2.4 O=c1[nH]nc2nc(-c3ccc(F)cc3)c3ccccc3n12 10.1016/j.bmcl.2020.127066
117642134 147148 None 0 Human Binding pIC50 = 6.9 6.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 379 5 1 4 3.4 CO[C@H]1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1 nan
CHEMBL3927029 147148 None 0 Human Binding pIC50 = 6.9 6.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 379 5 1 4 3.4 CO[C@H]1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1 nan
44309303 206521 None 0 Rat Binding pIC50 = 5.9 5.9 - 0
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 351 4 0 4 5.0 FC(F)(F)c1ccc(/C(=C/n2cncn2)OC2CCCCCC2)cc1 10.1016/s0960-894x(99)00346-7
CHEMBL70026 206521 None 0 Rat Binding pIC50 = 5.9 5.9 - 0
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 351 4 0 4 5.0 FC(F)(F)c1ccc(/C(=C/n2cncn2)OC2CCCCCC2)cc1 10.1016/s0960-894x(99)00346-7
117644742 147722 None 0 Human Binding pIC50 = 6.9 6.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 296 3 1 3 3.1 COc1ccc(-c2cc(C(N)=O)nc3ccccc23)c(F)c1 nan
CHEMBL3931394 147722 None 0 Human Binding pIC50 = 6.9 6.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 296 3 1 3 3.1 COc1ccc(-c2cc(C(N)=O)nc3ccccc23)c(F)c1 nan
89554852 148226 None 0 Human Binding pIC50 = 7.9 7.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 432 4 2 4 3.5 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(C(F)(F)F)C3)cc2n1 nan
CHEMBL3935453 148226 None 0 Human Binding pIC50 = 7.9 7.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 432 4 2 4 3.5 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(C(F)(F)F)C3)cc2n1 nan
89554870 148327 None 0 Human Binding pIC50 = 7.9 7.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 405 5 1 6 3.2 COc1cc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2F)cc(C)n1 nan
CHEMBL3936247 148327 None 0 Human Binding pIC50 = 7.9 7.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 405 5 1 6 3.2 COc1cc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2F)cc(C)n1 nan
71566126 148870 None 0 Human Binding pIC50 = 7.9 7.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 430 6 2 5 4.5 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4N)ccc23)c(F)c1 nan
CHEMBL3940665 148870 None 0 Human Binding pIC50 = 7.9 7.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 430 6 2 5 4.5 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4N)ccc23)c(F)c1 nan
89554745 149678 None 0 Human Binding pIC50 = 7.9 7.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 401 5 2 4 4.1 Cc1ccc(CC(O)c2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 nan
CHEMBL3946940 149678 None 0 Human Binding pIC50 = 7.9 7.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 401 5 2 4 4.1 Cc1ccc(CC(O)c2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 nan
71566207 150442 None 0 Human Binding pIC50 = 7.9 7.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 388 5 1 5 3.5 COc1ncc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 nan
CHEMBL3953157 150442 None 0 Human Binding pIC50 = 7.9 7.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 388 5 1 5 3.5 COc1ncc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 nan
89554909 160428 None 0 Human Binding pIC50 = 7.9 7.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 468 5 1 6 4.1 C[C@@H]1CN(Cc2ccc3c(-c4cnc(CF)s4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1 nan
CHEMBL4110690 160428 None 0 Human Binding pIC50 = 7.9 7.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 468 5 1 6 4.1 C[C@@H]1CN(Cc2ccc3c(-c4cnc(CF)s4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1 nan
89554960 160809 None 0 Human Binding pIC50 = 7.9 7.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 452 4 0 7 3.3 COC(=O)c1cc(-c2cnn(C)c2)c2ccc(CN3CCO[C@@H](C(F)(F)F)C3)c(F)c2n1 nan
CHEMBL4113735 160809 None 0 Human Binding pIC50 = 7.9 7.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 452 4 0 7 3.3 COC(=O)c1cc(-c2cnn(C)c2)c2ccc(CN3CCO[C@@H](C(F)(F)F)C3)c(F)c2n1 nan
22317185 56307 None 0 Rat Binding pIC50 = 7.9 7.9 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 410 2 2 4 5.1 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(N)nc3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1629848 56307 None 0 Rat Binding pIC50 = 7.9 7.9 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 410 2 2 4 5.1 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(N)nc3)c1)=N2 10.1016/j.bmcl.2010.09.125
22317918 56316 None 0 Rat Binding pIC50 = 7.9 7.9 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 439 3 2 4 5.3 Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(CO)n1 10.1016/j.bmcl.2010.09.125
CHEMBL1629858 56316 None 0 Rat Binding pIC50 = 7.9 7.9 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 439 3 2 4 5.3 Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(CO)n1 10.1016/j.bmcl.2010.09.125
22448874 95351 None 0 Rat Binding pIC50 = 6.9 6.9 - 0
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 493 5 2 6 4.3 CN(CCO)c1cc2c(cc1C#Cc1ccc(F)cc1)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2007.12.005
CHEMBL256424 95351 None 0 Rat Binding pIC50 = 6.9 6.9 - 0
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 493 5 2 6 4.3 CN(CCO)c1cc2c(cc1C#Cc1ccc(F)cc1)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2007.12.005
89554836 160718 None 0 Human Binding pIC50 = 6.9 6.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 451 4 2 7 3.2 C[C@@H]1CN(Cc2ccc3c(-c4cnc(N)s4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1 nan
CHEMBL4113073 160718 None 0 Human Binding pIC50 = 6.9 6.9 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 451 4 2 7 3.2 C[C@@H]1CN(Cc2ccc3c(-c4cnc(N)s4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1 nan
156017916 177910 None 0 Human Binding pIC50 = 6.8 6.8 - 0
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 473 6 2 6 3.9 CC[C@@](O)(c1cn(Cc2ccc3c(-c4cccc(F)c4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
CHEMBL4643527 177910 None 0 Human Binding pIC50 = 6.8 6.8 - 0
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 473 6 2 6 3.9 CC[C@@](O)(c1cn(Cc2ccc3c(-c4cccc(F)c4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
89554840 150602 None 0 Human Binding pIC50 = 6.8 6.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 393 3 0 5 4.5 Cn1cc(-c2cc(C#N)nc3cc(Cc4ccnc(C(F)(F)F)c4)ccc23)cn1 nan
CHEMBL3954534 150602 None 0 Human Binding pIC50 = 6.8 6.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 393 3 0 5 4.5 Cn1cc(-c2cc(C#N)nc3cc(Cc4ccnc(C(F)(F)F)c4)ccc23)cn1 nan
89554892 150689 None 0 Human Binding pIC50 = 6.8 6.8 - 1
Negative allosteric modulation of mGlu2R (unknown origin)Negative allosteric modulation of mGlu2R (unknown origin)
ChEMBL 416 6 1 5 4.0 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)c(F)c1 10.1021/acs.jmedchem.8b01266
CHEMBL3955188 150689 None 0 Human Binding pIC50 = 6.8 6.8 - 1
Negative allosteric modulation of mGlu2R (unknown origin)Negative allosteric modulation of mGlu2R (unknown origin)
ChEMBL 416 6 1 5 4.0 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)c(F)c1 10.1021/acs.jmedchem.8b01266
71566275 151729 None 0 Human Binding pIC50 = 6.8 6.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 375 4 1 5 3.3 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCCCC45CC5)ccc23)cn1 nan
CHEMBL3963813 151729 None 0 Human Binding pIC50 = 6.8 6.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 375 4 1 5 3.3 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCCCC45CC5)ccc23)cn1 nan
117642068 154364 None 0 Human Binding pIC50 = 6.8 6.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 367 4 1 5 2.7 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCC(F)CC4)ccc23)cn1 nan
CHEMBL3986471 154364 None 0 Human Binding pIC50 = 6.8 6.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 367 4 1 5 2.7 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCC(F)CC4)ccc23)cn1 nan
71566522 149431 None 0 Human Binding pIC50 = 6.8 6.8 - 0
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 266 2 1 2 3.1 NC(=O)c1cc(-c2ccc(F)cc2)c2ccccc2n1 10.1016/j.bmcl.2020.127066
CHEMBL3945170 149431 None 0 Human Binding pIC50 = 6.8 6.8 - 0
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 266 2 1 2 3.1 NC(=O)c1cc(-c2ccc(F)cc2)c2ccccc2n1 10.1016/j.bmcl.2020.127066
49765871 2145 None 41 Human Binding pIC50 = 7.8 7.8 - 1
Binding affinity to human mGlu2R expressed in CHO cells by radioligand binding assayBinding affinity to human mGlu2R expressed in CHO cells by radioligand binding assay
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/jm3010724
6317 2145 None 41 Human Binding pIC50 = 7.8 7.8 - 1
Binding affinity to human mGlu2R expressed in CHO cells by radioligand binding assayBinding affinity to human mGlu2R expressed in CHO cells by radioligand binding assay
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/jm3010724
CHEMBL2179319 2145 None 41 Human Binding pIC50 = 7.8 7.8 - 1
Binding affinity to human mGlu2R expressed in CHO cells by radioligand binding assayBinding affinity to human mGlu2R expressed in CHO cells by radioligand binding assay
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/jm3010724
89554911 143081 None 0 Human Binding pIC50 = 7.8 7.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 446 4 2 4 3.9 CC1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC(C(F)(F)F)N1 nan
CHEMBL3894556 143081 None 0 Human Binding pIC50 = 7.8 7.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 446 4 2 4 3.9 CC1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC(C(F)(F)F)N1 nan
89554889 144892 None 0 Human Binding pIC50 = 7.8 7.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 368 4 1 6 2.6 Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4ccnc(C#N)c4)ccc23)cn1 nan
CHEMBL3909377 144892 None 0 Human Binding pIC50 = 7.8 7.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 368 4 1 6 2.6 Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4ccnc(C#N)c4)ccc23)cn1 nan
89554788 146471 None 0 Human Binding pIC50 = 7.8 7.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 437 5 1 6 2.9 NC(=O)c1cc(-c2cnn(CF)c2)c2ccc(CN3CCO[C@H](C(F)(F)F)C3)cc2n1 nan
CHEMBL3921588 146471 None 0 Human Binding pIC50 = 7.8 7.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 437 5 1 6 2.9 NC(=O)c1cc(-c2cnn(CF)c2)c2ccc(CN3CCO[C@H](C(F)(F)F)C3)cc2n1 nan
89554753 146862 None 0 Human Binding pIC50 = 7.8 7.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 502 7 2 6 4.6 CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)cc4F)cc(C(N)=O)nc3c2)cn1)C(F)(F)F nan
CHEMBL3924490 146862 None 0 Human Binding pIC50 = 7.8 7.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 502 7 2 6 4.6 CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)cc4F)cc(C(N)=O)nc3c2)cn1)C(F)(F)F nan
117642146 148575 None 0 Human Binding pIC50 = 7.8 7.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 472 6 2 5 4.5 CC[C@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F nan
CHEMBL3938177 148575 None 0 Human Binding pIC50 = 7.8 7.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 472 6 2 5 4.5 CC[C@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F nan
71566048 150812 None 0 Human Binding pIC50 = 7.8 7.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 412 6 2 5 4.3 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4N)ccc23)cc1 nan
CHEMBL3956202 150812 None 0 Human Binding pIC50 = 7.8 7.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 412 6 2 5 4.3 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4N)ccc23)cc1 nan
89554977 151230 None 0 Human Binding pIC50 = 7.8 7.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 405 5 2 4 3.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cc3ccc(CO)nc3)c(F)c2n1 nan
CHEMBL3959505 151230 None 0 Human Binding pIC50 = 7.8 7.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 405 5 2 4 3.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cc3ccc(CO)nc3)c(F)c2n1 nan
117641924 152496 None 0 Human Binding pIC50 = 7.8 7.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 437 5 1 6 2.9 NC(=O)c1cc(-c2cnn(CF)c2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1 nan
CHEMBL3970507 152496 None 0 Human Binding pIC50 = 7.8 7.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 437 5 1 6 2.9 NC(=O)c1cc(-c2cnn(CF)c2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1 nan
71565961 153584 None 0 Human Binding pIC50 = 7.8 7.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 433 5 1 6 3.0 CCn1cc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)cn1 nan
CHEMBL3979694 153584 None 0 Human Binding pIC50 = 7.8 7.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 433 5 1 6 3.0 CCn1cc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)cn1 nan
124201730 160496 None 0 Human Binding pIC50 = 7.8 7.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 421 5 2 4 4.5 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc([C@H](O)Cc3ccc(Cl)nc3)cc2n1 nan
CHEMBL4111267 160496 None 0 Human Binding pIC50 = 7.8 7.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 421 5 2 4 4.5 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc([C@H](O)Cc3ccc(Cl)nc3)cc2n1 nan
44434257 151516 None 0 Rat Binding pIC50 = 5.8 5.8 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 318 1 1 2 4.5 Cc1ccc2c(c1)NC(=O)CC(c1cccc(C(F)(F)F)c1)=N2 10.1016/j.bmcl.2007.10.026
CHEMBL396181 151516 None 0 Rat Binding pIC50 = 5.8 5.8 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 318 1 1 2 4.5 Cc1ccc2c(c1)NC(=O)CC(c1cccc(C(F)(F)F)c1)=N2 10.1016/j.bmcl.2007.10.026
22224695 88738 None 0 Rat Binding pIC50 = 6.8 6.8 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 462 1 1 2 5.2 O=C1CC(c2cccc(I)c2)=Nc2ccc(C#Cc3ccccc3)cc2N1 10.1016/j.bmcl.2007.10.026
CHEMBL236035 88738 None 0 Rat Binding pIC50 = 6.8 6.8 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 462 1 1 2 5.2 O=C1CC(c2cccc(I)c2)=Nc2ccc(C#Cc3ccccc3)cc2N1 10.1016/j.bmcl.2007.10.026
89543901 150662 None 0 Human Binding pIC50 = 6.8 6.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 280 2 1 2 3.4 Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
CHEMBL3955040 150662 None 0 Human Binding pIC50 = 6.8 6.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 280 2 1 2 3.4 Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
71565963 152801 None 0 Human Binding pIC50 = 6.8 6.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 487 5 1 6 3.5 NC(=O)c1cc(-c2cnn(CC(F)(F)F)c2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1 nan
CHEMBL3973004 152801 None 0 Human Binding pIC50 = 6.8 6.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 487 5 1 6 3.5 NC(=O)c1cc(-c2cnn(CC(F)(F)F)c2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1 nan
89554753 146862 None 0 Human Binding pIC50 = 7.8 7.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 502 7 2 6 4.6 CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)cc4F)cc(C(N)=O)nc3c2)cn1)C(F)(F)F nan
CHEMBL3924490 146862 None 0 Human Binding pIC50 = 7.8 7.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 502 7 2 6 4.6 CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)cc4F)cc(C(N)=O)nc3c2)cn1)C(F)(F)F nan
89554752 147471 None 0 Human Binding pIC50 = 7.8 7.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 502 7 2 6 4.6 CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)c(F)c4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F nan
CHEMBL3929631 147471 None 0 Human Binding pIC50 = 7.8 7.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 502 7 2 6 4.6 CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)c(F)c4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F nan
71565525 150004 None 0 Human Binding pIC50 = 7.8 7.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 363 4 1 4 2.9 NC(=O)c1cc(C2=CCCCC2)c2ccc(CN3C(=O)CCC3=O)cc2n1 nan
CHEMBL3949476 150004 None 0 Human Binding pIC50 = 7.8 7.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 363 4 1 4 2.9 NC(=O)c1cc(C2=CCCCC2)c2ccc(CN3C(=O)CCC3=O)cc2n1 nan
71566048 150812 None 0 Human Binding pIC50 = 7.8 7.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 412 6 2 5 4.3 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4N)ccc23)cc1 nan
CHEMBL3956202 150812 None 0 Human Binding pIC50 = 7.8 7.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 412 6 2 5 4.3 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4N)ccc23)cc1 nan
89554891 160754 None 0 Human Binding pIC50 = 7.8 7.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 433 4 1 6 2.9 C[C@@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)C[C@@H](C(F)(F)F)O1 nan
CHEMBL4113348 160754 None 0 Human Binding pIC50 = 7.8 7.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 433 4 1 6 2.9 C[C@@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)C[C@@H](C(F)(F)F)O1 nan
9952648 96361 None 0 Rat Binding pIC50 = 7.8 7.8 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 397 3 1 5 4.5 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL261288 96361 None 0 Rat Binding pIC50 = 7.8 7.8 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 397 3 1 5 4.5 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1 10.1016/j.bmcl.2008.02.076
9952648 96361 None 0 Rat Binding pIC50 = 7.8 7.8 - 0
Displacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cells
ChEMBL 397 3 1 5 4.5 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1 10.1016/j.bmcl.2010.09.125
CHEMBL261288 96361 None 0 Rat Binding pIC50 = 7.8 7.8 - 0
Displacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cells
ChEMBL 397 3 1 5 4.5 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccccc3F)cc2N1 10.1016/j.bmcl.2010.09.125
89554732 160264 None 0 Human Binding pIC50 = 7.8 7.8 - 0
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 472 6 2 5 4.5 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
CHEMBL4109248 160264 None 0 Human Binding pIC50 = 7.8 7.8 - 0
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 472 6 2 5 4.5 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
156017027 177832 None 0 Human Binding pIC50 = 7.8 7.8 - 0
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 474 6 2 7 3.3 CC[C@@](O)(c1nnn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)n1)C(F)(F)F 10.1016/j.bmcl.2020.127066
CHEMBL4642338 177832 None 0 Human Binding pIC50 = 7.8 7.8 - 0
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 474 6 2 7 3.3 CC[C@@](O)(c1nnn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)n1)C(F)(F)F 10.1016/j.bmcl.2020.127066
53325611 56432 None 0 Rat Binding pIC50 = 7.8 7.8 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 485 4 1 3 7.1 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(Cc4ccccc4)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631867 56432 None 0 Rat Binding pIC50 = 7.8 7.8 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 485 4 1 3 7.1 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(Cc4ccccc4)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
22448864 89216 None 0 Rat Binding pIC50 = 6.8 6.8 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 494 2 1 6 3.7 N#Cc1cccc(C2=Nc3cc(N4CCS(=O)(=O)CC4)c(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
CHEMBL236669 89216 None 0 Rat Binding pIC50 = 6.8 6.8 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 494 2 1 6 3.7 N#Cc1cccc(C2=Nc3cc(N4CCS(=O)(=O)CC4)c(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
89554793 146429 None 0 Human Binding pIC50 = 6.8 6.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 420 4 2 4 4.0 CC(C)(C)C1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CCN1 nan
CHEMBL3921230 146429 None 0 Human Binding pIC50 = 6.8 6.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 420 4 2 4 4.0 CC(C)(C)C1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CCN1 nan
89554846 143236 None 0 Human Binding pIC50 = 5.8 5.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 420 4 1 6 3.1 Cc1ncc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)o1 nan
CHEMBL3895854 143236 None 0 Human Binding pIC50 = 5.8 5.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 420 4 1 6 3.1 Cc1ncc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)o1 nan
89545189 152984 None 0 Human Binding pIC50 = 6.8 6.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 365 4 1 4 3.0 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCOCC3)cc2n1 nan
CHEMBL3974648 152984 None 0 Human Binding pIC50 = 6.8 6.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 365 4 1 4 3.0 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCOCC3)cc2n1 nan
71565885 153523 None 0 Human Binding pIC50 = 6.8 6.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 395 6 1 7 1.6 COCC1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)CCO1 nan
CHEMBL3979211 153523 None 0 Human Binding pIC50 = 6.8 6.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 395 6 1 7 1.6 COCC1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)CCO1 nan
89554890 160959 None 0 Human Binding pIC50 = 6.8 6.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 365 4 1 6 2.0 C[C@@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)CCO1 nan
CHEMBL4114982 160959 None 0 Human Binding pIC50 = 6.8 6.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 365 4 1 6 2.0 C[C@@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)CCO1 nan
71566522 149431 None 0 Human Binding pIC50 = 6.8 6.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 266 2 1 2 3.1 NC(=O)c1cc(-c2ccc(F)cc2)c2ccccc2n1 nan
CHEMBL3945170 149431 None 0 Human Binding pIC50 = 6.8 6.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 266 2 1 2 3.1 NC(=O)c1cc(-c2ccc(F)cc2)c2ccccc2n1 nan
89554932 150007 None 0 Human Binding pIC50 = 6.8 6.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 385 4 1 5 2.8 Cn1cc(-c2cc(C(N)=O)nc3c(F)c(CN4CCC(F)CC4)ccc23)cn1 nan
CHEMBL3949512 150007 None 0 Human Binding pIC50 = 6.8 6.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 385 4 1 5 2.8 Cn1cc(-c2cc(C(N)=O)nc3c(F)c(CN4CCC(F)CC4)ccc23)cn1 nan
71566349 154257 None 0 Human Binding pIC50 = 6.8 6.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 326 2 1 2 3.8 NC(=O)c1cc(-c2ccc(Br)cc2)c2ccccc2n1 nan
CHEMBL3985577 154257 None 0 Human Binding pIC50 = 6.8 6.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 326 2 1 2 3.8 NC(=O)c1cc(-c2ccc(Br)cc2)c2ccccc2n1 nan
89554829 143038 None 0 Human Binding pIC50 = 7.8 7.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 433 4 1 6 2.9 C[C@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1 nan
CHEMBL3894162 143038 None 0 Human Binding pIC50 = 7.8 7.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 433 4 1 6 2.9 C[C@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1 nan
71565596 144880 None 0 Human Binding pIC50 = 7.8 7.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 379 4 1 4 3.3 CC1CCC(c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)CC1 nan
CHEMBL3909273 144880 None 0 Human Binding pIC50 = 7.8 7.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 379 4 1 4 3.3 CC1CCC(c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)CC1 nan
89554881 148336 None 0 Human Binding pIC50 = 7.8 7.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 433 4 1 6 2.9 C[C@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)C[C@@H](C(F)(F)F)O1 nan
CHEMBL3936318 148336 None 0 Human Binding pIC50 = 7.8 7.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 433 4 1 6 2.9 C[C@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)C[C@@H](C(F)(F)F)O1 nan
89554933 151512 None 0 Human Binding pIC50 = 7.8 7.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 490 6 2 5 4.7 CCC(O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2F)cn1)C(F)(F)F nan
CHEMBL3961788 151512 None 0 Human Binding pIC50 = 7.8 7.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 490 6 2 5 4.7 CCC(O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2F)cn1)C(F)(F)F nan
22224852 95917 None 0 Rat Binding pIC50 = 7.8 7.8 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 396 3 1 4 5.1 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL259054 95917 None 0 Rat Binding pIC50 = 7.8 7.8 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 396 3 1 4 5.1 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2008.02.076
18548908 96317 None 0 Rat Binding pIC50 = 7.8 7.8 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 404 2 1 4 5.0 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(Cl)c(C(F)(F)F)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL261051 96317 None 0 Rat Binding pIC50 = 7.8 7.8 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 404 2 1 4 5.0 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(Cl)c(C(F)(F)F)cc2N1 10.1016/j.bmcl.2008.02.076
22224670 96320 None 0 Rat Binding pIC50 = 7.8 7.8 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 415 3 1 5 4.7 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3cc(F)ccc3F)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL261081 96320 None 0 Rat Binding pIC50 = 7.8 7.8 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 415 3 1 5 4.7 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3cc(F)ccc3F)cc2N1 10.1016/j.bmcl.2008.02.076
89554950 148306 None 0 Human Binding pIC50 = 6.8 6.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 443 5 1 5 4.5 Cc1cn(C2CCN(Cc3ccc4c(-c5ccc(F)cc5)cc(C(N)=O)nc4c3)CC2)cn1 nan
CHEMBL3936050 148306 None 0 Human Binding pIC50 = 6.8 6.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 443 5 1 5 4.5 Cc1cn(C2CCN(Cc3ccc4c(-c5ccc(F)cc5)cc(C(N)=O)nc4c3)CC2)cn1 nan
117642183 153464 None 0 Human Binding pIC50 = 6.8 6.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 354 4 0 4 4.5 N#Cc1cc(-c2ccc(F)cc2)c2ccc(CCc3cncnc3)cc2n1 nan
CHEMBL3978639 153464 None 0 Human Binding pIC50 = 6.8 6.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 354 4 0 4 4.5 N#Cc1cc(-c2ccc(F)cc2)c2ccc(CCc3cncnc3)cc2n1 nan
22224972 97748 None 0 Rat Binding pIC50 = 6.8 6.8 - 0
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 430 2 1 4 5.4 Cc1cn(-c2cccc(C3=Nc4ccc(C#Cc5ccccc5)cc4NC(=O)C3)c2)c(C)n1 10.1016/j.bmcl.2007.12.005
CHEMBL271319 97748 None 0 Rat Binding pIC50 = 6.8 6.8 - 0
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 430 2 1 4 5.4 Cc1cn(-c2cccc(C3=Nc4ccc(C#Cc5ccccc5)cc4NC(=O)C3)c2)c(C)n1 10.1016/j.bmcl.2007.12.005
11503055 2400 None 2 Human Binding pIC50 = 4.8 4.8 - 0
Negative allosteric modulation of mGlu2 assessed as thallium flux through GIRK channels by cell-based assayNegative allosteric modulation of mGlu2 assessed as thallium flux through GIRK channels by cell-based assay
ChEMBL 400 4 1 4 3.9 Clc1ccc(c(c1)Cl)CN[C@H]1CCN(C1)c1ncc(cn1)Br 10.1016/j.bmcl.2012.04.112
9694 2400 None 2 Human Binding pIC50 = 4.8 4.8 - 0
Negative allosteric modulation of mGlu2 assessed as thallium flux through GIRK channels by cell-based assayNegative allosteric modulation of mGlu2 assessed as thallium flux through GIRK channels by cell-based assay
ChEMBL 400 4 1 4 3.9 Clc1ccc(c(c1)Cl)CN[C@H]1CCN(C1)c1ncc(cn1)Br 10.1016/j.bmcl.2012.04.112
CHEMBL2204436 2400 None 2 Human Binding pIC50 = 4.8 4.8 - 0
Negative allosteric modulation of mGlu2 assessed as thallium flux through GIRK channels by cell-based assayNegative allosteric modulation of mGlu2 assessed as thallium flux through GIRK channels by cell-based assay
ChEMBL 400 4 1 4 3.9 Clc1ccc(c(c1)Cl)CN[C@H]1CCN(C1)c1ncc(cn1)Br 10.1016/j.bmcl.2012.04.112
71566435 152743 None 0 Human Binding pIC50 = 6.8 6.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 318 2 1 2 3.9 NC(=O)c1cc(-c2c(F)cc(Cl)cc2F)c2ccccc2n1 nan
CHEMBL3972482 152743 None 0 Human Binding pIC50 = 6.8 6.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 318 2 1 2 3.9 NC(=O)c1cc(-c2c(F)cc(Cl)cc2F)c2ccccc2n1 nan
89554799 160890 None 0 Human Binding pIC50 = 6.8 6.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 404 4 1 4 3.4 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCN4CCC[C@@H]4C3)cc2n1 nan
CHEMBL4114381 160890 None 0 Human Binding pIC50 = 6.8 6.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 404 4 1 4 3.4 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCN4CCC[C@@H]4C3)cc2n1 nan
89554919 143877 None 0 Human Binding pIC50 = 7.8 7.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 435 4 1 6 3.2 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCSC(C(F)(F)F)C4)ccc23)cn1 nan
CHEMBL3901084 143877 None 0 Human Binding pIC50 = 7.8 7.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 435 4 1 6 3.2 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCSC(C(F)(F)F)C4)ccc23)cn1 nan
71566204 148780 None 0 Human Binding pIC50 = 7.8 7.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 387 5 1 4 4.1 COc1cc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)ccn1 nan
CHEMBL3939934 148780 None 0 Human Binding pIC50 = 7.8 7.8 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 387 5 1 4 4.1 COc1cc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)ccn1 nan
22448830 89471 None 0 Rat Binding pIC50 = 7.8 7.8 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 416 3 1 5 4.3 N#CCOc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(C#N)c1)=N2 10.1016/j.bmcl.2007.10.026
CHEMBL237091 89471 None 0 Rat Binding pIC50 = 7.8 7.8 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 416 3 1 5 4.3 N#CCOc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(C#N)c1)=N2 10.1016/j.bmcl.2007.10.026
22448689 97608 None 0 Rat Binding pIC50 = 7.8 7.8 - 0
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 457 4 1 6 4.6 N#CCOc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2007.12.005
CHEMBL270616 97608 None 0 Rat Binding pIC50 = 7.8 7.8 - 0
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 457 4 1 6 4.6 N#CCOc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2007.12.005
22317408 56309 None 0 Rat Binding pIC50 = 7.8 7.8 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 396 2 1 4 4.9 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnnc3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1629850 56309 None 0 Rat Binding pIC50 = 7.8 7.8 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 396 2 1 4 4.9 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnnc3)c1)=N2 10.1016/j.bmcl.2010.09.125
11211597 56324 None 0 Rat Binding pIC50 = 7.8 7.8 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 395 2 1 3 5.5 Cc1cc(-c2cccc(C3=Nc4ccc(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
CHEMBL1629865 56324 None 0 Rat Binding pIC50 = 7.8 7.8 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 395 2 1 3 5.5 Cc1cc(-c2cccc(C3=Nc4ccc(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
89554780 145471 None 0 Human Binding pIC50 = 6.7 6.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 417 4 1 3 4.7 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC3C(F)(F)F)cc2n1 nan
CHEMBL3913806 145471 None 0 Human Binding pIC50 = 6.7 6.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 417 4 1 3 4.7 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC3C(F)(F)F)cc2n1 nan
89554777 145385 None 0 Human Binding pIC50 = 6.7 6.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 406 5 2 4 2.9 CC(=O)NC1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1 nan
CHEMBL3913090 145385 None 0 Human Binding pIC50 = 6.7 6.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 406 5 2 4 2.9 CC(=O)NC1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1 nan
89554839 153481 None 0 Human Binding pIC50 = 6.7 6.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 445 5 1 6 3.3 NC(=O)c1cc(-c2cnn(C3CC3)c2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1 nan
CHEMBL3978791 153481 None 0 Human Binding pIC50 = 6.7 6.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 445 5 1 6 3.3 NC(=O)c1cc(-c2cnn(C3CC3)c2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1 nan
89554772 144879 None 0 Human Binding pIC50 = 6.7 6.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 473 5 1 5 5.6 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(-c4ccccn4)nc4ccccc43)cc2n1 nan
CHEMBL3909260 144879 None 0 Human Binding pIC50 = 6.7 6.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 473 5 1 5 5.6 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(-c4ccccn4)nc4ccccc43)cc2n1 nan
89554745 149678 None 0 Human Binding pIC50 = 7.7 7.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 401 5 2 4 4.1 Cc1ccc(CC(O)c2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 nan
CHEMBL3946940 149678 None 0 Human Binding pIC50 = 7.7 7.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 401 5 2 4 4.1 Cc1ccc(CC(O)c2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 nan
89554794 152488 None 0 Human Binding pIC50 = 7.7 7.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 399 5 1 3 5.2 Cc1ccc(CC(C)c2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 nan
CHEMBL3970463 152488 None 0 Human Binding pIC50 = 7.7 7.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 399 5 1 3 5.2 Cc1ccc(CC(C)c2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 nan
89554732 160264 None 0 Human Binding pIC50 = 7.7 7.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 472 6 2 5 4.5 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F nan
CHEMBL4109248 160264 None 0 Human Binding pIC50 = 7.7 7.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 472 6 2 5 4.5 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F nan
10297067 96357 None 0 Rat Binding pIC50 = 7.7 7.7 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 441 5 2 5 5.4 CC(C)CNc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2008.02.076
CHEMBL261263 96357 None 0 Rat Binding pIC50 = 7.7 7.7 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 441 5 2 5 5.4 CC(C)CNc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2008.02.076
156016312 177838 None 0 Human Binding pIC50 = 7.7 7.7 - 0
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 487 6 2 6 4.5 CC[C@@](O)(c1cn(C(C)c2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
CHEMBL4642428 177838 None 0 Human Binding pIC50 = 7.7 7.7 - 0
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 487 6 2 6 4.5 CC[C@@](O)(c1cn(C(C)c2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
156018942 177975 None 0 Human Binding pIC50 = 7.7 7.7 - 0
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 507 6 2 6 4.6 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(Cl)cc4F)cc(C(N)=O)nc3c2)nn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
CHEMBL4644424 177975 None 0 Human Binding pIC50 = 7.7 7.7 - 0
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 507 6 2 6 4.6 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(Cl)cc4F)cc(C(N)=O)nc3c2)nn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
89554861 149912 None 0 Human Binding pIC50 = 6.7 6.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 287 2 1 3 3.2 Cc1ccc2c(-c3ccc(C#N)cc3)cc(C(N)=O)nc2c1 nan
CHEMBL3948794 149912 None 0 Human Binding pIC50 = 6.7 6.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 287 2 1 3 3.2 Cc1ccc2c(-c3ccc(C#N)cc3)cc(C(N)=O)nc2c1 nan
71565804 144002 None 0 Human Binding pIC50 = 6.7 6.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 444 6 2 5 4.6 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cc(C(O)C4CCCC4)cn3)cc2n1 nan
CHEMBL3902047 144002 None 0 Human Binding pIC50 = 6.7 6.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 444 6 2 5 4.6 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cc(C(O)C4CCCC4)cn3)cc2n1 nan
89554886 159976 None 0 Human Binding pIC50 = 6.7 6.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 365 4 1 6 2.0 C[C@@H]1COCCN1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1 nan
CHEMBL4106809 159976 None 0 Human Binding pIC50 = 6.7 6.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 365 4 1 6 2.0 C[C@@H]1COCCN1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1 nan
11158623 3351 None 11 Rat Binding pIC50 = 8.7 8.7 8 2
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 10.1016/j.bmcl.2010.09.125
6226 3351 None 11 Rat Binding pIC50 = 8.7 8.7 8 2
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 10.1016/j.bmcl.2010.09.125
CHEMBL1629855 3351 None 11 Rat Binding pIC50 = 8.7 8.7 8 2
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 10.1016/j.bmcl.2010.09.125
11351088 56314 None 0 Rat Binding pIC50 = 8.7 8.7 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 437 3 1 3 6.4 CCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C)n1 10.1016/j.bmcl.2010.09.125
CHEMBL1629856 56314 None 0 Rat Binding pIC50 = 8.7 8.7 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 437 3 1 3 6.4 CCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C)n1 10.1016/j.bmcl.2010.09.125
22317928 56315 None 0 Rat Binding pIC50 = 8.7 8.7 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 449 3 1 3 6.7 Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C2CC2)n1 10.1016/j.bmcl.2010.09.125
CHEMBL1629857 56315 None 0 Rat Binding pIC50 = 8.7 8.7 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 449 3 1 3 6.7 Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C2CC2)n1 10.1016/j.bmcl.2010.09.125
11406781 56441 None 0 Rat Binding pIC50 = 8.7 8.7 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 395 2 1 3 5.5 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cccnc3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631876 56441 None 0 Rat Binding pIC50 = 8.7 8.7 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 395 2 1 3 5.5 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cccnc3)c1)=N2 10.1016/j.bmcl.2010.09.125
1378 2417 None 39 Human Binding pIC50 = 8.5 8.5 -2 10
Displacement of [3H]-MGS0008 from mGluR2 expressed in CHO cellsDisplacement of [3H]-MGS0008 from mGluR2 expressed in CHO cells
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1016/j.bmc.2008.02.066
1399 2417 None 39 Human Binding pIC50 = 8.5 8.5 -2 10
Displacement of [3H]-MGS0008 from mGluR2 expressed in CHO cellsDisplacement of [3H]-MGS0008 from mGluR2 expressed in CHO cells
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1016/j.bmc.2008.02.066
9819927 2417 None 39 Human Binding pIC50 = 8.5 8.5 -2 10
Displacement of [3H]-MGS0008 from mGluR2 expressed in CHO cellsDisplacement of [3H]-MGS0008 from mGluR2 expressed in CHO cells
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1016/j.bmc.2008.02.066
CHEMBL432038 2417 None 39 Human Binding pIC50 = 8.5 8.5 -2 10
Displacement of [3H]-MGS0008 from mGluR2 expressed in CHO cellsDisplacement of [3H]-MGS0008 from mGluR2 expressed in CHO cells
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1016/j.bmc.2008.02.066
89554746 143842 None 0 Human Binding pIC50 = 7.7 7.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 385 5 1 3 4.9 CC(Cc1cccnc1)c1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
CHEMBL3900813 143842 None 0 Human Binding pIC50 = 7.7 7.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 385 5 1 3 4.9 CC(Cc1cccnc1)c1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
89554931 147644 None 0 Human Binding pIC50 = 7.7 7.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 416 5 1 4 4.5 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cc3cnc(C4CC4)nc3)c(F)c2n1 nan
CHEMBL3930820 147644 None 0 Human Binding pIC50 = 7.7 7.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 416 5 1 4 4.5 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cc3cnc(C4CC4)nc3)c(F)c2n1 nan
1397 2529 None 15 Rat Binding pIC50 = 7.7 7.7 -1 5
Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells
ChEMBL 377 5 3 4 2.1 OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
9886034 2529 None 15 Rat Binding pIC50 = 7.7 7.7 -1 5
Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells
ChEMBL 377 5 3 4 2.1 OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL186453 2529 None 15 Rat Binding pIC50 = 7.7 7.7 -1 5
Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells
ChEMBL 377 5 3 4 2.1 OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
22224970 155582 None 0 Rat Binding pIC50 = 7.7 7.7 - 0
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 420 2 1 4 4.9 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C#Cc3ccccc3F)cc2N1 10.1016/j.bmcl.2007.12.005
CHEMBL404080 155582 None 0 Rat Binding pIC50 = 7.7 7.7 - 0
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 420 2 1 4 4.9 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C#Cc3ccccc3F)cc2N1 10.1016/j.bmcl.2007.12.005
135544097 155755 None 0 Rat Binding pIC50 = 7.7 7.7 - 0
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 437 2 2 6 4.0 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2007.12.005
CHEMBL404886 155755 None 0 Rat Binding pIC50 = 7.7 7.7 - 0
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 437 2 2 6 4.0 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2007.12.005
22317715 56313 None 0 Rat Binding pIC50 = 7.7 7.7 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 396 2 1 4 4.9 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cnccn3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1629854 56313 None 0 Rat Binding pIC50 = 7.7 7.7 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 396 2 1 4 4.9 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cnccn3)c1)=N2 10.1016/j.bmcl.2010.09.125
9885546 110601 None 0 Human Binding pIC50 = 6.7 6.7 - 1
Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2
ChEMBL 367 6 3 4 3.1 NC(C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1CCC1c2ccccc2Oc2ccccc21 10.1016/s0960-894x(01)00656-4
CHEMBL325140 110601 None 0 Human Binding pIC50 = 6.7 6.7 - 1
Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2
ChEMBL 367 6 3 4 3.1 NC(C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1CCC1c2ccccc2Oc2ccccc21 10.1016/s0960-894x(01)00656-4
1378 2417 None 39 Human Binding pIC50 = 6.7 6.7 -2 10
Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1016/s0960-894x(01)00656-4
1399 2417 None 39 Human Binding pIC50 = 6.7 6.7 -2 10
Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1016/s0960-894x(01)00656-4
9819927 2417 None 39 Human Binding pIC50 = 6.7 6.7 -2 10
Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1016/s0960-894x(01)00656-4
CHEMBL432038 2417 None 39 Human Binding pIC50 = 6.7 6.7 -2 10
Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human mGluR2
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1016/s0960-894x(01)00656-4
44309302 206520 None 0 Rat Binding pIC50 = 5.7 5.7 - 0
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 345 5 0 4 4.8 Clc1cccc(Cl)c1/C(=C/n1cncn1)OCc1ccccc1 10.1016/s0960-894x(99)00346-7
CHEMBL70025 206520 None 0 Rat Binding pIC50 = 5.7 5.7 - 0
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 345 5 0 4 4.8 Clc1cccc(Cl)c1/C(=C/n1cncn1)OCc1ccccc1 10.1016/s0960-894x(99)00346-7
89554729 146483 None 0 Human Binding pIC50 = 6.7 6.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 514 8 2 7 4.4 CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)c(OC)c4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F nan
CHEMBL3921665 146483 None 0 Human Binding pIC50 = 6.7 6.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 514 8 2 7 4.4 CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)c(OC)c4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F nan
121447916 170051 None 3 Human Binding pIC50 = 6.7 6.7 - 0
Negative allosteric modulation of mGlu2R (unknown origin)Negative allosteric modulation of mGlu2R (unknown origin)
ChEMBL 409 4 1 5 2.8 C[C@H]1CN(Cc2ccc3c(c2)c(=O)c(C(N)=O)cn3-c2ccc(F)cc2)C[C@@H](C)O1 10.1021/acs.jmedchem.8b01266
CHEMBL4441595 170051 None 3 Human Binding pIC50 = 6.7 6.7 - 0
Negative allosteric modulation of mGlu2R (unknown origin)Negative allosteric modulation of mGlu2R (unknown origin)
ChEMBL 409 4 1 5 2.8 C[C@H]1CN(Cc2ccc3c(c2)c(=O)c(C(N)=O)cn3-c2ccc(F)cc2)C[C@@H](C)O1 10.1021/acs.jmedchem.8b01266
66791078 142761 None 0 Human Binding pIC50 = 7.7 7.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 489 6 2 6 4.5 CC[C@](O)(c1cn(Cc2ccc3c(-c4ccc(Cl)cc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F nan
CHEMBL3891986 142761 None 0 Human Binding pIC50 = 7.7 7.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 489 6 2 6 4.5 CC[C@](O)(c1cn(Cc2ccc3c(-c4ccc(Cl)cc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F nan
89554746 143842 None 0 Human Binding pIC50 = 7.7 7.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 385 5 1 3 4.9 CC(Cc1cccnc1)c1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
CHEMBL3900813 143842 None 0 Human Binding pIC50 = 7.7 7.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 385 5 1 3 4.9 CC(Cc1cccnc1)c1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
71566596 144234 None 0 Human Binding pIC50 = 7.7 7.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 392 4 1 4 2.5 CN1CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O nan
CHEMBL3903901 144234 None 0 Human Binding pIC50 = 7.7 7.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 392 4 1 4 2.5 CN1CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O nan
89554855 146630 None 0 Human Binding pIC50 = 7.7 7.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 391 5 1 6 2.9 COc1ncccc1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1F nan
CHEMBL3922719 146630 None 0 Human Binding pIC50 = 7.7 7.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 391 5 1 6 2.9 COc1ncccc1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1F nan
89554970 147302 None 0 Human Binding pIC50 = 7.7 7.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 452 4 0 7 3.3 COC(=O)c1cc(-c2cnn(C)c2)c2ccc(CN3CCO[C@H](C(F)(F)F)C3)c(F)c2n1 nan
CHEMBL3928272 147302 None 0 Human Binding pIC50 = 7.7 7.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 452 4 0 7 3.3 COC(=O)c1cc(-c2cnn(C)c2)c2ccc(CN3CCO[C@H](C(F)(F)F)C3)c(F)c2n1 nan
71566599 147394 None 0 Human Binding pIC50 = 7.7 7.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 419 4 1 4 3.8 CC1(C)CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C(=O)C1 nan
CHEMBL3929001 147394 None 0 Human Binding pIC50 = 7.7 7.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 419 4 1 4 3.8 CC1(C)CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C(=O)C1 nan
89554806 149305 None 0 Human Binding pIC50 = 7.7 7.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 474 6 2 7 3.3 CCC(O)(c1nnnn1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1)C(F)(F)F nan
CHEMBL3944124 149305 None 0 Human Binding pIC50 = 7.7 7.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 474 6 2 7 3.3 CCC(O)(c1nnnn1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1)C(F)(F)F nan
89554883 150289 None 0 Human Binding pIC50 = 7.7 7.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 395 4 1 4 2.9 NC(=O)c1cc(-c2ccc(F)cc2)c2cc(F)c(CN3C(=O)CCC3=O)cc2n1 nan
CHEMBL3951983 150289 None 0 Human Binding pIC50 = 7.7 7.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 395 4 1 4 2.9 NC(=O)c1cc(-c2ccc(F)cc2)c2cc(F)c(CN3C(=O)CCC3=O)cc2n1 nan
71566130 151970 None 0 Human Binding pIC50 = 7.7 7.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 384 5 1 6 3.0 Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cnc(C5CC5)nc4)ccc23)cn1 nan
CHEMBL3965748 151970 None 0 Human Binding pIC50 = 7.7 7.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 384 5 1 6 3.0 Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cnc(C5CC5)nc4)ccc23)cn1 nan
89554794 152488 None 0 Human Binding pIC50 = 7.7 7.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 399 5 1 3 5.2 Cc1ccc(CC(C)c2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 nan
CHEMBL3970463 152488 None 0 Human Binding pIC50 = 7.7 7.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 399 5 1 3 5.2 Cc1ccc(CC(C)c2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 nan
89554759 160140 None 0 Human Binding pIC50 = 7.7 7.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 474 6 2 7 3.3 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cn4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F nan
CHEMBL4108213 160140 None 0 Human Binding pIC50 = 7.7 7.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 474 6 2 7 3.3 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cn4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F nan
71566672 152918 None 0 Human Binding pIC50 = 7.7 7.7 - 0
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 391 4 1 4 3.2 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCCC3=O)cc2n1 10.1016/j.bmcl.2020.127066
CHEMBL3973949 152918 None 0 Human Binding pIC50 = 7.7 7.7 - 0
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 391 4 1 4 3.2 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCCC3=O)cc2n1 10.1016/j.bmcl.2020.127066
22224962 96356 None 0 Rat Binding pIC50 = 6.7 6.7 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 342 3 1 4 4.2 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C3CC3)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL261251 96356 None 0 Rat Binding pIC50 = 6.7 6.7 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 342 3 1 4 4.2 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C3CC3)cc2N1 10.1016/j.bmcl.2008.02.076
11559750 96008 None 0 Human Binding pIC50 = 6.7 6.7 - 0
Displacement of [3H]-MGS0008 from mGluR2 expressed in CHO cellsDisplacement of [3H]-MGS0008 from mGluR2 expressed in CHO cells
ChEMBL 371 5 3 4 2.9 NC(CC1c2ccccc2Oc2ccccc21)(C(=O)O)C1CC1(F)C(=O)O 10.1016/j.bmc.2008.02.066
CHEMBL259435 96008 None 0 Human Binding pIC50 = 6.7 6.7 - 0
Displacement of [3H]-MGS0008 from mGluR2 expressed in CHO cellsDisplacement of [3H]-MGS0008 from mGluR2 expressed in CHO cells
ChEMBL 371 5 3 4 2.9 NC(CC1c2ccccc2Oc2ccccc21)(C(=O)O)C1CC1(F)C(=O)O 10.1016/j.bmc.2008.02.066
89554860 145459 None 0 Human Binding pIC50 = 6.7 6.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 410 4 2 6 1.7 Cn1cc(-c2cc(C(N)=O)nc3c(F)c(CN4C(=O)NC(C)(C)C4=O)ccc23)cn1 nan
CHEMBL3913733 145459 None 0 Human Binding pIC50 = 6.7 6.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 410 4 2 6 1.7 Cn1cc(-c2cc(C(N)=O)nc3c(F)c(CN4C(=O)NC(C)(C)C4=O)ccc23)cn1 nan
71566519 153932 None 0 Human Binding pIC50 = 6.7 6.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 292 3 1 3 3.3 COc1ccc(-c2cc(C(N)=O)nc3cc(C)ccc23)cc1 nan
CHEMBL3982696 153932 None 0 Human Binding pIC50 = 6.7 6.7 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 292 3 1 3 3.3 COc1ccc(-c2cc(C(N)=O)nc3cc(C)ccc23)cc1 nan
89554797 143202 None 0 Human Binding pIC50 = 7.7 7.7 - 1
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 398 6 1 5 3.9 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)cc1 nan
CHEMBL3895570 143202 None 0 Human Binding pIC50 = 7.7 7.7 - 1
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 398 6 1 5 3.9 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)cc1 nan
22448579 155868 None 0 Rat Binding pIC50 = 7.7 7.7 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 412 3 2 5 4.8 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(-c3ccccc3F)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL405895 155868 None 0 Rat Binding pIC50 = 7.7 7.7 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 412 3 2 5 4.8 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(-c3ccccc3F)cc2N1 10.1016/j.bmcl.2008.02.076
11084869 90087 None 1 Human Binding pIC50 = 7.7 7.7 - 1
Agonist activity at mGlu2 (unknown origin)Agonist activity at mGlu2 (unknown origin)
ChEMBL 201 2 4 4 -1.5 N[C@@]1(C(=O)O)C[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL2381643 90087 None 1 Human Binding pIC50 = 7.7 7.7 - 1
Agonist activity at mGlu2 (unknown origin)Agonist activity at mGlu2 (unknown origin)
ChEMBL 201 2 4 4 -1.5 N[C@@]1(C(=O)O)C[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
11405687 66478 None 0 Rat Binding pIC50 = 7.6 7.6 2 2
Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells
ChEMBL 359 5 3 4 2.0 N[C@@]1(C(=O)O)[C@H](OCc2ccc3ccccc3c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL185210 66478 None 0 Rat Binding pIC50 = 7.6 7.6 2 2
Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells
ChEMBL 359 5 3 4 2.0 N[C@@]1(C(=O)O)[C@H](OCc2ccc3ccccc3c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
117646988 149569 None 0 Human Binding pIC50 = 6.6 6.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 393 4 1 5 2.0 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)COCC3=O)cc2n1 nan
CHEMBL3946311 149569 None 0 Human Binding pIC50 = 6.6 6.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 393 4 1 5 2.0 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)COCC3=O)cc2n1 nan
10192719 66135 None 0 Rat Binding pIC50 = 6.6 6.6 2 2
Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells
ChEMBL 233 3 3 4 -0.8 CO[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL183956 66135 None 0 Rat Binding pIC50 = 6.6 6.6 2 2
Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells
ChEMBL 233 3 3 4 -0.8 CO[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O 10.1021/jm0400294
89554911 143081 None 0 Human Binding pIC50 = 7.6 7.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 446 4 2 4 3.9 CC1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC(C(F)(F)F)N1 nan
CHEMBL3894556 143081 None 0 Human Binding pIC50 = 7.6 7.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 446 4 2 4 3.9 CC1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC(C(F)(F)F)N1 nan
71565881 143112 None 0 Human Binding pIC50 = 7.6 7.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 380 4 1 4 4.0 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3ccnc3Cl)cc2n1 nan
CHEMBL3894799 143112 None 0 Human Binding pIC50 = 7.6 7.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 380 4 1 4 4.0 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3ccnc3Cl)cc2n1 nan
71566672 152918 None 0 Human Binding pIC50 = 7.6 7.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 391 4 1 4 3.2 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCCC3=O)cc2n1 nan
CHEMBL3973949 152918 None 0 Human Binding pIC50 = 7.6 7.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 391 4 1 4 3.2 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCCC3=O)cc2n1 nan
89554767 153504 None 0 Human Binding pIC50 = 7.6 7.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 404 5 1 6 3.2 COC(=O)c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 nan
CHEMBL3978978 153504 None 0 Human Binding pIC50 = 7.6 7.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 404 5 1 6 3.2 COC(=O)c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 nan
9891158 155676 None 0 Rat Binding pIC50 = 7.6 7.6 - 0
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 476 6 1 6 4.8 COCCOc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2007.12.005
CHEMBL404463 155676 None 0 Rat Binding pIC50 = 7.6 7.6 - 0
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 476 6 1 6 4.8 COCCOc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2007.12.005
22317491 56312 None 0 Rat Binding pIC50 = 7.6 7.6 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 396 2 1 4 4.9 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cncnc3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1629853 56312 None 0 Rat Binding pIC50 = 7.6 7.6 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 396 2 1 4 4.9 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3cncnc3)c1)=N2 10.1016/j.bmcl.2010.09.125
1378 2417 None 39 Rat Binding pIC50 = 7.6 7.6 -1 10
Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/jm0400294
1399 2417 None 39 Rat Binding pIC50 = 7.6 7.6 -1 10
Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/jm0400294
9819927 2417 None 39 Rat Binding pIC50 = 7.6 7.6 -1 10
Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/jm0400294
CHEMBL432038 2417 None 39 Rat Binding pIC50 = 7.6 7.6 -1 10
Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/jm0400294
89554965 144611 None 0 Human Binding pIC50 = 6.6 6.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 432 4 2 4 3.5 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNCC3C(F)(F)F)cc2n1 nan
CHEMBL3907125 144611 None 0 Human Binding pIC50 = 6.6 6.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 432 4 2 4 3.5 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNCC3C(F)(F)F)cc2n1 nan
89554894 150193 None 0 Human Binding pIC50 = 6.6 6.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 379 4 1 6 2.3 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCOCC4(C)C)ccc23)cn1 nan
CHEMBL3951081 150193 None 0 Human Binding pIC50 = 6.6 6.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 379 4 1 6 2.3 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCOCC4(C)C)ccc23)cn1 nan
89554916 154018 None 0 Human Binding pIC50 = 6.6 6.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 375 4 1 5 3.1 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCCC5(CC5)C4)ccc23)cn1 nan
CHEMBL3983396 154018 None 0 Human Binding pIC50 = 6.6 6.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 375 4 1 5 3.1 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCCC5(CC5)C4)ccc23)cn1 nan
156014599 177278 None 0 Human Binding pIC50 = 6.6 6.6 - 0
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 472 6 1 6 5.0 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(C)=O)nc3c2)nn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
CHEMBL4634754 177278 None 0 Human Binding pIC50 = 6.6 6.6 - 0
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 472 6 1 6 5.0 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(C)=O)nc3c2)nn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
89554911 143081 None 0 Human Binding pIC50 = 7.6 7.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 446 4 2 4 3.9 CC1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC(C(F)(F)F)N1 nan
CHEMBL3894556 143081 None 0 Human Binding pIC50 = 7.6 7.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 446 4 2 4 3.9 CC1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC(C(F)(F)F)N1 nan
71565884 143512 None 0 Human Binding pIC50 = 7.6 7.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 433 4 1 4 3.9 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1 nan
CHEMBL3898121 143512 None 0 Human Binding pIC50 = 7.6 7.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 433 4 1 4 3.9 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1 nan
71565736 152662 None 0 Human Binding pIC50 = 7.6 7.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 474 6 2 7 3.3 CCC(O)(c1nnn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)n1)C(F)(F)F nan
CHEMBL3971819 152662 None 0 Human Binding pIC50 = 7.6 7.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 474 6 2 7 3.3 CCC(O)(c1nnn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)n1)C(F)(F)F nan
89554728 152963 None 0 Human Binding pIC50 = 7.6 7.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 407 6 1 6 3.0 CC(C)CC1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)CCO1 nan
CHEMBL3974406 152963 None 0 Human Binding pIC50 = 7.6 7.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 407 6 1 6 3.0 CC(C)CC1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)CCO1 nan
89554776 153242 None 0 Human Binding pIC50 = 7.6 7.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 478 5 1 4 5.6 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(CC(F)(F)F)nc4ccccc43)cc2n1 nan
CHEMBL3976706 153242 None 0 Human Binding pIC50 = 7.6 7.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 478 5 1 4 5.6 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(CC(F)(F)F)nc4ccccc43)cc2n1 nan
11257636 168475 None 0 Rat Binding pIC50 = 7.6 7.6 1 2
Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells
ChEMBL 385 6 3 4 2.4 N[C@@]1(C(=O)O)[C@H](OC(c2ccccc2)c2ccccc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL434536 168475 None 0 Rat Binding pIC50 = 7.6 7.6 1 2
Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells
ChEMBL 385 6 3 4 2.4 N[C@@]1(C(=O)O)[C@H](OC(c2ccccc2)c2ccccc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
22448659 154692 None 0 Rat Binding pIC50 = 5.6 5.6 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 434 4 2 5 3.3 N#Cc1cccc(C2=Nc3cc(OCC(N)=O)c(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
CHEMBL399186 154692 None 0 Rat Binding pIC50 = 5.6 5.6 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 434 4 2 5 3.3 N#Cc1cccc(C2=Nc3cc(OCC(N)=O)c(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
89555004 143718 None 0 Human Binding pIC50 = 6.6 6.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 367 7 1 4 3.2 COCCN(C)Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
CHEMBL3899807 143718 None 0 Human Binding pIC50 = 6.6 6.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 367 7 1 4 3.2 COCCN(C)Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
89554821 147438 None 0 Human Binding pIC50 = 6.6 6.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 367 4 1 5 2.7 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCCC(F)C4)ccc23)cn1 nan
CHEMBL3929361 147438 None 0 Human Binding pIC50 = 6.6 6.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 367 4 1 5 2.7 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCCC(F)C4)ccc23)cn1 nan
89554837 147927 None 0 Human Binding pIC50 = 6.6 6.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 375 4 1 5 3.1 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCC5(CC4)CC5)ccc23)cn1 nan
CHEMBL3933004 147927 None 0 Human Binding pIC50 = 6.6 6.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 375 4 1 5 3.1 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCC5(CC4)CC5)ccc23)cn1 nan
117641885 143103 None 0 Human Binding pIC50 = 7.6 7.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 419 4 1 6 2.5 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCO[C@H](C(F)(F)F)C4)ccc23)cn1 nan
CHEMBL3894759 143103 None 0 Human Binding pIC50 = 7.6 7.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 419 4 1 6 2.5 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCO[C@H](C(F)(F)F)C4)ccc23)cn1 nan
89554923 146534 None 0 Human Binding pIC50 = 7.6 7.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 371 4 1 5 3.3 Cc1cc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)cc(C)n1 nan
CHEMBL3922052 146534 None 0 Human Binding pIC50 = 7.6 7.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 371 4 1 5 3.3 Cc1cc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)cc(C)n1 nan
89554968 149675 None 0 Human Binding pIC50 = 7.6 7.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 407 4 1 5 3.4 CC1(C)OC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O nan
CHEMBL3946909 149675 None 0 Human Binding pIC50 = 7.6 7.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 407 4 1 5 3.4 CC1(C)OC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O nan
89554820 149962 None 0 Human Binding pIC50 = 7.6 7.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 417 4 1 5 3.5 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCCC(C(F)(F)F)C4)ccc23)cn1 nan
CHEMBL3949126 149962 None 0 Human Binding pIC50 = 7.6 7.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 417 4 1 5 3.5 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCCC(C(F)(F)F)C4)ccc23)cn1 nan
89554792 150485 None 0 Human Binding pIC50 = 7.6 7.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 414 5 2 4 3.2 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(C(F)F)C3)cc2n1 nan
CHEMBL3953648 150485 None 0 Human Binding pIC50 = 7.6 7.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 414 5 2 4 3.2 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(C(F)F)C3)cc2n1 nan
89554765 151552 None 0 Human Binding pIC50 = 7.6 7.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 404 5 1 6 3.2 COC(=O)c1cncn1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
CHEMBL3962095 151552 None 0 Human Binding pIC50 = 7.6 7.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 404 5 1 6 3.2 COC(=O)c1cncn1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
22224729 96182 None 0 Rat Binding pIC50 = 7.6 7.6 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 396 3 1 4 5.1 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3cccc(F)c3)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL260415 96182 None 0 Rat Binding pIC50 = 7.6 7.6 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 396 3 1 4 5.1 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3cccc(F)c3)cc2N1 10.1016/j.bmcl.2008.02.076
156020940 178212 None 0 Human Binding pIC50 = 7.6 7.6 - 0
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 489 6 2 6 4.5 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(Cl)cc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
CHEMBL4647980 178212 None 0 Human Binding pIC50 = 7.6 7.6 - 0
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 489 6 2 6 4.5 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(Cl)cc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
89554884 143295 None 0 Human Binding pIC50 = 6.6 6.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 365 4 1 6 2.0 C[C@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)CCO1 nan
CHEMBL3896344 143295 None 0 Human Binding pIC50 = 6.6 6.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 365 4 1 6 2.0 C[C@H]1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)CCO1 nan
89554835 149610 None 0 Human Binding pIC50 = 6.6 6.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 378 4 1 4 2.9 CN1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC1 nan
CHEMBL3946509 149610 None 0 Human Binding pIC50 = 6.6 6.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 378 4 1 4 2.9 CN1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC1 nan
44309103 102928 None 0 Rat Binding pIC50 = 5.6 5.6 - 0
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 323 4 0 4 4.5 Clc1ccc(/C(=C/n2cncn2)OC2CCCC2)c(Cl)c1 10.1016/s0960-894x(99)00346-7
CHEMBL305799 102928 None 0 Rat Binding pIC50 = 5.6 5.6 - 0
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 323 4 0 4 4.5 Clc1ccc(/C(=C/n2cncn2)OC2CCCC2)c(Cl)c1 10.1016/s0960-894x(99)00346-7
9845873 160893 None 0 Rat Binding pIC50 = 7.6 7.6 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 436 2 2 5 4.6 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL411440 160893 None 0 Rat Binding pIC50 = 7.6 7.6 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 436 2 2 5 4.6 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2008.02.076
44434259 88688 None 0 Rat Binding pIC50 = 7.6 7.6 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 336 1 1 2 4.5 O=C1CC(c2ccccc2)=Nc2ccc(C#Cc3ccccc3)cc2N1 10.1016/j.bmcl.2007.10.026
CHEMBL235806 88688 None 0 Rat Binding pIC50 = 7.6 7.6 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 336 1 1 2 4.5 O=C1CC(c2ccccc2)=Nc2ccc(C#Cc3ccccc3)cc2N1 10.1016/j.bmcl.2007.10.026
22448890 89353 None 0 Rat Binding pIC50 = 7.6 7.6 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 490 4 2 5 4.7 CC(C)(C)NC(=O)COc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(C#N)c1)=N2 10.1016/j.bmcl.2007.10.026
CHEMBL236883 89353 None 0 Rat Binding pIC50 = 7.6 7.6 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 490 4 2 5 4.7 CC(C)(C)NC(=O)COc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(C#N)c1)=N2 10.1016/j.bmcl.2007.10.026
9845873 160893 None 0 Rat Binding pIC50 = 7.6 7.6 - 0
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 436 2 2 5 4.6 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2007.12.005
CHEMBL411440 160893 None 0 Rat Binding pIC50 = 7.6 7.6 - 0
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 436 2 2 5 4.6 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2007.12.005
9845873 160893 None 0 Rat Binding pIC50 = 7.6 7.6 - 0
Displacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cells
ChEMBL 436 2 2 5 4.6 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2010.09.125
CHEMBL411440 160893 None 0 Rat Binding pIC50 = 7.6 7.6 - 0
Displacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cells
ChEMBL 436 2 2 5 4.6 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2010.09.125
22317318 56440 None 0 Rat Binding pIC50 = 7.6 7.6 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 395 2 1 3 5.5 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccccn3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631875 56440 None 0 Rat Binding pIC50 = 7.6 7.6 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 395 2 1 3 5.5 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccccn3)c1)=N2 10.1016/j.bmcl.2010.09.125
9845873 160893 None 0 Rat Binding pIC50 = 7.6 7.6 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 436 2 2 5 4.6 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2010.09.125
CHEMBL411440 160893 None 0 Rat Binding pIC50 = 7.6 7.6 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 436 2 2 5 4.6 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2010.09.125
89554791 159938 None 0 Human Binding pIC50 = 6.6 6.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 419 4 2 5 2.9 C[C@@H]1CN(Cc2ccc3c(-c4cn[nH]c4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1 nan
CHEMBL4106552 159938 None 0 Human Binding pIC50 = 6.6 6.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 419 4 2 5 2.9 C[C@@H]1CN(Cc2ccc3c(-c4cn[nH]c4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1 nan
22224765 88793 None 0 Rat Binding pIC50 = 4.6 4.6 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 343 1 2 4 3.1 CC(C)(O)C#Cc1ccc2c(c1)NC(=O)CC(c1cccc(C#N)c1)=N2 10.1016/j.bmcl.2007.10.026
CHEMBL236258 88793 None 0 Rat Binding pIC50 = 4.6 4.6 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 343 1 2 4 3.1 CC(C)(O)C#Cc1ccc2c(c1)NC(=O)CC(c1cccc(C#N)c1)=N2 10.1016/j.bmcl.2007.10.026
71565962 149728 None 0 Human Binding pIC50 = 6.6 6.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 462 5 1 6 4.1 NC(=O)c1cc(-c2cnc(C3CC3)s2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1 nan
CHEMBL3947299 149728 None 0 Human Binding pIC50 = 6.6 6.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 462 5 1 6 4.1 NC(=O)c1cc(-c2cnc(C3CC3)s2)c2ccc(CN3CCOC(C(F)(F)F)C3)cc2n1 nan
22224583 154693 None 0 Rat Binding pIC50 = 6.6 6.6 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 404 1 1 2 5.6 O=C1CC(c2cccc(C(F)(F)F)c2)=Nc2ccc(C#Cc3ccccc3)cc2N1 10.1016/j.bmcl.2007.10.026
CHEMBL399187 154693 None 0 Rat Binding pIC50 = 6.6 6.6 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 404 1 1 2 5.6 O=C1CC(c2cccc(C(F)(F)F)c2)=Nc2ccc(C#Cc3ccccc3)cc2N1 10.1016/j.bmcl.2007.10.026
44309086 206392 None 0 Rat Binding pIC50 = 5.6 5.6 - 0
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 346 5 0 5 4.2 Clc1ccc(/C(=C/n2cnnn2)OCc2ccccc2)c(Cl)c1 10.1016/s0960-894x(99)00346-7
CHEMBL69204 206392 None 0 Rat Binding pIC50 = 5.6 5.6 - 0
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 346 5 0 5 4.2 Clc1ccc(/C(=C/n2cnnn2)OCc2ccccc2)c(Cl)c1 10.1016/s0960-894x(99)00346-7
71566597 149960 None 0 Human Binding pIC50 = 7.6 7.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 405 4 1 4 3.4 CC1(C)CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O nan
CHEMBL3949122 149960 None 0 Human Binding pIC50 = 7.6 7.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 405 4 1 4 3.4 CC1(C)CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O nan
89554867 150172 None 0 Human Binding pIC50 = 7.6 7.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 412 6 1 5 4.2 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)cc1C nan
CHEMBL3950864 150172 None 0 Human Binding pIC50 = 7.6 7.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 412 6 1 5 4.2 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)cc1C nan
71565671 150597 None 0 Human Binding pIC50 = 7.6 7.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 389 5 1 5 2.7 COc1ccc(-c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)cc1 nan
CHEMBL3954513 150597 None 0 Human Binding pIC50 = 7.6 7.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 389 5 1 5 2.7 COc1ccc(-c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)cc1 nan
89554775 153924 None 0 Human Binding pIC50 = 7.6 7.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 476 5 2 6 3.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(S(=O)(=O)O)nc4ccccc43)cc2n1 nan
CHEMBL3982636 153924 None 0 Human Binding pIC50 = 7.6 7.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 476 5 2 6 3.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(S(=O)(=O)O)nc4ccccc43)cc2n1 nan
18548766 95916 None 0 Rat Binding pIC50 = 7.6 7.6 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 405 2 1 5 4.4 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2cc(Cl)c(C(F)(F)F)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL259053 95916 None 0 Rat Binding pIC50 = 7.6 7.6 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 405 2 1 5 4.4 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2cc(Cl)c(C(F)(F)F)cc2N1 10.1016/j.bmcl.2008.02.076
156019727 178097 None 0 Human Binding pIC50 = 5.6 5.6 - 0
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 497 7 2 6 4.9 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(C(C)C)cc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
CHEMBL4646222 178097 None 0 Human Binding pIC50 = 5.6 5.6 - 0
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 497 7 2 6 4.9 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(C(C)C)cc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
89554914 160708 None 0 Human Binding pIC50 = 6.6 6.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 447 4 1 6 3.2 Cc1c(-c2cc(C(N)=O)nc3cc(CN4C[C@@H](C)O[C@@H](C(F)(F)F)C4)ccc23)cnn1C nan
CHEMBL4112966 160708 None 0 Human Binding pIC50 = 6.6 6.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 447 4 1 6 3.2 Cc1c(-c2cc(C(N)=O)nc3cc(CN4C[C@@H](C)O[C@@H](C(F)(F)F)C4)ccc23)cnn1C nan
89554778 143440 None 0 Human Binding pIC50 = 6.6 6.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 408 5 3 5 1.6 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CC(O)CC3C(N)=O)cc2n1 nan
CHEMBL3897537 143440 None 0 Human Binding pIC50 = 6.6 6.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 408 5 3 5 1.6 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CC(O)CC3C(N)=O)cc2n1 nan
53320742 56436 None 0 Rat Binding pIC50 = 6.6 6.6 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 452 4 1 4 5.6 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(CN(C)C)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631871 56436 None 0 Rat Binding pIC50 = 6.6 6.6 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 452 4 1 4 5.6 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(CN(C)C)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
9868835 149040 None 0 Rat Binding pIC50 = 6.6 6.6 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 459 2 1 5 4.2 CN1CCN(c2cc3c(cc2C#Cc2ccccc2)NC(=O)CC(c2cccc(C#N)c2)=N3)CC1 10.1016/j.bmcl.2007.10.026
CHEMBL394201 149040 None 0 Rat Binding pIC50 = 6.6 6.6 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 459 2 1 5 4.2 CN1CCN(c2cc3c(cc2C#Cc2ccccc2)NC(=O)CC(c2cccc(C#N)c2)=N3)CC1 10.1016/j.bmcl.2007.10.026
89554888 142696 None 0 Human Binding pIC50 = 7.6 7.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 411 4 1 5 3.7 Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cccc(C(F)(F)F)n4)ccc23)cn1 nan
CHEMBL3891468 142696 None 0 Human Binding pIC50 = 7.6 7.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 411 4 1 5 3.7 Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cccc(C(F)(F)F)n4)ccc23)cn1 nan
89554859 150115 None 0 Human Binding pIC50 = 7.6 7.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 429 4 1 5 3.9 Cn1cc(-c2cc(C(N)=O)nc3c(F)c(Cc4ccc(C(F)(F)F)nc4)ccc23)cn1 nan
CHEMBL3950438 150115 None 0 Human Binding pIC50 = 7.6 7.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 429 4 1 5 3.9 Cn1cc(-c2cc(C(N)=O)nc3c(F)c(Cc4ccc(C(F)(F)F)nc4)ccc23)cn1 nan
71565521 150572 None 0 Human Binding pIC50 = 7.6 7.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 431 4 1 4 4.0 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CC4(CCCC4)C3=O)cc2n1 nan
CHEMBL3954371 150572 None 0 Human Binding pIC50 = 7.6 7.6 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 431 4 1 4 4.0 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CC4(CCCC4)C3=O)cc2n1 nan
22448614 89351 None 0 Rat Binding pIC50 = 7.6 7.6 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 435 5 1 5 4.4 COCCOc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(C#N)c1)=N2 10.1016/j.bmcl.2007.10.026
CHEMBL236881 89351 None 0 Rat Binding pIC50 = 7.6 7.6 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 435 5 1 5 4.4 COCCOc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(C#N)c1)=N2 10.1016/j.bmcl.2007.10.026
44434256 88639 None 0 Rat Binding pIC50 = 5.6 5.6 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 284 1 1 2 4.1 Cc1ccc2c(c1)NC(=O)CC(c1cccc(Cl)c1)=N2 10.1016/j.bmcl.2007.10.026
CHEMBL235599 88639 None 0 Rat Binding pIC50 = 5.6 5.6 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 284 1 1 2 4.1 Cc1ccc2c(c1)NC(=O)CC(c1cccc(Cl)c1)=N2 10.1016/j.bmcl.2007.10.026
71565526 151535 None 0 Human Binding pIC50 = 7.5 7.5 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 365 4 1 4 3.0 NC(=O)c1cc(C2CCCCC2)c2ccc(CN3C(=O)CCC3=O)cc2n1 nan
CHEMBL3961948 151535 None 0 Human Binding pIC50 = 7.5 7.5 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 365 4 1 4 3.0 NC(=O)c1cc(C2CCCCC2)c2ccc(CN3C(=O)CCC3=O)cc2n1 nan
18548910 95987 None 0 Rat Binding pIC50 = 7.5 7.5 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 401 3 1 6 3.8 COc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
CHEMBL259340 95987 None 0 Rat Binding pIC50 = 7.5 7.5 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 401 3 1 6 3.8 COc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
22317258 56439 None 0 Rat Binding pIC50 = 7.5 7.5 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 480 3 1 5 5.4 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(N4CCOCC4)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631874 56439 None 0 Rat Binding pIC50 = 7.5 7.5 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 480 3 1 5 5.4 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(N4CCOCC4)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
11279365 67581 None 0 Rat Binding pIC50 = 7.5 7.5 1 2
Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells
ChEMBL 343 5 3 4 1.5 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL189814 67581 None 0 Rat Binding pIC50 = 7.5 7.5 1 2
Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells
ChEMBL 343 5 3 4 1.5 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
44434258 88640 None 0 Rat Binding pIC50 = 5.5 5.5 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 275 1 1 3 3.3 Cc1ccc2c(c1)NC(=O)CC(c1cccc(C#N)c1)=N2 10.1016/j.bmcl.2007.10.026
CHEMBL235600 88640 None 0 Rat Binding pIC50 = 5.5 5.5 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 275 1 1 3 3.3 Cc1ccc2c(c1)NC(=O)CC(c1cccc(C#N)c1)=N2 10.1016/j.bmcl.2007.10.026
11158623 3351 None 11 Human Binding pIC50 = 6.5 6.5 -8 2
Negative allosteric modulation of mGlu2 by cell-based assayNegative allosteric modulation of mGlu2 by cell-based assay
ChEMBL 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 10.1016/j.bmcl.2012.04.112
6226 3351 None 11 Human Binding pIC50 = 6.5 6.5 -8 2
Negative allosteric modulation of mGlu2 by cell-based assayNegative allosteric modulation of mGlu2 by cell-based assay
ChEMBL 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 10.1016/j.bmcl.2012.04.112
CHEMBL1629855 3351 None 11 Human Binding pIC50 = 6.5 6.5 -8 2
Negative allosteric modulation of mGlu2 by cell-based assayNegative allosteric modulation of mGlu2 by cell-based assay
ChEMBL 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 10.1016/j.bmcl.2012.04.112
11158623 3351 None 11 Human Binding pIC50 = 6.5 6.5 -8 2
Negative allosteric modulation of mGlu2 receptor (unknown origin)Negative allosteric modulation of mGlu2 receptor (unknown origin)
ChEMBL 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 10.1021/jm400439t
6226 3351 None 11 Human Binding pIC50 = 6.5 6.5 -8 2
Negative allosteric modulation of mGlu2 receptor (unknown origin)Negative allosteric modulation of mGlu2 receptor (unknown origin)
ChEMBL 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 10.1021/jm400439t
CHEMBL1629855 3351 None 11 Human Binding pIC50 = 6.5 6.5 -8 2
Negative allosteric modulation of mGlu2 receptor (unknown origin)Negative allosteric modulation of mGlu2 receptor (unknown origin)
ChEMBL 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 10.1021/jm400439t
89543886 148862 None 0 Human Binding pIC50 = 6.5 6.5 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 363 3 1 3 3.4 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(C(=O)N3CCCC3)cc2n1 nan
CHEMBL3940628 148862 None 0 Human Binding pIC50 = 6.5 6.5 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 363 3 1 3 3.4 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(C(=O)N3CCCC3)cc2n1 nan
44452714 159361 None 0 Human Binding pIC50 = 8.5 8.5 - 0
Displacement of [3H]-MGS0008 from mGluR2 expressed in CHO cellsDisplacement of [3H]-MGS0008 from mGluR2 expressed in CHO cells
ChEMBL 371 5 3 4 2.9 N[C@](CC1c2ccccc2Oc2ccccc21)(C(=O)O)[C@H]1C[C@]1(F)C(=O)O 10.1016/j.bmc.2008.02.066
CHEMBL409928 159361 None 0 Human Binding pIC50 = 8.5 8.5 - 0
Displacement of [3H]-MGS0008 from mGluR2 expressed in CHO cellsDisplacement of [3H]-MGS0008 from mGluR2 expressed in CHO cells
ChEMBL 371 5 3 4 2.9 N[C@](CC1c2ccccc2Oc2ccccc21)(C(=O)O)[C@H]1C[C@]1(F)C(=O)O 10.1016/j.bmc.2008.02.066
71566669 145572 None 0 Human Binding pIC50 = 7.5 7.5 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 419 5 1 4 3.8 CCC1(C)CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O nan
CHEMBL3914560 145572 None 0 Human Binding pIC50 = 7.5 7.5 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 419 5 1 4 3.8 CCC1(C)CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O nan
89554938 146763 None 0 Human Binding pIC50 = 7.5 7.5 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 401 5 1 5 3.7 Cn1cc(-c2cc(C(N)=O)nc3c(F)c(Cc4ccc(C5CC5)nc4)ccc23)cn1 nan
CHEMBL3923798 146763 None 0 Human Binding pIC50 = 7.5 7.5 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 401 5 1 5 3.7 Cn1cc(-c2cc(C(N)=O)nc3c(F)c(Cc4ccc(C5CC5)nc4)ccc23)cn1 nan
89554823 149120 None 0 Human Binding pIC50 = 7.5 7.5 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 385 4 1 5 3.0 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCCC(F)(F)C4)ccc23)cn1 nan
CHEMBL3942629 149120 None 0 Human Binding pIC50 = 7.5 7.5 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 385 4 1 5 3.0 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCCC(F)(F)C4)ccc23)cn1 nan
22224615 90098 None 0 Rat Binding pIC50 = 7.5 7.5 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 379 1 1 3 4.6 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4F)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
CHEMBL238167 90098 None 0 Rat Binding pIC50 = 7.5 7.5 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 379 1 1 3 4.6 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4F)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
22224975 88791 None 0 Rat Binding pIC50 = 6.5 6.5 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 368 1 1 5 3.9 N#Cc1cccc(C2=Nc3ccc(C#Cc4nccs4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
CHEMBL236256 88791 None 0 Rat Binding pIC50 = 6.5 6.5 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 368 1 1 5 3.9 N#Cc1cccc(C2=Nc3ccc(C#Cc4nccs4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
10359073 155064 None 0 Human Binding pIC50 = 5.5 5.5 -2 2
Inhibitory activity against human Metabotropic glutamate receptor 2Inhibitory activity against human Metabotropic glutamate receptor 2
ChEMBL 327 8 3 3 2.7 N[C@@H](C[C@H](CC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O 10.1021/jm980571q
CHEMBL40123 155064 None 0 Human Binding pIC50 = 5.5 5.5 -2 2
Inhibitory activity against human Metabotropic glutamate receptor 2Inhibitory activity against human Metabotropic glutamate receptor 2
ChEMBL 327 8 3 3 2.7 N[C@@H](C[C@H](CC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O 10.1021/jm980571q
89554903 152739 None 0 Human Binding pIC50 = 5.5 5.5 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 345 3 0 3 4.0 N#Cc1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC3=O)cc2n1 nan
CHEMBL3972456 152739 None 0 Human Binding pIC50 = 5.5 5.5 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 345 3 0 3 4.0 N#Cc1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC3=O)cc2n1 nan
71566274 146980 None 0 Human Binding pIC50 = 7.5 7.5 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 371 4 1 3 4.4 Cc1ccncc1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
CHEMBL3925507 146980 None 0 Human Binding pIC50 = 7.5 7.5 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 371 4 1 3 4.4 Cc1ccncc1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
71565738 150352 None 0 Human Binding pIC50 = 7.5 7.5 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 414 6 1 5 4.0 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cc(C(=O)C4CC4)cn3)cc2n1 nan
CHEMBL3952509 150352 None 0 Human Binding pIC50 = 7.5 7.5 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 414 6 1 5 4.0 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cc(C(=O)C4CC4)cn3)cc2n1 nan
71565805 152407 None 0 Human Binding pIC50 = 7.5 7.5 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 404 5 1 6 3.2 COC(=O)c1cnn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)c1 nan
CHEMBL3969686 152407 None 0 Human Binding pIC50 = 7.5 7.5 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 404 5 1 6 3.2 COC(=O)c1cnn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)c1 nan
71566206 153736 None 0 Human Binding pIC50 = 7.5 7.5 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 387 5 1 4 4.1 COc1cncc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)c1 nan
CHEMBL3981039 153736 None 0 Human Binding pIC50 = 7.5 7.5 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 387 5 1 4 4.1 COc1cncc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)c1 nan
89554764 154044 None 0 Human Binding pIC50 = 7.5 7.5 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 388 5 1 4 4.5 CC(C)c1nccn1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
CHEMBL3983614 154044 None 0 Human Binding pIC50 = 7.5 7.5 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 388 5 1 4 4.5 CC(C)c1nccn1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
22224825 159086 None 0 Rat Binding pIC50 = 7.5 7.5 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 397 3 1 5 4.5 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL409638 159086 None 0 Rat Binding pIC50 = 7.5 7.5 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 397 3 1 5 4.5 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(-c3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2008.02.076
44309101 206022 None 0 Rat Binding pIC50 = 5.5 5.5 - 0
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 278 6 0 5 3.1 CCCCO/C(=C\n1ncnn1)c1ccc(Cl)cc1 10.1016/s0960-894x(99)00346-7
CHEMBL66701 206022 None 0 Rat Binding pIC50 = 5.5 5.5 - 0
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 278 6 0 5 3.1 CCCCO/C(=C\n1ncnn1)c1ccc(Cl)cc1 10.1016/s0960-894x(99)00346-7
22224682 89643 None 0 Rat Binding pIC50 = 7.5 7.5 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 367 1 1 4 4.5 N#Cc1cccc(C2=Nc3ccc(C#Cc4cccs4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
CHEMBL237523 89643 None 0 Rat Binding pIC50 = 7.5 7.5 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 367 1 1 4 4.5 N#Cc1cccc(C2=Nc3ccc(C#Cc4cccs4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
89554733 142627 None 0 Human Binding pIC50 = 7.5 7.5 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 452 5 1 7 3.2 COc1ncc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)s1 nan
CHEMBL3890866 142627 None 0 Human Binding pIC50 = 7.5 7.5 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 452 5 1 7 3.2 COc1ncc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)s1 nan
71566126 148870 None 0 Human Binding pIC50 = 7.5 7.5 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 430 6 2 5 4.5 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4N)ccc23)c(F)c1 nan
CHEMBL3940665 148870 None 0 Human Binding pIC50 = 7.5 7.5 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 430 6 2 5 4.5 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4N)ccc23)c(F)c1 nan
89554774 153965 None 0 Human Binding pIC50 = 6.5 6.5 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 392 5 1 4 3.3 CN(C)C1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1 nan
CHEMBL3982968 153965 None 0 Human Binding pIC50 = 6.5 6.5 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 392 5 1 4 3.3 CN(C)C1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1 nan
89543925 152514 None 0 Human Binding pIC50 = 6.5 6.5 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 284 2 1 2 3.3 NC(=O)c1cc(-c2ccc(F)cc2)c2cccc(F)c2n1 nan
CHEMBL3970688 152514 None 0 Human Binding pIC50 = 6.5 6.5 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 284 2 1 2 3.3 NC(=O)c1cc(-c2ccc(F)cc2)c2cccc(F)c2n1 nan
89554911 143081 None 0 Human Binding pIC50 = 7.5 7.5 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 446 4 2 4 3.9 CC1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC(C(F)(F)F)N1 nan
CHEMBL3894556 143081 None 0 Human Binding pIC50 = 7.5 7.5 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 446 4 2 4 3.9 CC1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC(C(F)(F)F)N1 nan
89554971 147372 None 0 Human Binding pIC50 = 7.5 7.5 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 378 4 1 6 2.8 Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cnc(Cl)nc4)ccc23)cn1 nan
CHEMBL3928860 147372 None 0 Human Binding pIC50 = 7.5 7.5 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 378 4 1 6 2.8 Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cnc(Cl)nc4)ccc23)cn1 nan
9820321 155098 None 0 Rat Binding pIC50 = 7.5 7.5 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 361 1 1 3 4.4 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.12.005
9820321 155098 None 0 Rat Binding pIC50 = 7.5 7.5 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 361 1 1 3 4.4 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2008.02.076
CHEMBL401446 155098 None 0 Rat Binding pIC50 = 7.5 7.5 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 361 1 1 3 4.4 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.12.005
CHEMBL401446 155098 None 0 Rat Binding pIC50 = 7.5 7.5 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 361 1 1 3 4.4 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2008.02.076
22224841 90097 None 0 Rat Binding pIC50 = 7.5 7.5 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 379 1 1 3 4.6 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccc(F)cc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
CHEMBL238166 90097 None 0 Rat Binding pIC50 = 7.5 7.5 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 379 1 1 3 4.6 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccc(F)cc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
9820321 155098 None 0 Rat Binding pIC50 = 7.5 7.5 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 361 1 1 3 4.4 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
CHEMBL401446 155098 None 0 Rat Binding pIC50 = 7.5 7.5 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 361 1 1 3 4.4 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
9820321 155098 None 0 Rat Binding pIC50 = 7.5 7.5 - 0
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 361 1 1 3 4.4 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.12.005
CHEMBL401446 155098 None 0 Rat Binding pIC50 = 7.5 7.5 - 0
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 361 1 1 3 4.4 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.12.005
9820321 155098 None 0 Rat Binding pIC50 = 7.5 7.5 - 0
Displacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cells
ChEMBL 361 1 1 3 4.4 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2010.09.125
CHEMBL401446 155098 None 0 Rat Binding pIC50 = 7.5 7.5 - 0
Displacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cells
ChEMBL 361 1 1 3 4.4 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2010.09.125
44285839 100206 None 0 Human Binding pIC50 = 7.5 7.5 - 0
Inhibitory activity against human Metabotropic glutamate receptor 2Inhibitory activity against human Metabotropic glutamate receptor 2
ChEMBL 353 4 3 4 2.9 CC1c2ccccc2Oc2cccc([C@@](N)(C(=O)O)[C@H]3C[C@@H]3C(=O)O)c21 10.1021/jm980571q
CHEMBL287831 100206 None 0 Human Binding pIC50 = 7.5 7.5 - 0
Inhibitory activity against human Metabotropic glutamate receptor 2Inhibitory activity against human Metabotropic glutamate receptor 2
ChEMBL 353 4 3 4 2.9 CC1c2ccccc2Oc2cccc([C@@](N)(C(=O)O)[C@H]3C[C@@H]3C(=O)O)c21 10.1021/jm980571q
9820321 155098 None 0 Rat Binding pIC50 = 7.5 7.5 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 361 1 1 3 4.4 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2010.09.125
CHEMBL401446 155098 None 0 Rat Binding pIC50 = 7.5 7.5 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 361 1 1 3 4.4 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2010.09.125
117642059 143796 None 0 Human Binding pIC50 = 7.5 7.5 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 428 4 1 4 4.5 Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4ccc(F)c(C(F)(F)F)c4)ccc23)cn1 nan
CHEMBL3900371 143796 None 0 Human Binding pIC50 = 7.5 7.5 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 428 4 1 4 4.5 Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4ccc(F)c(C(F)(F)F)c4)ccc23)cn1 nan
53318106 56420 None 0 Rat Binding pIC50 = 6.5 6.5 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 385 2 1 4 5.1 Cc1nc(-c2cccc(C3=Nc4ccc(C(F)(F)F)cc4NC(=O)C3)c2)co1 10.1016/j.bmcl.2010.09.125
CHEMBL1631855 56420 None 0 Rat Binding pIC50 = 6.5 6.5 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 385 2 1 4 5.1 Cc1nc(-c2cccc(C3=Nc4ccc(C(F)(F)F)cc4NC(=O)C3)c2)co1 10.1016/j.bmcl.2010.09.125
22224908 88785 None 0 Rat Binding pIC50 = 6.5 6.5 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 379 2 2 3 3.6 NC(=O)c1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
CHEMBL236244 88785 None 0 Rat Binding pIC50 = 6.5 6.5 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 379 2 2 3 3.6 NC(=O)c1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
117642047 142621 None 0 Human Binding pIC50 = 7.4 7.4 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 473 6 2 6 3.9 CC[C@](O)(c1cn(Cc2ccc3c(-c4ccccc4F)cc(C(N)=O)nc3c2)nn1)C(F)(F)F nan
CHEMBL3890814 142621 None 0 Human Binding pIC50 = 7.4 7.4 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 473 6 2 6 3.9 CC[C@](O)(c1cn(Cc2ccc3c(-c4ccccc4F)cc(C(N)=O)nc3c2)nn1)C(F)(F)F nan
89554868 149430 None 0 Human Binding pIC50 = 7.4 7.4 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 402 5 1 6 3.1 Cn1cc(-c2cc(C(N)=O)nc3c(F)c(Cc4cnc(C5CC5)nc4)ccc23)cn1 nan
CHEMBL3945166 149430 None 0 Human Binding pIC50 = 7.4 7.4 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 402 5 1 6 3.1 Cn1cc(-c2cc(C(N)=O)nc3c(F)c(Cc4cnc(C5CC5)nc4)ccc23)cn1 nan
10204007 97570 None 0 Rat Binding pIC50 = 7.4 7.4 - 0
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 446 3 1 6 4.2 CN(C)c1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2007.12.005
CHEMBL270402 97570 None 0 Rat Binding pIC50 = 7.4 7.4 - 0
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 446 3 1 6 4.2 CN(C)c1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2007.12.005
89554759 160140 None 0 Human Binding pIC50 = 7.4 7.4 - 0
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 474 6 2 7 3.3 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cn4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
CHEMBL4108213 160140 None 0 Human Binding pIC50 = 7.4 7.4 - 0
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 474 6 2 7 3.3 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cn4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
156015207 177678 None 0 Human Binding pIC50 = 7.4 7.4 - 0
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 473 6 2 6 3.9 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccccc4F)cc(C(N)=O)nc3c2)nn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
CHEMBL4640529 177678 None 0 Human Binding pIC50 = 7.4 7.4 - 0
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 473 6 2 6 3.9 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccccc4F)cc(C(N)=O)nc3c2)nn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
22224803 89949 None 0 Rat Binding pIC50 = 6.4 6.4 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 449 2 1 4 4.0 O=C1CC(c2cccc(C(=O)N3CCOCC3)c2)=Nc2ccc(C#Cc3ccccc3)cc2N1 10.1016/j.bmcl.2007.10.026
CHEMBL237938 89949 None 0 Rat Binding pIC50 = 6.4 6.4 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 449 2 1 4 4.0 O=C1CC(c2cccc(C(=O)N3CCOCC3)c2)=Nc2ccc(C#Cc3ccccc3)cc2N1 10.1016/j.bmcl.2007.10.026
156013741 177371 None 0 Human Binding pIC50 = 6.4 6.4 - 0
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 282 1 1 4 2.3 O=c1[nH]nc2ccccccc(-c3ccc(F)cc3)nn12 10.1016/j.bmcl.2020.127066
CHEMBL4636186 177371 None 0 Human Binding pIC50 = 6.4 6.4 - 0
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 282 1 1 4 2.3 O=c1[nH]nc2ccccccc(-c3ccc(F)cc3)nn12 10.1016/j.bmcl.2020.127066
71566438 152950 None 0 Human Binding pIC50 = 6.4 6.4 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 296 2 1 2 4.0 Cc1cc(Cl)ccc1-c1cc(C(N)=O)nc2ccccc12 nan
CHEMBL3974279 152950 None 0 Human Binding pIC50 = 6.4 6.4 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 296 2 1 2 4.0 Cc1cc(Cl)ccc1-c1cc(C(N)=O)nc2ccccc12 nan
89554845 146497 None 0 Human Binding pIC50 = 6.4 6.4 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 296 2 1 2 4.0 Cc1ccc2c(-c3ccccc3Cl)cc(C(N)=O)nc2c1 nan
CHEMBL3921799 146497 None 0 Human Binding pIC50 = 6.4 6.4 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 296 2 1 2 4.0 Cc1ccc2c(-c3ccccc3Cl)cc(C(N)=O)nc2c1 nan
22448617 89084 None 0 Rat Binding pIC50 = 6.4 6.4 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 446 2 1 5 4.3 N#Cc1cccc(C2=Nc3cc(N4CCOCC4)c(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
CHEMBL236467 89084 None 0 Rat Binding pIC50 = 6.4 6.4 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 446 2 1 5 4.3 N#Cc1cccc(C2=Nc3cc(N4CCOCC4)c(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
136152920 95266 None 0 Rat Binding pIC50 = 6.4 6.4 - 0
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 467 3 3 7 3.5 O=C1CC(c2cccc(-n3nncc3CO)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2007.12.005
CHEMBL256008 95266 None 0 Rat Binding pIC50 = 6.4 6.4 - 0
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 467 3 3 7 3.5 O=C1CC(c2cccc(-n3nncc3CO)c2)=Nc2cc(O)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2007.12.005
71566600 146285 None 0 Human Binding pIC50 = 7.4 7.4 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 378 4 2 4 2.2 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CNC3=O)cc2n1 nan
CHEMBL3920092 146285 None 0 Human Binding pIC50 = 7.4 7.4 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 378 4 2 4 2.2 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CNC3=O)cc2n1 nan
89554814 152972 None 0 Human Binding pIC50 = 7.4 7.4 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 469 4 1 5 4.4 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCn4cc(C(F)(F)F)nc4C3)cc2n1 nan
CHEMBL3974523 152972 None 0 Human Binding pIC50 = 7.4 7.4 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 469 4 1 5 4.4 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCn4cc(C(F)(F)F)nc4C3)cc2n1 nan
18613455 96103 None 0 Rat Binding pIC50 = 7.4 7.4 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 414 3 1 6 3.8 CN(C)c1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
CHEMBL259924 96103 None 0 Rat Binding pIC50 = 7.4 7.4 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 414 3 1 6 3.8 CN(C)c1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
89554808 145312 None 0 Human Binding pIC50 = 6.4 6.4 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 378 4 2 4 3.1 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC(N)CC3)cc2n1 nan
CHEMBL3912631 145312 None 0 Human Binding pIC50 = 6.4 6.4 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 378 4 2 4 3.1 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC(N)CC3)cc2n1 nan
89554869 144754 None 0 Human Binding pIC50 = 7.4 7.4 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 389 4 1 5 3.5 Cc1cc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2F)cc(C)n1 nan
CHEMBL3908309 144754 None 0 Human Binding pIC50 = 7.4 7.4 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 389 4 1 5 3.5 Cc1cc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2F)cc(C)n1 nan
89554849 151044 None 0 Human Binding pIC50 = 7.4 7.4 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 391 5 1 6 2.9 COc1ccc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2F)cn1 nan
CHEMBL3958094 151044 None 0 Human Binding pIC50 = 7.4 7.4 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 391 5 1 6 2.9 COc1ccc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2F)cn1 nan
22224570 95968 None 0 Rat Binding pIC50 = 7.4 7.4 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 378 3 1 4 5.0 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccccc3)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL259269 95968 None 0 Rat Binding pIC50 = 7.4 7.4 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 378 3 1 4 5.0 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3ccccc3)cc2N1 10.1016/j.bmcl.2008.02.076
53316798 56421 None 0 Rat Binding pIC50 = 7.4 7.4 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 384 2 1 4 4.6 Cn1nccc1-c1cccc(C2=Nc3ccc(C(F)(F)F)cc3NC(=O)C2)c1 10.1016/j.bmcl.2010.09.125
CHEMBL1631856 56421 None 0 Rat Binding pIC50 = 7.4 7.4 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 384 2 1 4 4.6 Cn1nccc1-c1cccc(C2=Nc3ccc(C(F)(F)F)cc3NC(=O)C2)c1 10.1016/j.bmcl.2010.09.125
89554811 147950 None 0 Human Binding pIC50 = 6.4 6.4 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 379 4 2 4 3.1 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC(O)CC3)cc2n1 nan
CHEMBL3933190 147950 None 0 Human Binding pIC50 = 6.4 6.4 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 379 4 2 4 3.1 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC(O)CC3)cc2n1 nan
71566521 143414 None 0 Human Binding pIC50 = 6.4 6.4 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 280 2 1 2 3.4 Cc1ccc2c(-c3ccccc3F)cc(C(N)=O)nc2c1 nan
CHEMBL3897268 143414 None 0 Human Binding pIC50 = 6.4 6.4 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 280 2 1 2 3.4 Cc1ccc2c(-c3ccccc3F)cc(C(N)=O)nc2c1 nan
89554885 144391 None 0 Human Binding pIC50 = 6.4 6.4 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 365 4 1 6 2.0 C[C@H]1COCCN1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1 nan
CHEMBL3905282 144391 None 0 Human Binding pIC50 = 6.4 6.4 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 365 4 1 6 2.0 C[C@H]1COCCN1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1 nan
89554951 154362 None 0 Human Binding pIC50 = 6.4 6.4 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 361 3 0 5 3.4 N#Cc1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)COC3=O)cc2n1 nan
CHEMBL3986465 154362 None 0 Human Binding pIC50 = 6.4 6.4 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 361 3 0 5 3.4 N#Cc1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)COC3=O)cc2n1 nan
89554872 149486 None 0 Human Binding pIC50 = 8.4 8.4 - 1
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 416 6 1 5 4.0 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)cc1F nan
CHEMBL3945590 149486 None 0 Human Binding pIC50 = 8.4 8.4 - 1
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 416 6 1 5 4.0 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)cc1F nan
44450479 96316 None 0 Rat Binding pIC50 = 8.4 8.4 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 398 3 1 4 4.9 CCc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2008.02.076
CHEMBL261050 96316 None 0 Rat Binding pIC50 = 8.4 8.4 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 398 3 1 4 4.9 CCc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2008.02.076
11235624 56321 None 0 Rat Binding pIC50 = 8.4 8.4 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 425 4 1 4 5.6 CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncc3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1629862 56321 None 0 Rat Binding pIC50 = 8.4 8.4 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 425 4 1 4 5.6 CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncc3)c1)=N2 10.1016/j.bmcl.2010.09.125
11304010 56323 None 0 Rat Binding pIC50 = 8.4 8.4 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 395 2 1 3 5.8 Cc1cc(-c2cccc(C3=Nc4cc(Cl)c(Cl)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
CHEMBL1629864 56323 None 0 Rat Binding pIC50 = 8.4 8.4 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 395 2 1 3 5.8 Cc1cc(-c2cccc(C3=Nc4cc(Cl)c(Cl)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
11474913 56423 None 0 Rat Binding pIC50 = 8.4 8.4 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 395 2 1 3 5.5 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncc3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631858 56423 None 0 Rat Binding pIC50 = 8.4 8.4 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 395 2 1 3 5.5 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncc3)c1)=N2 10.1016/j.bmcl.2010.09.125
11281280 56424 None 0 Rat Binding pIC50 = 8.4 8.4 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 409 2 1 3 5.8 Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
CHEMBL1631859 56424 None 0 Rat Binding pIC50 = 8.4 8.4 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 409 2 1 3 5.8 Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
22317431 56429 None 0 Rat Binding pIC50 = 8.4 8.4 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 437 3 1 3 6.7 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C(C)C)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631864 56429 None 0 Rat Binding pIC50 = 8.4 8.4 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 437 3 1 3 6.7 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C(C)C)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
11559750 96008 None 0 Human Binding pIC50 = 8.4 8.4 - 0
Displacement of [3H]-MGS0008 from mGluR2 expressed in CHO cellsDisplacement of [3H]-MGS0008 from mGluR2 expressed in CHO cells
ChEMBL 371 5 3 4 2.9 NC(CC1c2ccccc2Oc2ccccc21)(C(=O)O)C1CC1(F)C(=O)O 10.1016/j.bmc.2008.02.066
CHEMBL259435 96008 None 0 Human Binding pIC50 = 8.4 8.4 - 0
Displacement of [3H]-MGS0008 from mGluR2 expressed in CHO cellsDisplacement of [3H]-MGS0008 from mGluR2 expressed in CHO cells
ChEMBL 371 5 3 4 2.9 NC(CC1c2ccccc2Oc2ccccc21)(C(=O)O)C1CC1(F)C(=O)O 10.1016/j.bmc.2008.02.066
71565740 144657 None 0 Human Binding pIC50 = 7.4 7.4 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 418 6 1 6 3.6 CCOC(=O)c1cnn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)c1 nan
CHEMBL3907527 144657 None 0 Human Binding pIC50 = 7.4 7.4 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 418 6 1 6 3.6 CCOC(=O)c1cnn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)c1 nan
22448643 89085 None 0 Rat Binding pIC50 = 7.4 7.4 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 462 2 1 5 5.0 N#Cc1cccc(C2=Nc3cc(N4CCSCC4)c(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
CHEMBL236468 89085 None 0 Rat Binding pIC50 = 7.4 7.4 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 462 2 1 5 5.0 N#Cc1cccc(C2=Nc3cc(N4CCSCC4)c(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
53324715 56435 None 0 Rat Binding pIC50 = 7.4 7.4 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 453 3 2 4 5.8 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C(C)(C)O)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631870 56435 None 0 Rat Binding pIC50 = 7.4 7.4 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 453 3 2 4 5.8 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C(C)(C)O)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
11382367 66958 None 0 Rat Binding pIC50 = 7.4 7.4 1 2
Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells
ChEMBL 345 5 3 4 1.1 N[C@@]1(C(=O)O)[C@H](OCc2ccc(F)c(F)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL186630 66958 None 0 Rat Binding pIC50 = 7.4 7.4 1 2
Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells
ChEMBL 345 5 3 4 1.1 N[C@@]1(C(=O)O)[C@H](OCc2ccc(F)c(F)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
22224567 167507 None 0 Rat Binding pIC50 = 6.4 6.4 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 325 1 1 3 3.9 C=C(C)C#Cc1ccc2c(c1)NC(=O)CC(c1cccc(C#N)c1)=N2 10.1016/j.bmcl.2007.10.026
CHEMBL429629 167507 None 0 Rat Binding pIC50 = 6.4 6.4 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 325 1 1 3 3.9 C=C(C)C#Cc1ccc2c(c1)NC(=O)CC(c1cccc(C#N)c1)=N2 10.1016/j.bmcl.2007.10.026
6324634 148032 None 10 Human Binding pIC50 = 6.4 6.4 -1 2
Inhibitory activity against human Metabotropic glutamate receptor 2Inhibitory activity against human Metabotropic glutamate receptor 2
ChEMBL 355 10 3 3 3.5 N[C@@H](C[C@H](CCCC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O 10.1021/jm980571q
CHEMBL39338 148032 None 10 Human Binding pIC50 = 6.4 6.4 -1 2
Inhibitory activity against human Metabotropic glutamate receptor 2Inhibitory activity against human Metabotropic glutamate receptor 2
ChEMBL 355 10 3 3 3.5 N[C@@H](C[C@H](CCCC(c1ccccc1)c1ccccc1)C(=O)O)C(=O)O 10.1021/jm980571q
156009702 177276 None 0 Human Binding pIC50 = 6.4 6.4 - 0
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 277 1 1 1 3.9 O=C1NCc2c1cc(-c1ccc(F)cc1)c1ccccc21 10.1016/j.bmcl.2020.127066
CHEMBL4634600 177276 None 0 Human Binding pIC50 = 6.4 6.4 - 0
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 277 1 1 1 3.9 O=C1NCc2c1cc(-c1ccc(F)cc1)c1ccccc21 10.1016/j.bmcl.2020.127066
71566442 145335 None 0 Human Binding pIC50 = 6.4 6.4 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 276 2 1 2 3.6 Cc1ccc(-c2cc(C(N)=O)nc3cc(C)ccc23)cc1 nan
CHEMBL3912824 145335 None 0 Human Binding pIC50 = 6.4 6.4 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 276 2 1 2 3.6 Cc1ccc(-c2cc(C(N)=O)nc3cc(C)ccc23)cc1 nan
156017399 177819 None 0 Human Binding pIC50 = 6.4 6.4 - 0
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 455 5 1 6 4.7 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C#N)nc3c2)nn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
CHEMBL4642255 177819 None 0 Human Binding pIC50 = 6.4 6.4 - 0
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 455 5 1 6 4.7 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C#N)nc3c2)nn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
117642070 151138 None 0 Human Binding pIC50 = 7.4 7.4 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 374 5 1 7 2.1 COc1ncc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)cn1 nan
CHEMBL3958736 151138 None 0 Human Binding pIC50 = 7.4 7.4 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 374 5 1 7 2.1 COc1ncc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)cn1 nan
71566668 144313 None 0 Human Binding pIC50 = 6.4 6.4 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 359 3 0 4 3.6 N#Cc1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1 nan
CHEMBL3904529 144313 None 0 Human Binding pIC50 = 6.4 6.4 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 359 3 0 4 3.6 N#Cc1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1 nan
89554730 143101 None 0 Human Binding pIC50 = 7.4 7.4 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 413 4 1 4 3.1 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCCS3(=O)=O)cc2n1 nan
CHEMBL3894724 143101 None 0 Human Binding pIC50 = 7.4 7.4 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 413 4 1 4 3.1 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCCS3(=O)=O)cc2n1 nan
89554897 145503 None 0 Human Binding pIC50 = 7.4 7.4 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 411 4 1 5 3.7 Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cccnc4C(F)(F)F)ccc23)cn1 nan
CHEMBL3914040 145503 None 0 Human Binding pIC50 = 7.4 7.4 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 411 4 1 5 3.7 Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cccnc4C(F)(F)F)ccc23)cn1 nan
89554771 149748 None 0 Human Binding pIC50 = 7.4 7.4 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 473 5 1 5 5.6 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(-c4cccnc4)nc4ccccc43)cc2n1 nan
CHEMBL3947441 149748 None 0 Human Binding pIC50 = 7.4 7.4 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 473 5 1 5 5.6 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(-c4cccnc4)nc4ccccc43)cc2n1 nan
89554802 152741 None 0 Human Binding pIC50 = 7.4 7.4 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 379 4 1 4 3.4 C[C@H]1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CCO1 nan
CHEMBL3972468 152741 None 0 Human Binding pIC50 = 7.4 7.4 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 379 4 1 4 3.4 C[C@H]1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CCO1 nan
18613373 96227 None 0 Rat Binding pIC50 = 7.4 7.4 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 442 5 2 6 4.8 CC(C)CNc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
CHEMBL260643 96227 None 0 Rat Binding pIC50 = 7.4 7.4 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 442 5 2 6 4.8 CC(C)CNc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
71565807 142918 None 0 Human Binding pIC50 = 7.4 7.4 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 424 4 1 4 4.1 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cnc(Br)c3)cc2n1 nan
CHEMBL3893078 142918 None 0 Human Binding pIC50 = 7.4 7.4 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 424 4 1 4 4.1 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cnc(Br)c3)cc2n1 nan
44450484 96733 None 0 Rat Binding pIC50 = 7.4 7.4 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 370 2 1 4 4.4 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C(F)(F)F)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL263906 96733 None 0 Rat Binding pIC50 = 7.4 7.4 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 370 2 1 4 4.4 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C(F)(F)F)cc2N1 10.1016/j.bmcl.2008.02.076
89554879 153809 None 0 Human Binding pIC50 = 7.4 7.4 - 1
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 371 5 1 3 4.3 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3ccncc3)cc2n1 nan
CHEMBL3981623 153809 None 0 Human Binding pIC50 = 7.4 7.4 - 1
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 371 5 1 3 4.3 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3ccncc3)cc2n1 nan
22448569 89215 None 0 Rat Binding pIC50 = 6.4 6.4 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 478 2 1 5 4.0 N#Cc1cccc(C2=Nc3cc(N4CC[S+]([O-])CC4)c(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
CHEMBL236668 89215 None 0 Rat Binding pIC50 = 6.4 6.4 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 478 2 1 5 4.0 N#Cc1cccc(C2=Nc3cc(N4CC[S+]([O-])CC4)c(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
71565669 143049 None 0 Human Binding pIC50 = 7.4 7.4 - 0
Negative allosteric modulation of mGlu2R (unknown origin)Negative allosteric modulation of mGlu2R (unknown origin)
ChEMBL 407 5 1 5 2.8 COc1ccc(-c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)c(F)c1 10.1021/acs.jmedchem.8b01266
CHEMBL3894283 143049 None 0 Human Binding pIC50 = 7.4 7.4 - 0
Negative allosteric modulation of mGlu2R (unknown origin)Negative allosteric modulation of mGlu2R (unknown origin)
ChEMBL 407 5 1 5 2.8 COc1ccc(-c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)c(F)c1 10.1021/acs.jmedchem.8b01266
CHEMBL4515671 143049 None 0 Human Binding pIC50 = 7.4 7.4 - 0
Negative allosteric modulation of mGlu2R (unknown origin)Negative allosteric modulation of mGlu2R (unknown origin)
ChEMBL 407 5 1 5 2.8 COc1ccc(-c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)c(F)c1 10.1021/acs.jmedchem.8b01266
71565522 143037 None 0 Human Binding pIC50 = 6.3 6.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 495 4 1 6 5.8 CC(C)(C)OC(=O)N(Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1)C(=O)OC(C)(C)C nan
CHEMBL3894156 143037 None 0 Human Binding pIC50 = 6.3 6.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 495 4 1 6 5.8 CC(C)(C)OC(=O)N(Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1)C(=O)OC(C)(C)C nan
89554819 148403 None 0 Human Binding pIC50 = 7.3 7.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 410 4 1 4 4.8 Cc1nc2ccccc2n1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
CHEMBL3936939 148403 None 0 Human Binding pIC50 = 7.3 7.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 410 4 1 4 4.8 Cc1nc2ccccc2n1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
89554826 150573 None 0 Human Binding pIC50 = 7.3 7.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 385 4 1 5 3.0 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCC(F)(F)CC4)ccc23)cn1 nan
CHEMBL3954377 150573 None 0 Human Binding pIC50 = 7.3 7.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 385 4 1 5 3.0 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCC(F)(F)CC4)ccc23)cn1 nan
71566278 152331 None 0 Human Binding pIC50 = 7.3 7.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 396 4 1 4 4.5 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cnc4ccccc43)cc2n1 nan
CHEMBL3968939 152331 None 0 Human Binding pIC50 = 7.3 7.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 396 4 1 4 4.5 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cnc4ccccc43)cc2n1 nan
89554896 160056 None 0 Human Binding pIC50 = 7.3 7.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 379 4 1 6 2.3 C[C@@H]1COC[C@@H](C)N1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1 nan
CHEMBL4107449 160056 None 0 Human Binding pIC50 = 7.3 7.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 379 4 1 6 2.3 C[C@@H]1COC[C@@H](C)N1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1 nan
22448868 155387 None 0 Rat Binding pIC50 = 7.3 7.3 - 0
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 480 5 2 6 4.2 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(OCCO)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2007.12.005
CHEMBL402963 155387 None 0 Rat Binding pIC50 = 7.3 7.3 - 0
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 480 5 2 6 4.2 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(OCCO)c(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2007.12.005
44450455 167667 None 0 Rat Binding pIC50 = 6.3 6.3 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 345 3 1 5 3.9 CC(C)c1ccc2c(c1)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
CHEMBL430053 167667 None 0 Rat Binding pIC50 = 6.3 6.3 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 345 3 1 5 3.9 CC(C)c1ccc2c(c1)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
89554847 145009 None 0 Human Binding pIC50 = 7.3 7.3 - 1
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 357 4 1 3 4.1 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cc3cccnc3)cc2n1 nan
CHEMBL3910265 145009 None 0 Human Binding pIC50 = 7.3 7.3 - 1
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 357 4 1 3 4.1 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cc3cccnc3)cc2n1 nan
89554756 149804 None 0 Human Binding pIC50 = 7.3 7.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 419 4 1 4 3.7 CC1C(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C(=O)C1(C)C nan
CHEMBL3947898 149804 None 0 Human Binding pIC50 = 7.3 7.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 419 4 1 4 3.7 CC1C(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C(=O)C1(C)C nan
71565803 153395 None 0 Human Binding pIC50 = 7.3 7.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 486 6 1 6 4.6 CCOC(=O)c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)nc1C(F)(F)F nan
CHEMBL3978058 153395 None 0 Human Binding pIC50 = 7.3 7.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 486 6 1 6 4.6 CCOC(=O)c1cn(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)nc1C(F)(F)F nan
44309314 206435 None 0 Rat Binding pIC50 = 6.3 6.3 - 0
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 351 4 0 4 5.3 Clc1ccc(/C(=C/n2cncn2)OC2CCCCCC2)c(Cl)c1 10.1016/s0960-894x(99)00346-7
CHEMBL69461 206435 None 0 Rat Binding pIC50 = 6.3 6.3 - 0
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 351 4 0 4 5.3 Clc1ccc(/C(=C/n2cncn2)OC2CCCCCC2)c(Cl)c1 10.1016/s0960-894x(99)00346-7
89554962 153187 None 0 Human Binding pIC50 = 6.3 6.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 401 3 0 4 4.6 CC1(C)CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C#N)nc3c2)C(=O)C1 nan
CHEMBL3976206 153187 None 0 Human Binding pIC50 = 6.3 6.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 401 3 0 4 4.6 CC1(C)CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C#N)nc3c2)C(=O)C1 nan
10130658 66774 None 0 Rat Binding pIC50 = 6.3 6.3 2 2
Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells
ChEMBL 219 2 4 4 -1.4 N[C@@]1(C(=O)O)[C@H](O)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL185822 66774 None 0 Rat Binding pIC50 = 6.3 6.3 2 2
Concentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cellsConcentration required to inhibit metabotropic glutamate receptor 2 activity of rat expressed in CHO cells
ChEMBL 219 2 4 4 -1.4 N[C@@]1(C(=O)O)[C@H](O)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
89554743 151040 None 0 Human Binding pIC50 = 6.3 6.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 374 4 1 4 3.6 N#C[C@@H]1CCCN1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
CHEMBL3958048 151040 None 0 Human Binding pIC50 = 6.3 6.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 374 4 1 4 3.6 N#C[C@@H]1CCCN1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
89554738 151048 None 0 Human Binding pIC50 = 7.3 7.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 431 4 1 3 4.9 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC(C(F)(F)F)C3)cc2n1 nan
CHEMBL3958113 151048 None 0 Human Binding pIC50 = 7.3 7.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 431 4 1 3 4.9 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC(C(F)(F)F)C3)cc2n1 nan
89554921 153886 None 0 Human Binding pIC50 = 7.3 7.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 373 5 1 6 2.7 COc1ccc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)cn1 nan
CHEMBL3982294 153886 None 0 Human Binding pIC50 = 7.3 7.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 373 5 1 6 2.7 COc1ccc(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)cn1 nan
22224756 148040 None 0 Rat Binding pIC50 = 6.3 6.3 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 397 1 1 3 4.7 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccc(F)cc4F)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
CHEMBL393385 148040 None 0 Rat Binding pIC50 = 6.3 6.3 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 397 1 1 3 4.7 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccc(F)cc4F)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
89554738 151048 None 0 Human Binding pIC50 = 7.3 7.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 431 4 1 3 4.9 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC(C(F)(F)F)C3)cc2n1 nan
CHEMBL3958113 151048 None 0 Human Binding pIC50 = 7.3 7.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 431 4 1 3 4.9 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC(C(F)(F)F)C3)cc2n1 nan
89554866 146683 None 0 Human Binding pIC50 = 8.3 8.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 434 6 1 5 4.2 COc1cc(F)c(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)c(F)c1 nan
CHEMBL3923126 146683 None 0 Human Binding pIC50 = 8.3 8.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 434 6 1 5 4.2 COc1cc(F)c(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)c(F)c1 nan
89554768 149539 None 0 Human Binding pIC50 = 8.3 8.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 397 6 1 4 4.8 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4)ccc23)cc1 nan
CHEMBL3946016 149539 None 0 Human Binding pIC50 = 8.3 8.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 397 6 1 4 4.8 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4)ccc23)cc1 nan
89554800 151833 None 0 Human Binding pIC50 = 8.3 8.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 387 5 2 4 3.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(C(O)Cc3cccnc3)cc2n1 nan
CHEMBL3964644 151833 None 0 Human Binding pIC50 = 8.3 8.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 387 5 2 4 3.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(C(O)Cc3cccnc3)cc2n1 nan
71552551 152604 None 0 Human Binding pIC50 = 8.3 8.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 373 4 1 4 3.0 Cc1ccc(-c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)cc1 nan
CHEMBL3971388 152604 None 0 Human Binding pIC50 = 8.3 8.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 373 4 1 4 3.0 Cc1ccc(-c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)cc1 nan
22317744 56303 None 0 Rat Binding pIC50 = 8.3 8.3 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 425 3 1 4 5.5 COc1ccc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cn1 10.1016/j.bmcl.2010.09.125
CHEMBL1629844 56303 None 0 Rat Binding pIC50 = 8.3 8.3 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 425 3 1 4 5.5 COc1ccc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cn1 10.1016/j.bmcl.2010.09.125
18548795 56417 None 0 Rat Binding pIC50 = 8.3 8.3 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 399 2 1 4 5.4 Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)on1 10.1016/j.bmcl.2010.09.125
CHEMBL1631757 56417 None 0 Rat Binding pIC50 = 8.3 8.3 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 399 2 1 4 5.4 Cc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)on1 10.1016/j.bmcl.2010.09.125
69093928 83943 None 0 Human Binding pIC50 = 8.3 8.3 - 0
Displacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation countingDisplacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation counting
ChEMBL 432 5 0 5 5.0 COc1cc(F)cc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm300912k
CHEMBL2206447 83943 None 0 Human Binding pIC50 = 8.3 8.3 - 0
Displacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation countingDisplacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation counting
ChEMBL 432 5 0 5 5.0 COc1cc(F)cc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm300912k
89554892 150689 None 0 Human Binding pIC50 = 8.2 8.2 - 1
Binding affinity to mGluR2 (unknown origin) FLIPR assayBinding affinity to mGluR2 (unknown origin) FLIPR assay
ChEMBL 416 6 1 5 4.0 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)c(F)c1 10.1021/acsmedchemlett.3c00175
CHEMBL3955188 150689 None 0 Human Binding pIC50 = 8.2 8.2 - 1
Binding affinity to mGluR2 (unknown origin) FLIPR assayBinding affinity to mGluR2 (unknown origin) FLIPR assay
ChEMBL 416 6 1 5 4.0 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)c(F)c1 10.1021/acsmedchemlett.3c00175
89554792 150485 None 0 Human Binding pIC50 = 7.3 7.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 414 5 2 4 3.2 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(C(F)F)C3)cc2n1 nan
CHEMBL3953648 150485 None 0 Human Binding pIC50 = 7.3 7.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 414 5 2 4 3.2 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(C(F)F)C3)cc2n1 nan
10428048 3361 None 25 Rat Binding pIC50 = 6.3 6.3 - 1
Inhibition of [3H]-DCG IV binding on rat mGluR2 transfected cell membranes from CHO cellsInhibition of [3H]-DCG IV binding on rat mGluR2 transfected cell membranes from CHO cells
ChEMBL 351 4 0 4 5.3 Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl 10.1016/s0960-894x(99)00346-7
3955 3361 None 25 Rat Binding pIC50 = 6.3 6.3 - 1
Inhibition of [3H]-DCG IV binding on rat mGluR2 transfected cell membranes from CHO cellsInhibition of [3H]-DCG IV binding on rat mGluR2 transfected cell membranes from CHO cells
ChEMBL 351 4 0 4 5.3 Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl 10.1016/s0960-894x(99)00346-7
CHEMBL305406 3361 None 25 Rat Binding pIC50 = 6.3 6.3 - 1
Inhibition of [3H]-DCG IV binding on rat mGluR2 transfected cell membranes from CHO cellsInhibition of [3H]-DCG IV binding on rat mGluR2 transfected cell membranes from CHO cells
ChEMBL 351 4 0 4 5.3 Clc1cccc(c1/C(=C/n1cncn1)/OC1CCCCCC1)Cl 10.1016/s0960-894x(99)00346-7
71566525 148770 None 0 Human Binding pIC50 = 6.3 6.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 314 3 1 4 3.2 NC(=O)c1cc(-c2cnn(-c3ccccc3)c2)c2ccccc2n1 nan
CHEMBL3939839 148770 None 0 Human Binding pIC50 = 6.3 6.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 314 3 1 4 3.2 NC(=O)c1cc(-c2cnn(-c3ccccc3)c2)c2ccccc2n1 nan
89554842 159981 None 0 Human Binding pIC50 = 6.3 6.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 405 4 2 5 2.5 NC(=O)c1cc(-c2cn[nH]c2)c2ccc(CN3CCO[C@@H](C(F)(F)F)C3)cc2n1 nan
CHEMBL4106872 159981 None 0 Human Binding pIC50 = 6.3 6.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 405 4 2 5 2.5 NC(=O)c1cc(-c2cn[nH]c2)c2ccc(CN3CCO[C@@H](C(F)(F)F)C3)cc2n1 nan
89554876 148246 None 0 Human Binding pIC50 = 7.3 7.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 426 6 1 5 4.5 COc1cc(C)c(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)c(C)c1 nan
CHEMBL3935571 148246 None 0 Human Binding pIC50 = 7.3 7.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 426 6 1 5 4.5 COc1cc(C)c(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)c(C)c1 nan
89554795 153532 None 0 Human Binding pIC50 = 7.3 7.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 433 5 1 6 2.9 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCOC(CC(F)(F)F)C4)ccc23)cn1 nan
CHEMBL3979288 153532 None 0 Human Binding pIC50 = 7.3 7.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 433 5 1 6 2.9 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCOC(CC(F)(F)F)C4)ccc23)cn1 nan
89554817 144199 None 0 Human Binding pIC50 = 7.3 7.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 430 5 1 6 3.6 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC(n4cncn4)C3)cc2n1 nan
CHEMBL3903609 144199 None 0 Human Binding pIC50 = 7.3 7.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 430 5 1 6 3.6 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC(n4cncn4)C3)cc2n1 nan
89554934 160262 None 0 Human Binding pIC50 = 7.3 7.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 486 5 1 6 4.5 C[C@@H]1CN(Cc2ccc3c(-c4cnc(C(F)F)s4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1 nan
CHEMBL4109232 160262 None 0 Human Binding pIC50 = 7.3 7.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 486 5 1 6 4.5 C[C@@H]1CN(Cc2ccc3c(-c4cnc(C(F)F)s4)cc(C(N)=O)nc3c2)C[C@H](C(F)(F)F)O1 nan
71565808 151352 None 0 Human Binding pIC50 = 7.3 7.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 360 4 1 4 3.7 Cc1nccn1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
CHEMBL3960284 151352 None 0 Human Binding pIC50 = 7.3 7.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 360 4 1 4 3.7 Cc1nccn1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
89554773 143777 None 0 Human Binding pIC50 = 7.3 7.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 397 4 1 5 3.9 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cnc4ncccc43)cc2n1 nan
CHEMBL3900236 143777 None 0 Human Binding pIC50 = 7.3 7.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 397 4 1 5 3.9 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cnc4ncccc43)cc2n1 nan
89554798 145292 None 0 Human Binding pIC50 = 7.3 7.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 379 5 1 6 2.3 CCC1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)CCO1 nan
CHEMBL3912490 145292 None 0 Human Binding pIC50 = 7.3 7.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 379 5 1 6 2.3 CCC1CN(Cc2ccc3c(-c4cnn(C)c4)cc(C(N)=O)nc3c2)CCO1 nan
117644752 146539 None 0 Human Binding pIC50 = 7.3 7.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 393 4 1 4 3.7 CC1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC(C)O1 nan
CHEMBL3922089 146539 None 0 Human Binding pIC50 = 7.3 7.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 393 4 1 4 3.7 CC1CN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC(C)O1 nan
89544007 147134 None 0 Human Binding pIC50 = 7.3 7.3 - 1
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 358 4 1 4 3.5 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cc3cncnc3)cc2n1 nan
CHEMBL3926904 147134 None 0 Human Binding pIC50 = 7.3 7.3 - 1
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 358 4 1 4 3.5 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cc3cncnc3)cc2n1 nan
71566128 147658 None 0 Human Binding pIC50 = 7.3 7.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 421 5 1 4 4.8 COc1nccc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)c1Cl nan
CHEMBL3930919 147658 None 0 Human Binding pIC50 = 7.3 7.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 421 5 1 4 4.8 COc1nccc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)c1Cl nan
89554803 152338 None 0 Human Binding pIC50 = 7.3 7.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 413 4 1 5 2.4 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCS(=O)(=O)CC3)cc2n1 nan
CHEMBL3968972 152338 None 0 Human Binding pIC50 = 7.3 7.3 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 413 4 1 5 2.4 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCS(=O)(=O)CC3)cc2n1 nan
89554805 148802 None 0 Human Binding pIC50 = 7.2 7.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 379 4 1 4 3.4 C[C@H]1COCCN1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
CHEMBL3940116 148802 None 0 Human Binding pIC50 = 7.2 7.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 379 4 1 4 3.4 C[C@H]1COCCN1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
71566439 144163 None 0 Human Binding pIC50 = 7.2 7.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 300 2 1 2 3.8 NC(=O)c1cc(-c2ccc(Cl)cc2F)c2ccccc2n1 nan
CHEMBL3903327 144163 None 0 Human Binding pIC50 = 7.2 7.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 300 2 1 2 3.8 NC(=O)c1cc(-c2ccc(Cl)cc2F)c2ccccc2n1 nan
71565735 150473 None 0 Human Binding pIC50 = 7.2 7.2 - 0
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 377 4 1 3 3.7 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCCC3=O)cc2n1 10.1016/j.bmcl.2020.127066
CHEMBL3953417 150473 None 0 Human Binding pIC50 = 7.2 7.2 - 0
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 377 4 1 3 3.7 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCCC3=O)cc2n1 10.1016/j.bmcl.2020.127066
44309315 102315 None 0 Rat Binding pIC50 = 6.2 6.2 - 0
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 337 4 0 4 4.9 Clc1cccc(Cl)c1/C(=C/n1cncn1)OC1CCCCC1 10.1016/s0960-894x(99)00346-7
CHEMBL303193 102315 None 0 Rat Binding pIC50 = 6.2 6.2 - 0
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 337 4 0 4 4.9 Clc1cccc(Cl)c1/C(=C/n1cncn1)OC1CCCCC1 10.1016/s0960-894x(99)00346-7
71565523 153415 None 0 Human Binding pIC50 = 6.2 6.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 374 3 0 4 3.3 CN1CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C#N)nc3c2)C1=O nan
CHEMBL3978239 153415 None 0 Human Binding pIC50 = 6.2 6.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 374 3 0 4 3.3 CN1CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C#N)nc3c2)C1=O nan
71566671 150457 None 0 Human Binding pIC50 = 7.2 7.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 406 4 2 4 3.0 CC1(C)NC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O nan
CHEMBL3953282 150457 None 0 Human Binding pIC50 = 7.2 7.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 406 4 2 4 3.0 CC1(C)NC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O nan
71565735 150473 None 0 Human Binding pIC50 = 7.2 7.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 377 4 1 3 3.7 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCCC3=O)cc2n1 nan
CHEMBL3953417 150473 None 0 Human Binding pIC50 = 7.2 7.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 377 4 1 3 3.7 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCCC3=O)cc2n1 nan
89554738 151048 None 0 Human Binding pIC50 = 7.2 7.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 431 4 1 3 4.9 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC(C(F)(F)F)C3)cc2n1 nan
CHEMBL3958113 151048 None 0 Human Binding pIC50 = 7.2 7.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 431 4 1 3 4.9 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC(C(F)(F)F)C3)cc2n1 nan
53324292 56438 None 0 Rat Binding pIC50 = 7.2 7.2 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 460 3 1 4 6.3 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(-n4cccc4)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631873 56438 None 0 Rat Binding pIC50 = 7.2 7.2 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 460 3 1 4 6.3 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(-n4cccc4)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
89554993 149016 None 0 Human Binding pIC50 = 8.2 8.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 427 6 1 6 3.6 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C#N)nc4)ccc23)c(F)c1 nan
CHEMBL3941863 149016 None 0 Human Binding pIC50 = 8.2 8.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 427 6 1 6 3.6 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C#N)nc4)ccc23)c(F)c1 nan
89554892 150689 None 0 Human Binding pIC50 = 8.2 8.2 - 1
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 416 6 1 5 4.0 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)c(F)c1 nan
CHEMBL3955188 150689 None 0 Human Binding pIC50 = 8.2 8.2 - 1
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 416 6 1 5 4.0 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)c(F)c1 nan
89554749 152094 None 0 Human Binding pIC50 = 8.2 8.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 433 6 2 5 4.3 COc1ccc(-c2cc(C(N)=O)nc3cc(C(O)Cc4ccc(Cl)nc4)ccc23)cc1 nan
CHEMBL3966866 152094 None 0 Human Binding pIC50 = 8.2 8.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 433 6 2 5 4.3 COc1ccc(-c2cc(C(N)=O)nc3cc(C(O)Cc4ccc(Cl)nc4)ccc23)cc1 nan
71565966 152889 None 0 Human Binding pIC50 = 8.2 8.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 430 6 1 5 4.6 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cnc(C)nc4)ccc23)c(F)c1 nan
CHEMBL3973721 152889 None 0 Human Binding pIC50 = 8.2 8.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 430 6 1 5 4.6 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cnc(C)nc4)ccc23)c(F)c1 nan
89554893 154070 None 0 Human Binding pIC50 = 8.2 8.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 411 4 1 5 3.7 Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4ccnc(C(F)(F)F)c4)ccc23)cn1 nan
CHEMBL3983863 154070 None 0 Human Binding pIC50 = 8.2 8.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 411 4 1 5 3.7 Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4ccnc(C(F)(F)F)c4)ccc23)cn1 nan
22224854 95437 None 0 Rat Binding pIC50 = 8.2 8.2 - 0
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 421 2 1 5 4.3 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2007.12.005
CHEMBL256812 95437 None 0 Rat Binding pIC50 = 8.2 8.2 - 0
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 421 2 1 5 4.3 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2007.12.005
22317728 56305 None 0 Rat Binding pIC50 = 8.2 8.2 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 435 3 1 3 6.4 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(C4CC4)nc3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1629846 56305 None 0 Rat Binding pIC50 = 8.2 8.2 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 435 3 1 3 6.4 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(C4CC4)nc3)c1)=N2 10.1016/j.bmcl.2010.09.125
53320632 56311 None 0 Rat Binding pIC50 = 8.2 8.2 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 396 2 1 4 4.9 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncn3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1629852 56311 None 0 Rat Binding pIC50 = 8.2 8.2 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 396 2 1 4 4.9 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccncn3)c1)=N2 10.1016/j.bmcl.2010.09.125
11442010 56325 None 0 Rat Binding pIC50 = 8.2 8.2 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 439 4 1 4 5.9 CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1629866 56325 None 0 Rat Binding pIC50 = 8.2 8.2 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 439 4 1 4 5.9 CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
44450453 155988 None 0 Rat Binding pIC50 = 7.2 7.2 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 337 2 1 5 3.4 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(Cl)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL406061 155988 None 0 Rat Binding pIC50 = 7.2 7.2 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 337 2 1 5 3.4 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(Cl)cc2N1 10.1016/j.bmcl.2008.02.076
18613404 89083 None 0 Rat Binding pIC50 = 7.2 7.2 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 404 2 1 4 4.5 CN(C)c1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(C#N)c1)=N2 10.1016/j.bmcl.2007.10.026
CHEMBL236466 89083 None 0 Rat Binding pIC50 = 7.2 7.2 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 404 2 1 4 4.5 CN(C)c1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(C#N)c1)=N2 10.1016/j.bmcl.2007.10.026
22448865 89352 None 0 Rat Binding pIC50 = 6.2 6.2 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 435 4 2 5 3.9 N#Cc1cccc(C2=Nc3cc(OCC(=O)O)c(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
CHEMBL236882 89352 None 0 Rat Binding pIC50 = 6.2 6.2 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 435 4 2 5 3.9 N#Cc1cccc(C2=Nc3cc(OCC(=O)O)c(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
44450444 96186 None 0 Rat Binding pIC50 = 6.2 6.2 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 353 3 1 5 3.7 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(C(F)F)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL260455 96186 None 0 Rat Binding pIC50 = 6.2 6.2 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 353 3 1 5 3.7 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(C(F)F)cc2N1 10.1016/j.bmcl.2008.02.076
89554779 146181 None 0 Human Binding pIC50 = 7.2 7.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 385 4 1 3 4.0 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC(F)(F)C3)cc2n1 nan
CHEMBL3919306 146181 None 0 Human Binding pIC50 = 7.2 7.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 385 4 1 3 4.0 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC(F)(F)C3)cc2n1 nan
89554779 146181 None 0 Human Binding pIC50 = 7.2 7.2 - 0
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 385 4 1 3 4.0 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC(F)(F)C3)cc2n1 10.1016/j.bmcl.2020.127066
CHEMBL3919306 146181 None 0 Human Binding pIC50 = 7.2 7.2 - 0
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 385 4 1 3 4.0 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC(F)(F)C3)cc2n1 10.1016/j.bmcl.2020.127066
71565737 144059 None 0 Human Binding pIC50 = 7.2 7.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 416 6 2 5 3.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cc(C(O)C4CC4)cn3)cc2n1 nan
CHEMBL3902679 144059 None 0 Human Binding pIC50 = 7.2 7.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 416 6 2 5 3.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cc(C(O)C4CC4)cn3)cc2n1 nan
89554831 147592 None 0 Human Binding pIC50 = 7.2 7.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 446 4 1 4 3.8 CN1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC1C(F)(F)F nan
CHEMBL3930529 147592 None 0 Human Binding pIC50 = 7.2 7.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 446 4 1 4 3.8 CN1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC1C(F)(F)F nan
71566670 146996 None 0 Human Binding pIC50 = 7.2 7.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 420 4 1 4 3.3 CN1C(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C(=O)C1(C)C nan
CHEMBL3925652 146996 None 0 Human Binding pIC50 = 7.2 7.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 420 4 1 4 3.3 CN1C(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C(=O)C1(C)C nan
89554761 150655 None 0 Human Binding pIC50 = 7.2 7.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 346 4 1 4 3.4 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3ccnc3)cc2n1 nan
CHEMBL3954993 150655 None 0 Human Binding pIC50 = 7.2 7.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 346 4 1 4 3.4 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3ccnc3)cc2n1 nan
22224809 154076 None 0 Rat Binding pIC50 = 7.2 7.2 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 375 1 1 3 4.7 Cc1ccc(C#Cc2ccc3c(c2)NC(=O)CC(c2cccc(C#N)c2)=N3)cc1 10.1016/j.bmcl.2007.10.026
CHEMBL398392 154076 None 0 Rat Binding pIC50 = 7.2 7.2 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 375 1 1 3 4.7 Cc1ccc(C#Cc2ccc3c(c2)NC(=O)CC(c2cccc(C#N)c2)=N3)cc1 10.1016/j.bmcl.2007.10.026
9847181 95104 None 0 Rat Binding pIC50 = 7.2 7.2 - 0
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 462 5 2 6 4.1 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(OCCO)c(C#Cc3ccccc3)cc2N1 10.1016/j.bmcl.2007.12.005
CHEMBL255151 95104 None 0 Rat Binding pIC50 = 7.2 7.2 - 0
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 462 5 2 6 4.1 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2cc(OCCO)c(C#Cc3ccccc3)cc2N1 10.1016/j.bmcl.2007.12.005
10089411 7529 None 0 Human Binding pIC50 = 5.2 5.2 - 1
Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2
ChEMBL 353 5 3 4 2.7 NC(C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1CC1c2ccccc2Oc2ccccc21 10.1016/s0960-894x(01)00656-4
CHEMBL108735 7529 None 0 Human Binding pIC50 = 5.2 5.2 - 1
Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2
ChEMBL 353 5 3 4 2.7 NC(C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1CC1c2ccccc2Oc2ccccc21 10.1016/s0960-894x(01)00656-4
353213 149146 None 12 Rat Binding pIC50 = 5.2 5.2 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 250 1 1 2 3.5 Cc1ccc2c(c1)NC(=O)CC(c1ccccc1)=N2 10.1016/j.bmcl.2007.12.005
353213 149146 None 12 Rat Binding pIC50 = 5.2 5.2 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 250 1 1 2 3.5 Cc1ccc2c(c1)NC(=O)CC(c1ccccc1)=N2 10.1016/j.bmcl.2008.02.076
CHEMBL394287 149146 None 12 Rat Binding pIC50 = 5.2 5.2 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 250 1 1 2 3.5 Cc1ccc2c(c1)NC(=O)CC(c1ccccc1)=N2 10.1016/j.bmcl.2007.12.005
CHEMBL394287 149146 None 12 Rat Binding pIC50 = 5.2 5.2 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 250 1 1 2 3.5 Cc1ccc2c(c1)NC(=O)CC(c1ccccc1)=N2 10.1016/j.bmcl.2008.02.076
353213 149146 None 12 Rat Binding pIC50 = 5.2 5.2 - 0
Displacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cells
ChEMBL 250 1 1 2 3.5 Cc1ccc2c(c1)NC(=O)CC(c1ccccc1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL394287 149146 None 12 Rat Binding pIC50 = 5.2 5.2 - 0
Displacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from recombinant rat mGluR2 expressed in CHO cells
ChEMBL 250 1 1 2 3.5 Cc1ccc2c(c1)NC(=O)CC(c1ccccc1)=N2 10.1016/j.bmcl.2010.09.125
71566437 147564 None 0 Human Binding pIC50 = 6.2 6.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 268 2 1 3 3.4 Cc1cscc1-c1cc(C(N)=O)nc2ccccc12 nan
CHEMBL3930346 147564 None 0 Human Binding pIC50 = 6.2 6.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 268 2 1 3 3.4 Cc1cscc1-c1cc(C(N)=O)nc2ccccc12 nan
44434255 88638 None 0 Rat Binding pIC50 = 5.2 5.2 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 280 2 1 3 3.5 COc1cccc(C2=Nc3ccc(C)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
CHEMBL235598 88638 None 0 Rat Binding pIC50 = 5.2 5.2 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 280 2 1 3 3.5 COc1cccc(C2=Nc3ccc(C)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
89554731 152200 None 0 Human Binding pIC50 = 7.2 7.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 438 5 1 4 5.7 CC(C)c1nc2ccccc2n1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
CHEMBL3967755 152200 None 0 Human Binding pIC50 = 7.2 7.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 438 5 1 4 5.7 CC(C)c1nc2ccccc2n1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
89554972 154274 None 0 Human Binding pIC50 = 7.2 7.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 460 5 1 4 4.2 CCN1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC1C(F)(F)F nan
CHEMBL3985765 154274 None 0 Human Binding pIC50 = 7.2 7.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 460 5 1 4 4.2 CCN1CCN(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)CC1C(F)(F)F nan
22317369 56427 None 0 Rat Binding pIC50 = 7.2 7.2 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 463 2 1 3 6.6 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C(F)(F)F)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631862 56427 None 0 Rat Binding pIC50 = 7.2 7.2 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 463 2 1 3 6.6 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccnc(C(F)(F)F)c3)c1)=N2 10.1016/j.bmcl.2010.09.125
71566346 149575 None 0 Human Binding pIC50 = 6.2 6.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 314 4 1 3 3.6 NC(=O)c1cc(-c2ccc(OC(F)F)cc2)c2ccccc2n1 nan
CHEMBL3946344 149575 None 0 Human Binding pIC50 = 6.2 6.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 314 4 1 3 3.6 NC(=O)c1cc(-c2ccc(OC(F)F)cc2)c2ccccc2n1 nan
71566348 151028 None 0 Human Binding pIC50 = 6.2 6.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 328 3 1 4 3.5 Cc1c(-c2cc(C(N)=O)nc3ccccc23)cnn1-c1ccccc1 nan
CHEMBL3957842 151028 None 0 Human Binding pIC50 = 6.2 6.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 328 3 1 4 3.5 Cc1c(-c2cc(C(N)=O)nc3ccccc23)cnn1-c1ccccc1 nan
89554750 142615 None 0 Human Binding pIC50 = 7.2 7.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 498 7 2 6 4.7 CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)c(C)c4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F nan
CHEMBL3890746 142615 None 0 Human Binding pIC50 = 7.2 7.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 498 7 2 6 4.7 CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)c(C)c4)cc(C(N)=O)nc3c2)cn1)C(F)(F)F nan
71566347 148785 None 0 Human Binding pIC50 = 6.2 6.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 252 2 1 4 1.7 Cn1cc(-c2cc(C(N)=O)nc3ccccc23)cn1 nan
CHEMBL3939979 148785 None 0 Human Binding pIC50 = 6.2 6.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 252 2 1 4 1.7 Cn1cc(-c2cc(C(N)=O)nc3ccccc23)cn1 nan
25195461 2144 None 42 Human Binding pIC50 = 7.2 7.2 - 1
Displacement of [3H]19 from human mGlu2 receptor expressed in CHO cellsDisplacement of [3H]19 from human mGlu2 receptor expressed in CHO cells
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/jm500496m
8946 2144 None 42 Human Binding pIC50 = 7.2 7.2 - 1
Displacement of [3H]19 from human mGlu2 receptor expressed in CHO cellsDisplacement of [3H]19 from human mGlu2 receptor expressed in CHO cells
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/jm500496m
CHEMBL3337527 2144 None 42 Human Binding pIC50 = 7.2 7.2 - 1
Displacement of [3H]19 from human mGlu2 receptor expressed in CHO cellsDisplacement of [3H]19 from human mGlu2 receptor expressed in CHO cells
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/jm500496m
DB12059 2144 None 42 Human Binding pIC50 = 7.2 7.2 - 1
Displacement of [3H]19 from human mGlu2 receptor expressed in CHO cellsDisplacement of [3H]19 from human mGlu2 receptor expressed in CHO cells
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/jm500496m
22224822 89950 None 0 Rat Binding pIC50 = 7.2 7.2 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 391 2 1 4 4.4 COc1ccc(C#Cc2ccc3c(c2)NC(=O)CC(c2cccc(C#N)c2)=N3)cc1 10.1016/j.bmcl.2007.10.026
CHEMBL237944 89950 None 0 Rat Binding pIC50 = 7.2 7.2 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 391 2 1 4 4.4 COc1ccc(C#Cc2ccc3c(c2)NC(=O)CC(c2cccc(C#N)c2)=N3)cc1 10.1016/j.bmcl.2007.10.026
89545189 152984 None 0 Human Binding pIC50 = 7.2 7.2 - 0
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 365 4 1 4 3.0 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCOCC3)cc2n1 10.1016/j.bmcl.2020.127066
CHEMBL3974648 152984 None 0 Human Binding pIC50 = 7.2 7.2 - 0
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 365 4 1 4 3.0 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCOCC3)cc2n1 10.1016/j.bmcl.2020.127066
156011740 177529 None 0 Human Binding pIC50 = 7.2 7.2 - 0
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 455 6 2 6 3.8 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccccc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
CHEMBL4638570 177529 None 0 Human Binding pIC50 = 7.2 7.2 - 0
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 455 6 2 6 3.8 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccccc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F 10.1016/j.bmcl.2020.127066
89554955 145269 None 0 Human Binding pIC50 = 6.2 6.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 326 2 1 2 3.8 NC(=O)c1cc(-c2ccccc2Br)c2ccccc2n1 nan
CHEMBL3912345 145269 None 0 Human Binding pIC50 = 6.2 6.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 326 2 1 2 3.8 NC(=O)c1cc(-c2ccccc2Br)c2ccccc2n1 nan
89554762 152602 None 0 Human Binding pIC50 = 7.2 7.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 397 4 1 5 3.9 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cnc4cccnc43)cc2n1 nan
CHEMBL3971379 152602 None 0 Human Binding pIC50 = 7.2 7.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 397 4 1 5 3.9 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cnc4cccnc43)cc2n1 nan
1393 1539 None 42 Human Binding pIC50 = 8.2 8.2 -2 6
Agonist activity at mGlu2 (unknown origin)Agonist activity at mGlu2 (unknown origin)
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/acs.jmedchem.6b01119
1396 1539 None 42 Human Binding pIC50 = 8.2 8.2 -2 6
Agonist activity at mGlu2 (unknown origin)Agonist activity at mGlu2 (unknown origin)
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/acs.jmedchem.6b01119
213056 1539 None 42 Human Binding pIC50 = 8.2 8.2 -2 6
Agonist activity at mGlu2 (unknown origin)Agonist activity at mGlu2 (unknown origin)
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL8759 1539 None 42 Human Binding pIC50 = 8.2 8.2 -2 6
Agonist activity at mGlu2 (unknown origin)Agonist activity at mGlu2 (unknown origin)
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/acs.jmedchem.6b01119
89554982 146940 None 0 Human Binding pIC50 = 8.2 8.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 399 6 2 6 3.2 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cncnc4N)ccc23)cc1 nan
CHEMBL3925177 146940 None 0 Human Binding pIC50 = 8.2 8.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 399 6 2 6 3.2 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cncnc4N)ccc23)cc1 nan
89554981 148546 None 0 Human Binding pIC50 = 8.2 8.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 409 6 1 6 3.5 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C#N)nc4)ccc23)cc1 nan
CHEMBL3937970 148546 None 0 Human Binding pIC50 = 8.2 8.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 409 6 1 6 3.5 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C#N)nc4)ccc23)cc1 nan
89554880 150132 None 0 Human Binding pIC50 = 8.2 8.2 - 1
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 372 5 1 4 3.7 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3cncnc3)cc2n1 nan
CHEMBL3950572 150132 None 0 Human Binding pIC50 = 8.2 8.2 - 1
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 372 5 1 4 3.7 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3cncnc3)cc2n1 nan
71565593 151050 None 0 Human Binding pIC50 = 8.2 8.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 377 4 1 4 3.2 CC1CC=C(c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)CC1 nan
CHEMBL3958138 151050 None 0 Human Binding pIC50 = 8.2 8.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 377 4 1 4 3.2 CC1CC=C(c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)CC1 nan
89554910 151483 None 0 Human Binding pIC50 = 8.2 8.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 445 4 1 5 4.4 Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cc(Cl)nc(C(F)(F)F)c4)ccc23)cn1 nan
CHEMBL3961599 151483 None 0 Human Binding pIC50 = 8.2 8.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 445 4 1 5 4.4 Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cc(Cl)nc(C(F)(F)F)c4)ccc23)cn1 nan
71565966 152889 None 0 Human Binding pIC50 = 8.2 8.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 430 6 1 5 4.6 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cnc(C)nc4)ccc23)c(F)c1 nan
CHEMBL3973721 152889 None 0 Human Binding pIC50 = 8.2 8.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 430 6 1 5 4.6 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cnc(C)nc4)ccc23)c(F)c1 nan
18548862 158031 None 0 Rat Binding pIC50 = 8.2 8.2 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 415 4 1 6 4.1 CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
CHEMBL408455 158031 None 0 Rat Binding pIC50 = 8.2 8.2 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 415 4 1 6 4.1 CCOc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
44450391 168938 None 0 Rat Binding pIC50 = 8.2 8.2 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 414 3 1 4 5.3 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3cc(F)ccc3F)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL437835 168938 None 0 Rat Binding pIC50 = 8.2 8.2 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 414 3 1 4 5.3 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(-c3cc(F)ccc3F)cc2N1 10.1016/j.bmcl.2008.02.076
22317892 56319 None 0 Rat Binding pIC50 = 8.2 8.2 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 477 2 1 3 6.9 Cc1cc(-c2cccc(C3=Nc4cc(C(F)(F)F)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C)n1 10.1016/j.bmcl.2010.09.125
CHEMBL1629860 56319 None 0 Rat Binding pIC50 = 8.2 8.2 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 477 2 1 3 6.9 Cc1cc(-c2cccc(C3=Nc4cc(C(F)(F)F)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C)n1 10.1016/j.bmcl.2010.09.125
69093344 83942 None 0 Human Binding pIC50 = 8.1 8.1 - 0
Displacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation countingDisplacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation counting
ChEMBL 432 5 0 5 5.0 COc1ccc(F)c(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm300912k
CHEMBL2206446 83942 None 0 Human Binding pIC50 = 8.1 8.1 - 0
Displacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation countingDisplacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation counting
ChEMBL 432 5 0 5 5.0 COc1ccc(F)c(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm300912k
44450434 167797 None 0 Rat Binding pIC50 = 7.2 7.2 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 401 4 1 6 3.7 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(OCC(F)(F)F)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL430231 167797 None 0 Rat Binding pIC50 = 7.2 7.2 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 401 4 1 6 3.7 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(OCC(F)(F)F)cc2N1 10.1016/j.bmcl.2008.02.076
44431050 142431 None 0 Human Binding pIC50 = 7.2 7.2 - 0
Antagonist activity at human mGlur2Antagonist activity at human mGlur2
ChEMBL 363 2 3 2 3.6 O=C1NCCc2c1[nH]c1ccc(NC(=O)C34CC5CC(CC(C5)C3)C4)cc21 10.1021/acs.jmedchem.0c01887
CHEMBL388669 142431 None 0 Human Binding pIC50 = 7.2 7.2 - 0
Antagonist activity at human mGlur2Antagonist activity at human mGlur2
ChEMBL 363 2 3 2 3.6 O=C1NCCc2c1[nH]c1ccc(NC(=O)C34CC5CC(CC(C5)C3)C4)cc21 10.1021/acs.jmedchem.0c01887
71566601 150312 None 0 Human Binding pIC50 = 7.2 7.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 467 5 1 4 4.4 CC1(c2ccccc2)CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O nan
CHEMBL3952222 150312 None 0 Human Binding pIC50 = 7.2 7.2 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 467 5 1 4 4.4 CC1(c2ccccc2)CC(=O)N(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)C1=O nan
44450483 168909 None 0 Rat Binding pIC50 = 7.1 7.1 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 380 2 1 4 4.1 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(Br)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL437646 168909 None 0 Rat Binding pIC50 = 7.1 7.1 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 380 2 1 4 4.1 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(Br)cc2N1 10.1016/j.bmcl.2008.02.076
9845127 167881 None 0 Rat Binding pIC50 = 7.1 7.1 - 0
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 422 2 1 6 3.7 O=C1CC(c2cccc(-n3cnnn3)c2)=Nc2ccc(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2007.12.005
CHEMBL430408 167881 None 0 Rat Binding pIC50 = 7.1 7.1 - 0
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 422 2 1 6 3.7 O=C1CC(c2cccc(-n3cnnn3)c2)=Nc2ccc(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2007.12.005
71565886 144135 None 0 Human Binding pIC50 = 7.1 7.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 407 6 1 6 3.0 CC(C)CC1COCCN1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1 nan
CHEMBL3903111 144135 None 0 Human Binding pIC50 = 7.1 7.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 407 6 1 6 3.0 CC(C)CC1COCCN1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1 nan
89554822 144730 None 0 Human Binding pIC50 = 7.1 7.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 436 5 1 4 5.4 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(C4CC4)nc4ccccc43)cc2n1 nan
CHEMBL3908110 144730 None 0 Human Binding pIC50 = 7.1 7.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 436 5 1 4 5.4 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(C4CC4)nc4ccccc43)cc2n1 nan
44453878 95730 None 0 Rat Binding pIC50 = 6.1 6.1 - 0
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 416 2 1 4 5.0 Cn1ccnc1-c1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.12.005
CHEMBL258113 95730 None 0 Rat Binding pIC50 = 6.1 6.1 - 0
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 416 2 1 4 5.0 Cn1ccnc1-c1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.12.005
89554929 150425 None 0 Human Binding pIC50 = 7.1 7.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 395 4 1 4 2.9 NC(=O)c1cc(-c2ccc(F)cc2)c2c(F)cc(CN3C(=O)CCC3=O)cc2n1 nan
CHEMBL3953060 150425 None 0 Human Binding pIC50 = 7.1 7.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 395 4 1 4 2.9 NC(=O)c1cc(-c2ccc(F)cc2)c2c(F)cc(CN3C(=O)CCC3=O)cc2n1 nan
89554907 160696 None 0 Human Binding pIC50 = 7.1 7.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 474 6 2 7 3.3 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)nc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F nan
CHEMBL4112899 160696 None 0 Human Binding pIC50 = 7.1 7.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 474 6 2 7 3.3 CC[C@@](O)(c1cn(Cc2ccc3c(-c4ccc(F)nc4)cc(C(N)=O)nc3c2)nn1)C(F)(F)F nan
44309080 206499 None 0 Rat Binding pIC50 = 4.1 4.1 - 0
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 265 4 0 4 2.9 CC(C)O/C(=C\n1cncn1)c1ccc(F)cc1F 10.1016/s0960-894x(99)00346-7
CHEMBL69869 206499 None 0 Rat Binding pIC50 = 4.1 4.1 - 0
Inhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cellsInhibition of 10 uM 1S, 3R-ACPD stimulated GTP gamma 35S binding to rat mGluR2 expressed in CHO cells
ChEMBL 265 4 0 4 2.9 CC(C)O/C(=C\n1cncn1)c1ccc(F)cc1F 10.1016/s0960-894x(99)00346-7
89554959 143426 None 0 Human Binding pIC50 = 7.1 7.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 362 4 1 6 2.3 Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cnc(F)nc4)ccc23)cn1 nan
CHEMBL3897362 143426 None 0 Human Binding pIC50 = 7.1 7.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 362 4 1 6 2.3 Cn1cc(-c2cc(C(N)=O)nc3cc(Cc4cnc(F)nc4)ccc23)cn1 nan
71566205 152385 None 0 Human Binding pIC50 = 7.1 7.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 386 5 1 3 4.7 COc1ccc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cc1 nan
CHEMBL3969476 152385 None 0 Human Binding pIC50 = 7.1 7.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 386 5 1 3 4.7 COc1ccc(Cc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cc1 nan
89554739 160000 None 0 Human Binding pIC50 = 7.1 7.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 450 4 1 6 3.9 Cc1cnc(-c2cc(C(N)=O)nc3cc(CN4C[C@@H](C)O[C@@H](C(F)(F)F)C4)ccc23)s1 nan
CHEMBL4107013 160000 None 0 Human Binding pIC50 = 7.1 7.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 450 4 1 6 3.9 Cc1cnc(-c2cc(C(N)=O)nc3cc(CN4C[C@@H](C)O[C@@H](C(F)(F)F)C4)ccc23)s1 nan
22224639 161864 None 0 Rat Binding pIC50 = 7.1 7.1 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 395 1 1 3 5.1 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4Cl)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
CHEMBL413979 161864 None 0 Rat Binding pIC50 = 7.1 7.1 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 395 1 1 3 5.1 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccc4Cl)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
1439 2469 None 12 Rat Binding pIC50 = 4.1 4.1 - 2
Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.
ChEMBL 173 3 3 3 -0.5 OC(=O)[C@H]1C[C@@H]1[C@@](C(=O)O)(N)C 10.1021/jm980571q
5311457 2469 None 12 Rat Binding pIC50 = 4.1 4.1 - 2
Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.
ChEMBL 173 3 3 3 -0.5 OC(=O)[C@H]1C[C@@H]1[C@@](C(=O)O)(N)C 10.1021/jm980571q
CHEMBL41013 2469 None 12 Rat Binding pIC50 = 4.1 4.1 - 2
Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.
ChEMBL 173 3 3 3 -0.5 OC(=O)[C@H]1C[C@@H]1[C@@](C(=O)O)(N)C 10.1021/jm980571q
89554782 150122 None 0 Human Binding pIC50 = 7.1 7.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 392 5 2 4 2.6 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC[C@H]3C(N)=O)cc2n1 nan
CHEMBL3950507 150122 None 0 Human Binding pIC50 = 7.1 7.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 392 5 2 4 2.6 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC[C@H]3C(N)=O)cc2n1 nan
122539788 162640 None 16 Human Binding pIC50 = 7.1 7.1 - 0
Negative allosteric modulation of mGlu2R (unknown origin)Negative allosteric modulation of mGlu2R (unknown origin)
ChEMBL 326 5 1 5 2.3 Cn1ccc(COc2cnc(C(N)=O)cc2-c2ccc(F)cc2)n1 10.1021/acs.jmedchem.8b01266
CHEMBL4168094 162640 None 16 Human Binding pIC50 = 7.1 7.1 - 0
Negative allosteric modulation of mGlu2R (unknown origin)Negative allosteric modulation of mGlu2R (unknown origin)
ChEMBL 326 5 1 5 2.3 Cn1ccc(COc2cnc(C(N)=O)cc2-c2ccc(F)cc2)n1 10.1021/acs.jmedchem.8b01266
71565669 143049 None 0 Human Binding pIC50 = 8.1 8.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 407 5 1 5 2.8 COc1ccc(-c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)c(F)c1 nan
CHEMBL3894283 143049 None 0 Human Binding pIC50 = 8.1 8.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 407 5 1 5 2.8 COc1ccc(-c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)c(F)c1 nan
CHEMBL4515671 143049 None 0 Human Binding pIC50 = 8.1 8.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 407 5 1 5 2.8 COc1ccc(-c2cc(C(N)=O)nc3cc(CN4C(=O)CCC4=O)ccc23)c(F)c1 nan
71565964 144338 None 0 Human Binding pIC50 = 8.1 8.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 429 7 1 4 5.2 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4ccc(CF)nc4)ccc23)cc1 nan
CHEMBL3904730 144338 None 0 Human Binding pIC50 = 8.1 8.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 429 7 1 4 5.2 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4ccc(CF)nc4)ccc23)cc1 nan
89554964 145311 None 0 Human Binding pIC50 = 8.1 8.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 433 4 1 6 2.9 C[C@H]1CO[C@@H](C(F)(F)F)CN1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1 nan
CHEMBL3912615 145311 None 0 Human Binding pIC50 = 8.1 8.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 433 4 1 6 2.9 C[C@H]1CO[C@@H](C(F)(F)F)CN1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1 nan
89554887 148419 None 0 Human Binding pIC50 = 8.1 8.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 387 5 2 4 3.6 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cc3ccnc(CO)c3)cc2n1 nan
CHEMBL3937038 148419 None 0 Human Binding pIC50 = 8.1 8.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 387 5 2 4 3.6 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cc3ccnc(CO)c3)cc2n1 nan
71566127 148725 None 0 Human Binding pIC50 = 8.1 8.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 415 6 1 4 4.9 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4)ccc23)c(F)c1 nan
CHEMBL3939455 148725 None 0 Human Binding pIC50 = 8.1 8.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 415 6 1 4 4.9 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cccnc4)ccc23)c(F)c1 nan
89554858 151188 None 0 Human Binding pIC50 = 8.1 8.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 520 7 2 6 4.7 CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)cc4F)cc(C(N)=O)nc3c2F)cn1)C(F)(F)F nan
CHEMBL3959134 151188 None 0 Human Binding pIC50 = 8.1 8.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 520 7 2 6 4.7 CCC(O)(c1cn(Cc2ccc3c(-c4ccc(OC)cc4F)cc(C(N)=O)nc3c2F)cn1)C(F)(F)F nan
89554984 152610 None 0 Human Binding pIC50 = 8.1 8.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 423 6 1 6 4.0 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cnc(C#N)nc4)ccc23)cc1 nan
CHEMBL3971450 152610 None 0 Human Binding pIC50 = 8.1 8.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 423 6 1 6 4.0 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4cnc(C#N)nc4)ccc23)cc1 nan
89554790 159961 None 0 Human Binding pIC50 = 8.1 8.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 447 4 1 6 3.3 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4C[C@H](C(F)(F)F)OCC4(C)C)ccc23)cn1 nan
CHEMBL4106729 159961 None 0 Human Binding pIC50 = 8.1 8.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 447 4 1 6 3.3 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4C[C@H](C(F)(F)F)OCC4(C)C)ccc23)cn1 nan
89554915 160195 None 0 Human Binding pIC50 = 8.1 8.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 447 4 1 6 3.2 Cc1nn(C)cc1-c1cc(C(N)=O)nc2cc(CN3C[C@@H](C)O[C@@H](C(F)(F)F)C3)ccc12 nan
CHEMBL4108673 160195 None 0 Human Binding pIC50 = 8.1 8.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 447 4 1 6 3.2 Cc1nn(C)cc1-c1cc(C(N)=O)nc2cc(CN3C[C@@H](C)O[C@@H](C(F)(F)F)C3)ccc12 nan
89554961 160378 None 0 Human Binding pIC50 = 8.1 8.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 433 4 1 6 2.9 C[C@@H]1CO[C@@H](C(F)(F)F)CN1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1 nan
CHEMBL4110317 160378 None 0 Human Binding pIC50 = 8.1 8.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 433 4 1 6 2.9 C[C@@H]1CO[C@@H](C(F)(F)F)CN1Cc1ccc2c(-c3cnn(C)c3)cc(C(N)=O)nc2c1 nan
53317987 56317 None 0 Rat Binding pIC50 = 8.1 8.1 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 453 4 1 4 6.0 COCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C)n1 10.1016/j.bmcl.2010.09.125
CHEMBL1629859 56317 None 0 Rat Binding pIC50 = 8.1 8.1 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 453 4 1 4 6.0 COCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cc(C)n1 10.1016/j.bmcl.2010.09.125
11484819 56322 None 0 Rat Binding pIC50 = 8.1 8.1 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 347 2 1 3 4.9 O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(Cl)cc2N1 10.1016/j.bmcl.2010.09.125
CHEMBL1629863 56322 None 0 Rat Binding pIC50 = 8.1 8.1 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 347 2 1 3 4.9 O=C1CC(c2cccc(-c3ccncc3)c2)=Nc2ccc(Cl)cc2N1 10.1016/j.bmcl.2010.09.125
18548737 56419 None 0 Rat Binding pIC50 = 8.1 8.1 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 385 2 1 5 4.1 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3cncn3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1631854 56419 None 0 Rat Binding pIC50 = 8.1 8.1 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 385 2 1 5 4.1 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3cncn3)c1)=N2 10.1016/j.bmcl.2010.09.125
11362246 56425 None 0 Rat Binding pIC50 = 8.1 8.1 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 423 3 1 3 6.1 CCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
CHEMBL1631860 56425 None 0 Rat Binding pIC50 = 8.1 8.1 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 423 3 1 3 6.1 CCc1cc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)ccn1 10.1016/j.bmcl.2010.09.125
70052526 90086 None 1 Human Binding pIC50 = 8.1 8.1 - 1
Agonist activity at mGlu2 (unknown origin)Agonist activity at mGlu2 (unknown origin)
ChEMBL 201 2 4 4 -1.5 N[C@@]1(C(=O)O)C[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL2381642 90086 None 1 Human Binding pIC50 = 8.1 8.1 - 1
Agonist activity at mGlu2 (unknown origin)Agonist activity at mGlu2 (unknown origin)
ChEMBL 201 2 4 4 -1.5 N[C@@]1(C(=O)O)C[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
71566598 142777 None 16 Rat Binding pIC50 = 8.1 8.1 - 1
Negative allosteric modulation of rat mGluR2 by FLIPR assayNegative allosteric modulation of rat mGluR2 by FLIPR assay
ChEMBL 377 4 1 4 2.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1 10.1016/j.bmcl.2020.127066
CHEMBL3892073 142777 None 16 Rat Binding pIC50 = 8.1 8.1 - 1
Negative allosteric modulation of rat mGluR2 by FLIPR assayNegative allosteric modulation of rat mGluR2 by FLIPR assay
ChEMBL 377 4 1 4 2.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1 10.1016/j.bmcl.2020.127066
89554908 142553 None 0 Human Binding pIC50 = 7.1 7.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 396 5 2 4 2.9 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(CF)C3)cc2n1 nan
CHEMBL3890277 142553 None 0 Human Binding pIC50 = 7.1 7.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 396 5 2 4 2.9 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(CF)C3)cc2n1 nan
9864190 88689 None 0 Rat Binding pIC50 = 7.1 7.1 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 370 1 1 2 5.2 O=C1CC(c2cccc(Cl)c2)=Nc2ccc(C#Cc3ccccc3)cc2N1 10.1016/j.bmcl.2007.10.026
CHEMBL235807 88689 None 0 Rat Binding pIC50 = 7.1 7.1 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 370 1 1 2 5.2 O=C1CC(c2cccc(Cl)c2)=Nc2ccc(C#Cc3ccccc3)cc2N1 10.1016/j.bmcl.2007.10.026
89554895 150322 None 0 Human Binding pIC50 = 7.1 7.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 450 5 1 4 5.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(C4CCC4)nc4ccccc43)cc2n1 nan
CHEMBL3952287 150322 None 0 Human Binding pIC50 = 7.1 7.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 450 5 1 4 5.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(C4CCC4)nc4ccccc43)cc2n1 nan
89554978 150793 None 0 Human Binding pIC50 = 7.1 7.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 447 5 1 6 3.5 CC(C)n1cc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)cn1 nan
CHEMBL3956019 150793 None 0 Human Binding pIC50 = 7.1 7.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 447 5 1 6 3.5 CC(C)n1cc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)cn1 nan
89555003 145313 None 0 Human Binding pIC50 = 7.1 7.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 339 5 1 4 3.1 CON(C)Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
CHEMBL3912634 145313 None 0 Human Binding pIC50 = 7.1 7.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 339 5 1 4 3.1 CON(C)Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
89554744 148426 None 0 Human Binding pIC50 = 7.1 7.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 378 4 2 4 2.1 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(=O)C3)cc2n1 nan
CHEMBL3937068 148426 None 0 Human Binding pIC50 = 7.1 7.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 378 4 2 4 2.1 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(=O)C3)cc2n1 nan
22448756 154691 None 0 Rat Binding pIC50 = 7.1 7.1 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 474 3 1 5 5.0 COC1CCN(c2cc3c(cc2C#Cc2ccccc2)NC(=O)CC(c2cccc(C#N)c2)=N3)CC1 10.1016/j.bmcl.2007.10.026
CHEMBL399185 154691 None 0 Rat Binding pIC50 = 7.1 7.1 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 474 3 1 5 5.0 COC1CCN(c2cc3c(cc2C#Cc2ccccc2)NC(=O)CC(c2cccc(C#N)c2)=N3)CC1 10.1016/j.bmcl.2007.10.026
89554949 148269 None 0 Human Binding pIC50 = 6.1 6.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 238 2 1 2 2.9 NC(=O)c1cc(C2=CCCC2)c2ccccc2n1 nan
CHEMBL3935751 148269 None 0 Human Binding pIC50 = 6.1 6.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 238 2 1 2 2.9 NC(=O)c1cc(C2=CCCC2)c2ccccc2n1 nan
89554741 147295 None 0 Human Binding pIC50 = 7.1 7.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 366 6 2 4 2.1 CN(CC(N)=O)Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
CHEMBL3928211 147295 None 0 Human Binding pIC50 = 7.1 7.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 366 6 2 4 2.1 CN(CC(N)=O)Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
89554957 150465 None 0 Human Binding pIC50 = 7.1 7.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 391 5 2 6 2.5 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cc(C(=O)O)nn3)cc2n1 nan
CHEMBL3953345 150465 None 0 Human Binding pIC50 = 7.1 7.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 391 5 2 6 2.5 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3cc(C(=O)O)nn3)cc2n1 nan
117642124 147429 None 0 Human Binding pIC50 = 7.1 7.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 469 6 2 6 4.1 CC[C@](O)(c1cn(Cc2ccc3c(-c4ccccc4C)cc(C(N)=O)nc3c2)nn1)C(F)(F)F nan
CHEMBL3929304 147429 None 0 Human Binding pIC50 = 7.1 7.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 469 6 2 6 4.1 CC[C@](O)(c1cn(Cc2ccc3c(-c4ccccc4C)cc(C(N)=O)nc3c2)nn1)C(F)(F)F nan
89554862 144071 None 0 Human Binding pIC50 = 7.1 7.1 - 1
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 371 5 1 3 4.3 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3ccccn3)cc2n1 nan
CHEMBL3902752 144071 None 0 Human Binding pIC50 = 7.1 7.1 - 1
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 371 5 1 3 4.3 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3ccccn3)cc2n1 nan
89554838 161029 None 0 Human Binding pIC50 = 7.1 7.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 461 4 1 6 3.5 Cc1nn(C)c(C)c1-c1cc(C(N)=O)nc2cc(CN3C[C@@H](C)O[C@@H](C(F)(F)F)C3)ccc12 nan
CHEMBL4115433 161029 None 0 Human Binding pIC50 = 7.1 7.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 461 4 1 6 3.5 Cc1nn(C)c(C)c1-c1cc(C(N)=O)nc2cc(CN3C[C@@H](C)O[C@@H](C(F)(F)F)C3)ccc12 nan
22318000 56308 None 0 Rat Binding pIC50 = 7.1 7.1 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 438 3 1 4 5.6 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(N(C)C)nc3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL1629849 56308 None 0 Rat Binding pIC50 = 7.1 7.1 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 438 3 1 4 5.6 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-c3ccc(N(C)C)nc3)c1)=N2 10.1016/j.bmcl.2010.09.125
22224608 88792 None 0 Rat Binding pIC50 = 6.1 6.1 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 362 1 1 4 3.8 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccn4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
CHEMBL236257 88792 None 0 Rat Binding pIC50 = 6.1 6.1 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 362 1 1 4 3.8 N#Cc1cccc(C2=Nc3ccc(C#Cc4ccccn4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
89554735 146716 None 0 Human Binding pIC50 = 7.1 7.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 379 4 1 6 2.3 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C)(C)C4)ccc23)cn1 nan
CHEMBL3923360 146716 None 0 Human Binding pIC50 = 7.1 7.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 379 4 1 6 2.3 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C)(C)C4)ccc23)cn1 nan
1408 265 None 24 Rat Binding pIC50 = 4.1 4.1 - 0
Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.
ChEMBL 217 3 4 4 -1.0 OC(=O)[C@@H]1C[C@](C[C@@H]1C(=O)O)(N)C(=O)O 10.1021/jm980571q
6604820 265 None 24 Rat Binding pIC50 = 4.1 4.1 - 0
Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.
ChEMBL 217 3 4 4 -1.0 OC(=O)[C@@H]1C[C@](C[C@@H]1C(=O)O)(N)C(=O)O 10.1021/jm980571q
CHEMBL285043 265 None 24 Rat Binding pIC50 = 4.1 4.1 - 0
Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.
ChEMBL 217 3 4 4 -1.0 OC(=O)[C@@H]1C[C@](C[C@@H]1C(=O)O)(N)C(=O)O 10.1021/jm980571q
CHEMBL288635 265 None 24 Rat Binding pIC50 = 4.1 4.1 - 0
Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.
ChEMBL 217 3 4 4 -1.0 OC(=O)[C@@H]1C[C@](C[C@@H]1C(=O)O)(N)C(=O)O 10.1021/jm980571q
89554810 151404 None 0 Human Binding pIC50 = 7.1 7.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 464 5 1 4 6.2 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(C4CCCC4)nc4ccccc43)cc2n1 nan
CHEMBL3960845 151404 None 0 Human Binding pIC50 = 7.1 7.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 464 5 1 4 6.2 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cn3c(C4CCCC4)nc4ccccc43)cc2n1 nan
71566598 142777 None 16 Human Binding pIC50 = 8.1 8.1 - 1
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 377 4 1 4 2.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1 nan
CHEMBL3892073 142777 None 16 Human Binding pIC50 = 8.1 8.1 - 1
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 377 4 1 4 2.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1 nan
89554770 144178 None 0 Human Binding pIC50 = 8.1 8.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 446 4 2 4 3.9 C[C@H]1CNC(C(F)(F)F)CN1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
CHEMBL3903459 144178 None 0 Human Binding pIC50 = 8.1 8.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 446 4 2 4 3.9 C[C@H]1CNC(C(F)(F)F)CN1Cc1ccc2c(-c3ccc(F)cc3)cc(C(N)=O)nc2c1 nan
71565965 148372 None 0 Human Binding pIC50 = 8.1 8.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 447 7 1 4 5.4 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4ccc(CF)nc4)ccc23)c(F)c1 nan
CHEMBL3936681 148372 None 0 Human Binding pIC50 = 8.1 8.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 447 7 1 4 5.4 COc1ccc(-c2cc(C(N)=O)nc3cc(C(C)Cc4ccc(CF)nc4)ccc23)c(F)c1 nan
89554985 150527 None 0 Human Binding pIC50 = 8.1 8.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 416 6 2 5 3.9 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cccnc4N)ccc23)c(F)c1 nan
CHEMBL3954035 150527 None 0 Human Binding pIC50 = 8.1 8.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 416 6 2 5 3.9 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cccnc4N)ccc23)c(F)c1 nan
89554980 154066 None 0 Human Binding pIC50 = 8.1 8.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 398 6 2 5 3.8 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cccnc4N)ccc23)cc1 nan
CHEMBL3983820 154066 None 0 Human Binding pIC50 = 8.1 8.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 398 6 2 5 3.8 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cccnc4N)ccc23)cc1 nan
89554809 154287 None 0 Human Binding pIC50 = 8.1 8.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 436 4 1 6 3.5 Cc1ncc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)s1 nan
CHEMBL3985872 154287 None 0 Human Binding pIC50 = 8.1 8.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 436 4 1 6 3.5 Cc1ncc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)s1 nan
89554789 160296 None 0 Human Binding pIC50 = 8.1 8.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 437 5 1 6 2.9 NC(=O)c1cc(-c2cnn(CF)c2)c2ccc(CN3CCO[C@@H](C(F)(F)F)C3)cc2n1 nan
CHEMBL4109555 160296 None 0 Human Binding pIC50 = 8.1 8.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 437 5 1 6 2.9 NC(=O)c1cc(-c2cnn(CF)c2)c2ccc(CN3CCO[C@@H](C(F)(F)F)C3)cc2n1 nan
10201802 96700 None 0 Rat Binding pIC50 = 8.1 8.1 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 413 3 1 5 4.4 CN(C)c1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2008.02.076
CHEMBL263649 96700 None 0 Rat Binding pIC50 = 8.1 8.1 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 413 3 1 5 4.4 CN(C)c1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnc3)c1)=N2 10.1016/j.bmcl.2008.02.076
18548824 157828 None 0 Rat Binding pIC50 = 8.1 8.1 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 385 2 1 5 4.1 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
CHEMBL408229 157828 None 0 Rat Binding pIC50 = 8.1 8.1 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 385 2 1 5 4.1 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2008.02.076
9888376 95268 None 1 Rat Binding pIC50 = 8.1 8.1 - 0
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 420 2 1 4 4.9 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2007.12.005
CHEMBL256011 95268 None 1 Rat Binding pIC50 = 8.1 8.1 - 0
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 420 2 1 4 4.9 O=C1CC(c2cccc(-n3ccnc3)c2)=Nc2ccc(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2007.12.005
71566598 142777 None 16 Human Binding pIC50 = 8.1 8.1 - 1
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 377 4 1 4 2.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1 10.1016/j.bmcl.2020.127066
CHEMBL3892073 142777 None 16 Human Binding pIC50 = 8.1 8.1 - 1
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 377 4 1 4 2.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1 10.1016/j.bmcl.2020.127066
53316736 56300 None 0 Rat Binding pIC50 = 8.1 8.1 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 423 3 1 3 6.1 CCc1ccc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cn1 10.1016/j.bmcl.2010.09.125
CHEMBL1629715 56300 None 0 Rat Binding pIC50 = 8.1 8.1 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 423 3 1 3 6.1 CCc1ccc(-c2cccc(C3=Nc4cc(C)c(C(F)(F)F)cc4NC(=O)C3)c2)cn1 10.1016/j.bmcl.2010.09.125
18548824 157828 None 0 Rat Binding pIC50 = 8.1 8.1 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 385 2 1 5 4.1 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2010.09.125
CHEMBL408229 157828 None 0 Rat Binding pIC50 = 8.1 8.1 - 0
Partial displacement of [3H]LY354740 from recombinant rat mGluR2Partial displacement of [3H]LY354740 from recombinant rat mGluR2
ChEMBL 385 2 1 5 4.1 Cc1cc2c(cc1C(F)(F)F)NC(=O)CC(c1cccc(-n3ccnn3)c1)=N2 10.1016/j.bmcl.2010.09.125
71461395 83941 None 1 Human Binding pIC50 = 8.0 8.0 - 0
Displacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation countingDisplacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation counting
ChEMBL 432 5 0 5 5.0 COc1c(F)ccc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm300912k
CHEMBL2206445 83941 None 1 Human Binding pIC50 = 8.0 8.0 - 0
Displacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation countingDisplacement of [3H]JNJ-40068782 from human mGLuR2 expressed in CHO cell membrane after 60 mins by liquid scintillation counting
ChEMBL 432 5 0 5 5.0 COc1c(F)ccc(F)c1C1CCN(c2ccn3c(CC4CC4)nnc3c2Cl)CC1 10.1021/jm300912k
89554912 146062 None 0 Human Binding pIC50 = 7.1 7.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 404 5 2 4 3.3 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(C4CC4)C3)cc2n1 nan
CHEMBL3918313 146062 None 0 Human Binding pIC50 = 7.1 7.1 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 404 5 2 4 3.3 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCNC(C4CC4)C3)cc2n1 nan
89554815 145234 None 0 Human Binding pIC50 = 7.0 7.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 450 5 1 6 3.8 CCc1ncc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)s1 nan
CHEMBL3912111 145234 None 0 Human Binding pIC50 = 7.0 7.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 450 5 1 6 3.8 CCc1ncc(-c2cc(C(N)=O)nc3cc(CN4CCOC(C(F)(F)F)C4)ccc23)s1 nan
71565670 177325 None 0 Human Binding pIC50 = 7.0 7.0 - 0
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 363 4 1 3 3.3 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC3=O)cc2n1 10.1016/j.bmcl.2020.127066
CHEMBL4635528 177325 None 0 Human Binding pIC50 = 7.0 7.0 - 0
Negative allosteric modulation of human mGluR2 by FLIPR assayNegative allosteric modulation of human mGluR2 by FLIPR assay
ChEMBL 363 4 1 3 3.3 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCCC3=O)cc2n1 10.1016/j.bmcl.2020.127066
44450445 96329 None 0 Rat Binding pIC50 = 7.0 7.0 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 371 2 1 5 3.7 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(C(F)(F)F)cc2N1 10.1016/j.bmcl.2008.02.076
CHEMBL261128 96329 None 0 Rat Binding pIC50 = 7.0 7.0 - 0
Displacement of [3H]LY354740 from rat mGluR2Displacement of [3H]LY354740 from rat mGluR2
ChEMBL 371 2 1 5 3.7 O=C1CC(c2cccc(-n3ccnn3)c2)=Nc2ccc(C(F)(F)F)cc2N1 10.1016/j.bmcl.2008.02.076
9886745 89217 None 0 Rat Binding pIC50 = 7.0 7.0 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 391 2 1 4 4.4 COc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(C#N)c1)=N2 10.1016/j.bmcl.2007.10.026
CHEMBL236670 89217 None 0 Rat Binding pIC50 = 7.0 7.0 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 391 2 1 4 4.4 COc1cc2c(cc1C#Cc1ccccc1)NC(=O)CC(c1cccc(C#N)c1)=N2 10.1016/j.bmcl.2007.10.026
117641966 146632 None 0 Human Binding pIC50 = 7.0 7.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 419 4 1 4 4.1 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC4(CCOC4)CC3)cc2n1 nan
CHEMBL3922743 146632 None 0 Human Binding pIC50 = 7.0 7.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 419 4 1 4 4.1 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3CCC4(CCOC4)CC3)cc2n1 nan
89554924 142795 None 0 Human Binding pIC50 = 6.0 6.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 365 4 2 6 1.7 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCC[C@H](O)C4)ccc23)cn1 nan
CHEMBL3892213 142795 None 0 Human Binding pIC50 = 6.0 6.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 365 4 2 6 1.7 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCC[C@H](O)C4)ccc23)cn1 nan
117642073 149063 None 0 Human Binding pIC50 = 7.0 7.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 428 7 1 6 3.9 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)cc1OC nan
CHEMBL3942209 149063 None 0 Human Binding pIC50 = 7.0 7.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 428 7 1 6 3.9 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)cc1OC nan
22224730 154834 None 0 Rat Binding pIC50 = 6.0 6.0 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 366 2 1 3 4.6 COc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
CHEMBL400018 154834 None 0 Rat Binding pIC50 = 6.0 6.0 - 0
Displacement of [3H]LY354740 from rat mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat mGluR2 expressed in CHO cells
ChEMBL 366 2 1 3 4.6 COc1cccc(C2=Nc3ccc(C#Cc4ccccc4)cc3NC(=O)C2)c1 10.1016/j.bmcl.2007.10.026
89554920 145651 None 0 Human Binding pIC50 = 7.0 7.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 439 5 1 7 1.7 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCS(=O)(=O)C(C5CC5)C4)ccc23)cn1 nan
CHEMBL3915181 145651 None 0 Human Binding pIC50 = 7.0 7.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 439 5 1 7 1.7 Cn1cc(-c2cc(C(N)=O)nc3cc(CN4CCS(=O)(=O)C(C5CC5)C4)ccc23)cn1 nan
9931956 95140 None 0 Rat Binding pIC50 = 7.0 7.0 - 0
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 421 2 1 5 4.3 O=C1CC(c2cccc(-n3cncn3)c2)=Nc2ccc(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2007.12.005
CHEMBL255356 95140 None 0 Rat Binding pIC50 = 7.0 7.0 - 0
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 421 2 1 5 4.3 O=C1CC(c2cccc(-n3cncn3)c2)=Nc2ccc(C#Cc3ccc(F)cc3)cc2N1 10.1016/j.bmcl.2007.12.005
22224761 166710 None 0 Rat Binding pIC50 = 7.0 7.0 - 0
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 434 2 1 4 5.2 Cc1cn(-c2cccc(C3=Nc4ccc(C#Cc5ccc(F)cc5)cc4NC(=O)C3)c2)cn1 10.1016/j.bmcl.2007.12.005
CHEMBL428066 166710 None 0 Rat Binding pIC50 = 7.0 7.0 - 0
Displacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cellsDisplacement of [3H]LY354740 from rat recombinant mGluR2 expressed in CHO cells
ChEMBL 434 2 1 4 5.2 Cc1cn(-c2cccc(C3=Nc4ccc(C#Cc5ccc(F)cc5)cc4NC(=O)C3)c2)cn1 10.1016/j.bmcl.2007.12.005
71566203 148723 None 0 Human Binding pIC50 = 6.0 6.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 379 3 1 4 2.6 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(C(=O)N3CCOCC3)cc2n1 nan
CHEMBL3939409 148723 None 0 Human Binding pIC50 = 6.0 6.0 - 0
Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.Biological Assay: The utility of the compounds in accordance with the present invention as antagonists of metabotropic glutamate receptor activity, in particular mGluR2 activity, may be demonstrated by methodology known in the art. Antagonist constants are determined as follows. The compounds of the present invention were tested in a fluorescence laser imaging plate reader based assay. This assay is a common functional assay to monitor Ca2+ mobilization in whole cells expressing recombinant receptor coupled with a promiscuous G-protein. CHO dhfr- cells stably expressing recombinant human mGluR2 and Gα16 loaded with Fluo-4 AM (Invitrogen, Carlsbad Calif.) are treated with various concentrations of antagonists of compounds and the Ca2+ response is monitored on a FLIPR384 (Molecular Devices, Sunnydale Calif.) for agonist activity.
ChEMBL 379 3 1 4 2.6 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(C(=O)N3CCOCC3)cc2n1 nan
3335 3015 None 1 Rat Binding pIC50 = 5 5.0 - 1
Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.
ChEMBL 235 4 3 3 0.5 OC(=O)[C@H]([C@H]1[C@H]([C@@H]1C(=O)O)c1ccccc1)N 10.1021/jm980571q
5311344 3015 None 1 Rat Binding pIC50 = 5 5.0 - 1
Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.
ChEMBL 235 4 3 3 0.5 OC(=O)[C@H]([C@H]1[C@H]([C@@H]1C(=O)O)c1ccccc1)N 10.1021/jm980571q
CHEMBL39573 3015 None 1 Rat Binding pIC50 = 5 5.0 - 1
Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.Inhibitory activity against Metabotropic glutamate receptor 2 in the rat HEK 293 cells.
ChEMBL 235 4 3 3 0.5 OC(=O)[C@H]([C@H]1[C@H]([C@@H]1C(=O)O)c1ccccc1)N 10.1021/jm980571q
68109335 157203 None 0 Human Binding pKd = 9 9.0 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 438 5 0 5 6.5 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2Cl)c(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4074664 157203 None 0 Human Binding pKd = 9 9.0 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 438 5 0 5 6.5 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2Cl)c(C)n1 10.1021/acs.jmedchem.7b00669
66785087 158232 None 0 Human Binding pKd = 9.0 9.0 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 390 5 1 4 5.1 Fc1cc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)ccc1NC1CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4087196 158232 None 0 Human Binding pKd = 9.0 9.0 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 390 5 1 4 5.1 Fc1cc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)ccc1NC1CC1 10.1021/acs.jmedchem.7b00669
49801370 157127 None 0 Human Binding pKd = 8.9 8.9 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 406 5 1 4 5.6 FC(F)(F)c1c(-c2ccc(NC3CC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
CHEMBL4073628 157127 None 0 Human Binding pKd = 8.9 8.9 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 406 5 1 4 5.6 FC(F)(F)c1c(-c2ccc(NC3CC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
68109941 156213 None 0 Human Binding pKd = 8.8 8.8 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 504 6 2 5 6.5 O[C@]1(C2CC2)CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4063313 156213 None 0 Human Binding pKd = 8.8 8.8 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 504 6 2 5 6.5 O[C@]1(C2CC2)CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
66786131 157258 None 0 Human Binding pKd = 8 8.0 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 402 5 0 5 5.6 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4075417 157258 None 0 Human Binding pKd = 8 8.0 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 402 5 0 5 5.6 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
66786493 157352 None 0 Human Binding pKd = 8.0 8.0 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 464 5 2 5 5.7 O[C@H]1CC[C@@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4076639 157352 None 0 Human Binding pKd = 8.0 8.0 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 464 5 2 5 5.7 O[C@H]1CC[C@@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
137652500 157281 None 0 Human Binding pKd = 8.0 8.0 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 430 6 0 5 6.4 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(C)C)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4075697 157281 None 0 Human Binding pKd = 8.0 8.0 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 430 6 0 5 6.4 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(C)C)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
68109677 157285 None 0 Human Binding pKd = 8.0 8.0 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 458 4 2 5 5.5 O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4075762 157285 None 0 Human Binding pKd = 8.0 8.0 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 458 4 2 5 5.5 O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
44595851 3802 None 6 Human Binding pKd = 7 7.0 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 475 8 2 6 4.5 Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C 10.1021/acs.jmedchem.7b00669
6259 3802 None 6 Human Binding pKd = 7 7.0 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 475 8 2 6 4.5 Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C 10.1021/acs.jmedchem.7b00669
CHEMBL4092105 3802 None 6 Human Binding pKd = 7 7.0 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 475 8 2 6 4.5 Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C 10.1021/acs.jmedchem.7b00669
68109605 158482 None 0 Human Binding pKd = 7.9 7.9 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 456 5 0 5 6.3 Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cc(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4089955 158482 None 0 Human Binding pKd = 7.9 7.9 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 456 5 0 5 6.3 Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cc(C)n1 10.1021/acs.jmedchem.7b00669
66786069 156552 None 0 Human Binding pKd = 7.9 7.9 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 451 5 0 5 5.6 FC(F)(F)c1c(-c2ccc(OC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
CHEMBL4067290 156552 None 0 Human Binding pKd = 7.9 7.9 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 451 5 0 5 5.6 FC(F)(F)c1c(-c2ccc(OC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
66784529 157185 None 0 Human Binding pKd = 7.9 7.9 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 430 5 2 5 5.4 O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4074421 157185 None 0 Human Binding pKd = 7.9 7.9 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 430 5 2 5 5.4 O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
66785027 158430 None 0 Human Binding pKd = 7.9 7.9 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 356 5 1 4 4.7 Fc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4089416 158430 None 0 Human Binding pKd = 7.9 7.9 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 356 5 1 4 4.7 Fc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CC1 10.1021/acs.jmedchem.7b00669
66785551 157245 None 0 Human Binding pKd = 7.8 7.8 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 422 5 0 5 5.9 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4075258 157245 None 0 Human Binding pKd = 7.8 7.8 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 422 5 0 5 5.9 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
66785393 156986 None 0 Human Binding pKd = 7.8 7.8 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 419 7 1 6 5.0 COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2)cn1 10.1021/acs.jmedchem.7b00669
CHEMBL4072134 156986 None 0 Human Binding pKd = 7.8 7.8 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 419 7 1 6 5.0 COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2)cn1 10.1021/acs.jmedchem.7b00669
66784675 157266 None 0 Human Binding pKd = 7.8 7.8 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 472 7 0 6 5.5 COc1ccc(COc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cn1 10.1021/acs.jmedchem.7b00669
CHEMBL4075537 157266 None 0 Human Binding pKd = 7.8 7.8 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 472 7 0 6 5.5 COc1ccc(COc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cn1 10.1021/acs.jmedchem.7b00669
68109333 157721 None 0 Human Binding pKd = 7.8 7.8 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 459 4 1 5 5.5 O[C@H]1CC[C@H](Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4081244 157721 None 0 Human Binding pKd = 7.8 7.8 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 459 4 1 5 5.5 O[C@H]1CC[C@H](Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
66784246 156455 None 0 Human Binding pKd = 7.8 7.8 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 418 5 0 5 6.1 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C)cc2Cl)c(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4066051 156455 None 0 Human Binding pKd = 7.8 7.8 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 418 5 0 5 6.1 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C)cc2Cl)c(C)n1 10.1021/acs.jmedchem.7b00669
68109272 158710 None 0 Human Binding pKd = 7.7 7.7 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 416 5 1 5 5.2 Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CCOCC1 10.1021/acs.jmedchem.7b00669
CHEMBL4092275 158710 None 0 Human Binding pKd = 7.7 7.7 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 416 5 1 5 5.2 Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CCOCC1 10.1021/acs.jmedchem.7b00669
3954 664 None 44 Human Binding pKd = 6.7 6.7 46 2
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 454 6 1 3 6.8 Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1 10.1021/acs.jmedchem.7b00669
9868580 664 None 44 Human Binding pKd = 6.7 6.7 46 2
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 454 6 1 3 6.8 Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1 10.1021/acs.jmedchem.7b00669
CHEMBL593013 664 None 44 Human Binding pKd = 6.7 6.7 46 2
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 454 6 1 3 6.8 Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1 10.1021/acs.jmedchem.7b00669
66785780 158836 None 0 Human Binding pKd = 8.7 8.7 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 453 7 1 6 5.4 COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2)cn1 10.1021/acs.jmedchem.7b00669
CHEMBL4093657 158836 None 0 Human Binding pKd = 8.7 8.7 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 453 7 1 6 5.4 COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2)cn1 10.1021/acs.jmedchem.7b00669
66787433 156554 None 0 Human Binding pKd = 8.7 8.7 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 460 6 0 6 5.9 CCOCc1nnc2c(C(F)(F)F)c(-c3ccc(Oc4ccc(C)nc4C)c(F)c3)ccn12 10.1021/acs.jmedchem.7b00669
CHEMBL4067298 156554 None 0 Human Binding pKd = 8.7 8.7 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 460 6 0 6 5.9 CCOCc1nnc2c(C(F)(F)F)c(-c3ccc(Oc4ccc(C)nc4C)c(F)c3)ccn12 10.1021/acs.jmedchem.7b00669
66784262 158323 None 0 Human Binding pKd = 8.7 8.7 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 392 5 1 4 5.3 CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1F 10.1021/acs.jmedchem.7b00669
CHEMBL4088239 158323 None 0 Human Binding pKd = 8.7 8.7 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 392 5 1 4 5.3 CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1F 10.1021/acs.jmedchem.7b00669
70209638 157701 None 0 Human Binding pKd = 8.6 8.6 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 456 5 0 5 6.3 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4080973 157701 None 0 Human Binding pKd = 8.6 8.6 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 456 5 0 5 6.3 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
68109580 158617 None 0 Human Binding pKd = 8.5 8.5 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 471 7 1 6 5.5 COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cn1 10.1021/acs.jmedchem.7b00669
CHEMBL4091370 158617 None 0 Human Binding pKd = 8.5 8.5 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 471 7 1 6 5.5 COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cn1 10.1021/acs.jmedchem.7b00669
66784890 156141 None 0 Human Binding pKd = 7.7 7.7 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 358 5 1 4 5.0 CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2Cl)cc1F 10.1021/acs.jmedchem.7b00669
CHEMBL4062535 156141 None 0 Human Binding pKd = 7.7 7.7 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 358 5 1 4 5.0 CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2Cl)cc1F 10.1021/acs.jmedchem.7b00669
66785101 158137 None 0 Human Binding pKd = 7.6 7.6 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 422 6 0 5 5.9 CCc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)ccn1 10.1021/acs.jmedchem.7b00669
CHEMBL4085882 158137 None 0 Human Binding pKd = 7.6 7.6 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 422 6 0 5 5.9 CCc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)ccn1 10.1021/acs.jmedchem.7b00669
66786816 158448 None 0 Human Binding pKd = 7.6 7.6 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 426 6 0 6 5.5 CCOCc1nnc2c(Cl)c(-c3ccc(Oc4ccc(C)nc4C)c(F)c3)ccn12 10.1021/acs.jmedchem.7b00669
CHEMBL4089612 158448 None 0 Human Binding pKd = 7.6 7.6 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 426 6 0 6 5.5 CCOCc1nnc2c(Cl)c(-c3ccc(Oc4ccc(C)nc4C)c(F)c3)ccn12 10.1021/acs.jmedchem.7b00669
68109425 158382 None 0 Human Binding pKd = 7.6 7.6 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 417 5 0 5 5.2 Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1OC1CCOCC1 10.1021/acs.jmedchem.7b00669
CHEMBL4088960 158382 None 0 Human Binding pKd = 7.6 7.6 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 417 5 0 5 5.2 Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1OC1CCOCC1 10.1021/acs.jmedchem.7b00669
68108857 157430 None 0 Human Binding pKd = 8.5 8.5 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 465 5 1 5 5.7 O[C@H]1CC[C@H](Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4077609 157430 None 0 Human Binding pKd = 8.5 8.5 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 465 5 1 5 5.7 O[C@H]1CC[C@H](Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
66786493 159773 None 0 Human Binding pKd = 8.5 8.5 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 464 5 2 5 5.7 O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4104081 159773 None 0 Human Binding pKd = 8.5 8.5 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 464 5 2 5 5.7 O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
49801369 158841 None 0 Human Binding pKd = 8.5 8.5 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 450 4 0 5 6.1 Cc1ccc(Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4093792 158841 None 0 Human Binding pKd = 8.5 8.5 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 450 4 0 5 6.1 Cc1ccc(Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
66785300 156563 None 0 Human Binding pKd = 8.5 8.5 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 408 5 1 4 5.8 CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1Cl 10.1021/acs.jmedchem.7b00669
CHEMBL4067421 156563 None 0 Human Binding pKd = 8.5 8.5 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 408 5 1 4 5.8 CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1Cl 10.1021/acs.jmedchem.7b00669
66787355 156316 None 0 Human Binding pKd = 8.4 8.4 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 450 5 1 5 5.6 FC(F)(F)c1c(-c2ccc(NC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
CHEMBL4064589 156316 None 0 Human Binding pKd = 8.4 8.4 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 450 5 1 5 5.6 FC(F)(F)c1c(-c2ccc(NC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
49801371 158833 None 0 Human Binding pKd = 7.4 7.4 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 408 5 0 5 5.6 Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)ccn1 10.1021/acs.jmedchem.7b00669
CHEMBL4093620 158833 None 0 Human Binding pKd = 7.4 7.4 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 408 5 0 5 5.6 Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)ccn1 10.1021/acs.jmedchem.7b00669
66785182 157270 None 0 Human Binding pKd = 7.4 7.4 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 434 6 0 5 6.2 Fc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1Oc1ccnc(C2CC2)c1 10.1021/acs.jmedchem.7b00669
CHEMBL4075593 157270 None 0 Human Binding pKd = 7.4 7.4 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 434 6 0 5 6.2 Fc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1Oc1ccnc(C2CC2)c1 10.1021/acs.jmedchem.7b00669
59234231 2143 None 4 Human Binding pKd = 7.3 7.3 -2 2
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.7b00669
6330 2143 None 4 Human Binding pKd = 7.3 7.3 -2 2
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.7b00669
6331 2143 None 4 Human Binding pKd = 7.3 7.3 -2 2
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.7b00669
CHEMBL3337510 2143 None 4 Human Binding pKd = 7.3 7.3 -2 2
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.7b00669
68109379 157317 None 0 Human Binding pKd = 7.3 7.3 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 464 6 1 5 5.3 FC(F)(F)c1c(-c2ccc(CNC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
CHEMBL4076286 157317 None 0 Human Binding pKd = 7.3 7.3 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 464 6 1 5 5.3 FC(F)(F)c1c(-c2ccc(CNC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
66785010 155953 None 0 Human Binding pKd = 8.2 8.2 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 372 5 1 4 5.2 Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4060306 155953 None 0 Human Binding pKd = 8.2 8.2 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 372 5 1 4 5.2 Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CC1 10.1021/acs.jmedchem.7b00669
25125217 555 None 27 Human Binding pKd = 6.2 6.2 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 487 6 1 7 3.5 Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1 10.1021/acs.jmedchem.7b00669
7678 555 None 27 Human Binding pKd = 6.2 6.2 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 487 6 1 7 3.5 Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1 10.1021/acs.jmedchem.7b00669
CHEMBL3937907 555 None 27 Human Binding pKd = 6.2 6.2 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 487 6 1 7 3.5 Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1 10.1021/acs.jmedchem.7b00669
DB16073 555 None 27 Human Binding pKd = 6.2 6.2 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 487 6 1 7 3.5 Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1 10.1021/acs.jmedchem.7b00669
66786902 159555 None 0 Human Binding pKd = 8.1 8.1 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 472 5 0 5 6.8 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)c(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4101354 159555 None 0 Human Binding pKd = 8.1 8.1 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 472 5 0 5 6.8 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)c(C)n1 10.1021/acs.jmedchem.7b00669
68109333 159486 None 0 Human Binding pKd = 8.1 8.1 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 459 4 1 5 5.5 O[C@H]1CC[C@@H](Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4100691 159486 None 0 Human Binding pKd = 8.1 8.1 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 459 4 1 5 5.5 O[C@H]1CC[C@@H](Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
66784572 157000 None 0 Human Binding pKd = 8.1 8.1 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 468 6 0 5 6.6 Fc1cc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)ccc1Oc1ccnc(C2CC2)c1 10.1021/acs.jmedchem.7b00669
CHEMBL4072262 157000 None 0 Human Binding pKd = 8.1 8.1 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 468 6 0 5 6.6 Fc1cc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)ccc1Oc1ccnc(C2CC2)c1 10.1021/acs.jmedchem.7b00669
137652320 157366 None 0 Human Binding pKd = 8.1 8.1 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 454 7 0 6 5.4 COc1ccc(COc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2)cn1 10.1021/acs.jmedchem.7b00669
CHEMBL4076786 157366 None 0 Human Binding pKd = 8.1 8.1 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 454 7 0 6 5.4 COc1ccc(COc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2)cn1 10.1021/acs.jmedchem.7b00669
49801368 159752 None 0 Human Binding pKd = 8.0 8.0 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 442 5 0 5 6.0 Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)ccn1 10.1021/acs.jmedchem.7b00669
CHEMBL4103808 159752 None 0 Human Binding pKd = 8.0 8.0 - 1
Binding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assayBinding affinity to human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes by scintillation proximity assay
ChEMBL 442 5 0 5 6.0 Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)ccn1 10.1021/acs.jmedchem.7b00669
89554892 150689 None 0 Human Binding pKi = 9.7 9.7 - 1
Binding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assayBinding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assay
ChEMBL 416 6 1 5 4.0 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)c(F)c1 10.1021/acsmedchemlett.3c00175
CHEMBL3955188 150689 None 0 Human Binding pKi = 9.7 9.7 - 1
Binding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assayBinding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assay
ChEMBL 416 6 1 5 4.0 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)c(F)c1 10.1021/acsmedchemlett.3c00175
172446995 195553 None 0 Human Binding pKi = 9.5 9.5 - 1
Binding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assayBinding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assay
ChEMBL 397 5 1 5 3.6 N#Cc1ncc(CCc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 10.1021/acsmedchemlett.3c00175
CHEMBL5405921 195553 None 0 Human Binding pKi = 9.5 9.5 - 1
Binding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assayBinding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assay
ChEMBL 397 5 1 5 3.6 N#Cc1ncc(CCc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 10.1021/acsmedchemlett.3c00175
89554872 149486 None 0 Human Binding pKi = 9.3 9.3 - 1
Binding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assayBinding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assay
ChEMBL 416 6 1 5 4.0 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)cc1F 10.1021/acsmedchemlett.3c00175
CHEMBL3945590 149486 None 0 Human Binding pKi = 9.3 9.3 - 1
Binding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assayBinding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assay
ChEMBL 416 6 1 5 4.0 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)cc1F 10.1021/acsmedchemlett.3c00175
172447324 195740 None 0 Human Binding pKi = 9.2 9.2 - 1
Binding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assayBinding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assay
ChEMBL 403 6 1 3 4.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3ccc(CF)nc3)cc2n1 10.1021/acsmedchemlett.3c00175
CHEMBL5409898 195740 None 0 Human Binding pKi = 9.2 9.2 - 1
Binding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assayBinding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assay
ChEMBL 403 6 1 3 4.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3ccc(CF)nc3)cc2n1 10.1021/acsmedchemlett.3c00175
172456888 196211 None 0 Human Binding pKi = 9.1 9.1 - 1
Binding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assayBinding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assay
ChEMBL 400 5 1 4 4.3 Cc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)c(F)c1 10.1021/acsmedchemlett.3c00175
CHEMBL5418895 196211 None 0 Human Binding pKi = 9.1 9.1 - 1
Binding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assayBinding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assay
ChEMBL 400 5 1 4 4.3 Cc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)c(F)c1 10.1021/acsmedchemlett.3c00175
172466838 196651 None 0 Human Binding pKi = 9.1 9.1 - 1
Binding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assayBinding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assay
ChEMBL 390 5 1 4 3.9 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3cnc(F)nc3)cc2n1 10.1021/acsmedchemlett.3c00175
CHEMBL5429000 196651 None 0 Human Binding pKi = 9.1 9.1 - 1
Binding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assayBinding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assay
ChEMBL 390 5 1 4 3.9 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3cnc(F)nc3)cc2n1 10.1021/acsmedchemlett.3c00175
172443728 194987 None 0 Human Binding pKi = 9.1 9.1 - 1
Binding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assayBinding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assay
ChEMBL 386 5 1 4 4.0 Cc1ncc(CCc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 10.1021/acsmedchemlett.3c00175
CHEMBL5394450 194987 None 0 Human Binding pKi = 9.1 9.1 - 1
Binding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assayBinding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assay
ChEMBL 386 5 1 4 4.0 Cc1ncc(CCc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 10.1021/acsmedchemlett.3c00175
68109941 156213 None 0 Human Binding pKi = 9.1 9.1 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 504 6 2 5 6.5 O[C@]1(C2CC2)CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4063313 156213 None 0 Human Binding pKi = 9.1 9.1 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 504 6 2 5 6.5 O[C@]1(C2CC2)CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
172465700 196940 None 0 Human Binding pKi = 9.0 9.0 - 1
Binding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assayBinding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assay
ChEMBL 389 5 1 3 4.5 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3ccc(F)nc3)cc2n1 10.1021/acsmedchemlett.3c00175
CHEMBL5435246 196940 None 0 Human Binding pKi = 9.0 9.0 - 1
Binding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assayBinding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assay
ChEMBL 389 5 1 3 4.5 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3ccc(F)nc3)cc2n1 10.1021/acsmedchemlett.3c00175
172462752 196664 None 0 Human Binding pKi = 9 9.0 - 1
Binding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assayBinding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assay
ChEMBL 396 5 1 4 4.2 N#Cc1ccc(CCc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 10.1021/acsmedchemlett.3c00175
CHEMBL5429261 196664 None 0 Human Binding pKi = 9 9.0 - 1
Binding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assayBinding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assay
ChEMBL 396 5 1 4 4.2 N#Cc1ccc(CCc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 10.1021/acsmedchemlett.3c00175
117972250 142399 None 4 Human Binding pKi = 9 9.0 - 1
Displacement of [3H]-JNJ-40068782 from human mGlu2 receptor expressed in HEK293 cell membranes coexpressing rat glutamate transporter measured after 30 mins in presence of orthosteric antagonist LY341495 by liquid scintillation counting methodDisplacement of [3H]-JNJ-40068782 from human mGlu2 receptor expressed in HEK293 cell membranes coexpressing rat glutamate transporter measured after 30 mins in presence of orthosteric antagonist LY341495 by liquid scintillation counting method
ChEMBL 421 6 0 4 5.5 FC(F)(F)c1c(OC[C@H]2C[C@@H]2c2ccc(Cl)cc2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
CHEMBL3885379 142399 None 4 Human Binding pKi = 9 9.0 - 1
Displacement of [3H]-JNJ-40068782 from human mGlu2 receptor expressed in HEK293 cell membranes coexpressing rat glutamate transporter measured after 30 mins in presence of orthosteric antagonist LY341495 by liquid scintillation counting methodDisplacement of [3H]-JNJ-40068782 from human mGlu2 receptor expressed in HEK293 cell membranes coexpressing rat glutamate transporter measured after 30 mins in presence of orthosteric antagonist LY341495 by liquid scintillation counting method
ChEMBL 421 6 0 4 5.5 FC(F)(F)c1c(OC[C@H]2C[C@@H]2c2ccc(Cl)cc2)ccn2c(CC3CC3)nnc12 10.1016/j.bmc.2016.11.018
11325656 126837 None 0 Rat Binding pKi = 9.0 9.0 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 353 6 4 5 0.5 N[C@@]1(C(=O)O)[C@H](OCc2cccc(C(=O)O)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL365305 126837 None 0 Rat Binding pKi = 9.0 9.0 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 353 6 4 5 0.5 N[C@@]1(C(=O)O)[C@H](OCc2cccc(C(=O)O)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
89554874 153560 None 0 Human Binding pKi = 9.0 9.0 - 1
Binding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assayBinding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assay
ChEMBL 371 5 1 3 4.3 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3cccnc3)cc2n1 10.1021/acsmedchemlett.3c00175
CHEMBL3979547 153560 None 0 Human Binding pKi = 9.0 9.0 - 1
Binding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assayBinding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assay
ChEMBL 371 5 1 3 4.3 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3cccnc3)cc2n1 10.1021/acsmedchemlett.3c00175
172469522 197012 None 0 Human Binding pKi = 9.0 9.0 - 1
Binding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assayBinding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assay
ChEMBL 385 5 1 3 4.6 Cc1ccc(CCc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 10.1021/acsmedchemlett.3c00175
CHEMBL5436775 197012 None 0 Human Binding pKi = 9.0 9.0 - 1
Binding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assayBinding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assay
ChEMBL 385 5 1 3 4.6 Cc1ccc(CCc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 10.1021/acsmedchemlett.3c00175
89554880 150132 None 0 Human Binding pKi = 8.9 8.9 - 1
Binding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assayBinding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assay
ChEMBL 372 5 1 4 3.7 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3cncnc3)cc2n1 10.1021/acsmedchemlett.3c00175
CHEMBL3950572 150132 None 0 Human Binding pKi = 8.9 8.9 - 1
Binding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assayBinding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assay
ChEMBL 372 5 1 4 3.7 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3cncnc3)cc2n1 10.1021/acsmedchemlett.3c00175
11211507 65468 None 0 Rat Binding pKi = 8.8 8.8 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 391 5 3 4 2.7 C[C@@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc(Cl)c(Cl)c1 10.1021/jm0400294
CHEMBL182972 65468 None 0 Rat Binding pKi = 8.8 8.8 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 391 5 3 4 2.7 C[C@@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc(Cl)c(Cl)c1 10.1021/jm0400294
11339150 127221 None 0 Rat Binding pKi = 8.8 8.8 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 419 7 3 4 3.4 CCC[C@@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc(Cl)c(Cl)c1 10.1021/jm0400294
CHEMBL365680 127221 None 0 Rat Binding pKi = 8.8 8.8 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 419 7 3 4 3.4 CCC[C@@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc(Cl)c(Cl)c1 10.1021/jm0400294
172440774 195545 None 0 Human Binding pKi = 8.8 8.8 - 1
Binding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assayBinding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assay
ChEMBL 404 6 1 4 4.2 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3cnc(CF)nc3)cc2n1 10.1021/acsmedchemlett.3c00175
CHEMBL5405655 195545 None 0 Human Binding pKi = 8.8 8.8 - 1
Binding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assayBinding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assay
ChEMBL 404 6 1 4 4.2 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3cnc(CF)nc3)cc2n1 10.1021/acsmedchemlett.3c00175
66786902 159555 None 0 Human Binding pKi = 8.8 8.8 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 472 5 0 5 6.8 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)c(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4101354 159555 None 0 Human Binding pKi = 8.8 8.8 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 472 5 0 5 6.8 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)c(C)n1 10.1021/acs.jmedchem.7b00669
11177216 66344 None 0 Rat Binding pKi = 8.8 8.8 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 405 6 3 4 3.1 CC[C@@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc(Cl)c(Cl)c1 10.1021/jm0400294
CHEMBL184983 66344 None 0 Rat Binding pKi = 8.8 8.8 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 405 6 3 4 3.1 CC[C@@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc(Cl)c(Cl)c1 10.1021/jm0400294
172450483 195760 None 0 Human Binding pKi = 8.8 8.8 - 1
Binding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assayBinding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assay
ChEMBL 400 6 1 4 4.4 Cc1ncc(CCc2ccc3c(-c4ccc(CF)cc4)cc(C(N)=O)nc3c2)cn1 10.1021/acsmedchemlett.3c00175
CHEMBL5410262 195760 None 0 Human Binding pKi = 8.8 8.8 - 1
Binding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assayBinding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assay
ChEMBL 400 6 1 4 4.4 Cc1ncc(CCc2ccc3c(-c4ccc(CF)cc4)cc(C(N)=O)nc3c2)cn1 10.1021/acsmedchemlett.3c00175
11383191 96657 None 0 Rat Binding pKi = 8.8 8.8 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 373 5 3 4 2.5 C[C@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc2ccccc2c1 10.1021/jm0400294
CHEMBL263312 96657 None 0 Rat Binding pKi = 8.8 8.8 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 373 5 3 4 2.5 C[C@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc2ccccc2c1 10.1021/jm0400294
71566598 142777 None 16 Human Binding pKi = 8.7 8.7 - 1
Binding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assayBinding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assay
ChEMBL 377 4 1 4 2.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1 10.1021/acsmedchemlett.3c00175
CHEMBL3892073 142777 None 16 Human Binding pKi = 8.7 8.7 - 1
Binding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assayBinding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assay
ChEMBL 377 4 1 4 2.8 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CN3C(=O)CCC3=O)cc2n1 10.1021/acsmedchemlett.3c00175
68108857 157430 None 0 Human Binding pKi = 8.7 8.7 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 465 5 1 5 5.7 O[C@H]1CC[C@H](Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4077609 157430 None 0 Human Binding pKi = 8.7 8.7 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 465 5 1 5 5.7 O[C@H]1CC[C@H](Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
66785551 157245 None 0 Human Binding pKi = 8.7 8.7 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 422 5 0 5 5.9 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4075258 157245 None 0 Human Binding pKi = 8.7 8.7 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 422 5 0 5 5.9 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
68109605 158482 None 0 Human Binding pKi = 8 8.0 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 456 5 0 5 6.3 Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cc(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4089955 158482 None 0 Human Binding pKi = 8 8.0 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 456 5 0 5 6.3 Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cc(C)n1 10.1021/acs.jmedchem.7b00669
66785027 158430 None 0 Human Binding pKi = 8.0 8.0 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 356 5 1 4 4.7 Fc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4089416 158430 None 0 Human Binding pKi = 8.0 8.0 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 356 5 1 4 4.7 Fc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CC1 10.1021/acs.jmedchem.7b00669
67637138 183724 None 0 Human Binding pKi = 8.0 8.0 -1 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 341 5 4 5 0.6 N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)cc2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4776989 183724 None 0 Human Binding pKi = 8.0 8.0 -1 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 341 5 4 5 0.6 N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)cc2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4802329 183724 None 0 Human Binding pKi = 8.0 8.0 -1 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 341 5 4 5 0.6 N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)cc2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
49836087 1061 None 0 Human Binding pKi = 6 6.0 - 1
Binding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assayBinding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assay
ChEMBL 328 2 2 4 3.3 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)Cl 10.1021/jm101069m
6222 1061 None 0 Human Binding pKi = 6 6.0 - 1
Binding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assayBinding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assay
ChEMBL 328 2 2 4 3.3 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)Cl 10.1021/jm101069m
CHEMBL1630805 1061 None 0 Human Binding pKi = 6 6.0 - 1
Binding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assayBinding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assay
ChEMBL 328 2 2 4 3.3 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)Cl 10.1021/jm101069m
15461589 100483 None 0 Rat Binding pKi = 6 6.0 - 1
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 517 7 0 7 5.8 COc1ccccc1C1C(C(=O)OCCN(C)C)=C(C)N=C2SC(c3ccc(Cl)cc3Cl)=CN21 10.1016/s0960-894x(99)00227-9
CHEMBL290416 100483 None 0 Rat Binding pKi = 6 6.0 - 1
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 517 7 0 7 5.8 COc1ccccc1C1C(C(=O)OCCN(C)C)=C(C)N=C2SC(c3ccc(Cl)cc3Cl)=CN21 10.1016/s0960-894x(99)00227-9
11756841 161412 None 0 Rat Binding pKi = 6 6.0 - 1
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 531 8 0 7 6.2 CCC1=C(C(=O)OCCN(C)C)C(c2ccccc2OC)N2C=C(c3c(Cl)cccc3Cl)SC2=N1 10.1016/s0960-894x(99)00227-9
CHEMBL41242 161412 None 0 Rat Binding pKi = 6 6.0 - 1
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 531 8 0 7 6.2 CCC1=C(C(=O)OCCN(C)C)C(c2ccccc2OC)N2C=C(c3c(Cl)cccc3Cl)SC2=N1 10.1016/s0960-894x(99)00227-9
11768848 115316 None 8 Human Binding pKi = 5.0 5.0 - 1
Displacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cellsDisplacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cells
ChEMBL 159 3 3 3 -0.7 N[C@@]1(C(=O)O)C[C@H]1CC(=O)O 10.1039/C1MD00186H
CHEMBL3347671 115316 None 8 Human Binding pKi = 5.0 5.0 - 1
Displacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cellsDisplacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cells
ChEMBL 159 3 3 3 -0.7 N[C@@]1(C(=O)O)C[C@H]1CC(=O)O 10.1039/C1MD00186H
11195342 124101 None 0 Rat Binding pKi = 7.0 7.0 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 219 2 4 4 -1.4 N[C@@]1(C(=O)O)[C@@H](O)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL363034 124101 None 0 Rat Binding pKi = 7.0 7.0 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 219 2 4 4 -1.4 N[C@@]1(C(=O)O)[C@@H](O)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
68109333 157721 None 0 Human Binding pKi = 7.9 7.9 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 459 4 1 5 5.5 O[C@H]1CC[C@H](Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4081244 157721 None 0 Human Binding pKi = 7.9 7.9 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 459 4 1 5 5.5 O[C@H]1CC[C@H](Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
66787433 156554 None 0 Human Binding pKi = 7.9 7.9 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 460 6 0 6 5.9 CCOCc1nnc2c(C(F)(F)F)c(-c3ccc(Oc4ccc(C)nc4C)c(F)c3)ccn12 10.1021/acs.jmedchem.7b00669
CHEMBL4067298 156554 None 0 Human Binding pKi = 7.9 7.9 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 460 6 0 6 5.9 CCOCc1nnc2c(C(F)(F)F)c(-c3ccc(Oc4ccc(C)nc4C)c(F)c3)ccn12 10.1021/acs.jmedchem.7b00669
66784675 157266 None 0 Human Binding pKi = 7.9 7.9 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 472 7 0 6 5.5 COc1ccc(COc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cn1 10.1021/acs.jmedchem.7b00669
CHEMBL4075537 157266 None 0 Human Binding pKi = 7.9 7.9 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 472 7 0 6 5.5 COc1ccc(COc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cn1 10.1021/acs.jmedchem.7b00669
11188098 123164 None 0 Rat Binding pKi = 7.9 7.9 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 377 5 3 4 2.1 N[C@@]1(C(=O)O)[C@H](OCc2cc(Cl)ccc2Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL361024 123164 None 0 Rat Binding pKi = 7.9 7.9 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 377 5 3 4 2.1 N[C@@]1(C(=O)O)[C@H](OCc2cc(Cl)ccc2Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
1377 1340 None 23 Human Binding pKi = 7.0 7.0 -2 6
Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2
ChEMBL 203 4 4 4 -1.6 N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O 10.1021/jm010323l
5310979 1340 None 23 Human Binding pKi = 7.0 7.0 -2 6
Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2
ChEMBL 203 4 4 4 -1.6 N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O 10.1021/jm010323l
CHEMBL284193 1340 None 23 Human Binding pKi = 7.0 7.0 -2 6
Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2
ChEMBL 203 4 4 4 -1.6 N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O 10.1021/jm010323l
1310 2315 None 61 Human Binding pKi = 5.0 5.0 -22 18
Displacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cellsDisplacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm070322e
1369 2315 None 61 Human Binding pKi = 5.0 5.0 -22 18
Displacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cellsDisplacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm070322e
33032 2315 None 61 Human Binding pKi = 5.0 5.0 -22 18
Displacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cellsDisplacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm070322e
44272391 2315 None 61 Human Binding pKi = 5.0 5.0 -22 18
Displacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cellsDisplacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm070322e
88747398 2315 None 61 Human Binding pKi = 5.0 5.0 -22 18
Displacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cellsDisplacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm070322e
CHEMBL575060 2315 None 61 Human Binding pKi = 5.0 5.0 -22 18
Displacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cellsDisplacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm070322e
DB00142 2315 None 61 Human Binding pKi = 5.0 5.0 -22 18
Displacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cellsDisplacement of [3H]LY341495 from mGluR2 receptor expressed in BHK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm070322e
71476419 123476 None 0 Human Binding pKi = 7.0 7.0 -1 2
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@H](Sc2c[nH]nn2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616860 123476 None 0 Human Binding pKi = 7.0 7.0 -1 2
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@H](Sc2c[nH]nn2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
155533313 171955 None 0 Human Binding pKi = 7.0 7.0 - 1
Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting method
ChEMBL 518 6 1 6 5.3 O=C(Nc1cccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)c1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
CHEMBL4468977 171955 None 0 Human Binding pKi = 7.0 7.0 - 1
Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting method
ChEMBL 518 6 1 6 5.3 O=C(Nc1cccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)c1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
60096194 156679 None 0 Human Binding pKi = 5.0 5.0 -10 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 290 5 4 4 0.3 N[C@@]1(C(=O)O)C[C@H](NCc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4068679 156679 None 0 Human Binding pKi = 5.0 5.0 -10 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 290 5 4 4 0.3 N[C@@]1(C(=O)O)C[C@H](NCc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
11462089 67363 None 0 Rat Binding pKi = 7.9 7.9 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 345 5 3 4 1.1 N[C@@]1(C(=O)O)[C@H](OCc2cc(F)cc(F)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL188532 67363 None 0 Rat Binding pKi = 7.9 7.9 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 345 5 3 4 1.1 N[C@@]1(C(=O)O)[C@H](OCc2cc(F)cc(F)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
1310 2315 None 61 Human Binding pKi = 5.9 5.9 -22 18
Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm010323l
1369 2315 None 61 Human Binding pKi = 5.9 5.9 -22 18
Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm010323l
33032 2315 None 61 Human Binding pKi = 5.9 5.9 -22 18
Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm010323l
44272391 2315 None 61 Human Binding pKi = 5.9 5.9 -22 18
Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm010323l
88747398 2315 None 61 Human Binding pKi = 5.9 5.9 -22 18
Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm010323l
CHEMBL575060 2315 None 61 Human Binding pKi = 5.9 5.9 -22 18
Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm010323l
DB00142 2315 None 61 Human Binding pKi = 5.9 5.9 -22 18
Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1021/jm010323l
162652146 180319 None 0 Human Binding pKi = 5.9 5.9 -1 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 289 5 4 5 -0.2 CC(C)SC[C@@H]1[C@@H](O)[C@@H]2[C@@H]([C@H]2C(=O)O)[C@]1(N)C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4749728 180319 None 0 Human Binding pKi = 5.9 5.9 -1 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 289 5 4 5 -0.2 CC(C)SC[C@@H]1[C@@H](O)[C@@H]2[C@@H]([C@H]2C(=O)O)[C@]1(N)C(=O)O 10.1021/acs.jmedchem.6b01119
71135411 123464 None 0 Human Binding pKi = 6.9 6.9 -1 2
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 298 4 4 6 -0.3 Cc1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
CHEMBL3616848 123464 None 0 Human Binding pKi = 6.9 6.9 -1 2
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 298 4 4 6 -0.3 Cc1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
71681826 90095 None 0 Human Binding pKi = 5.9 5.9 -4 2
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 293 4 3 4 1.3 N[C@@]1(C(=O)O)C[C@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL2381651 90095 None 0 Human Binding pKi = 5.9 5.9 -4 2
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 293 4 3 4 1.3 N[C@@]1(C(=O)O)C[C@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
1393 1539 None 42 Human Binding pKi = 7.9 7.9 -2 6
Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm010323l
1396 1539 None 42 Human Binding pKi = 7.9 7.9 -2 6
Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm010323l
213056 1539 None 42 Human Binding pKi = 7.9 7.9 -2 6
Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm010323l
CHEMBL8759 1539 None 42 Human Binding pKi = 7.9 7.9 -2 6
Binding affinity at Metabotropic glutamate receptor 2Binding affinity at Metabotropic glutamate receptor 2
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm010323l
172446853 195216 None 0 Human Binding pKi = 7.9 7.9 - 1
Binding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assayBinding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assay
ChEMBL 401 6 1 4 4.3 COc1ccc(CCc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 10.1021/acsmedchemlett.3c00175
CHEMBL5399050 195216 None 0 Human Binding pKi = 7.9 7.9 - 1
Binding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assayBinding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assay
ChEMBL 401 6 1 4 4.3 COc1ccc(CCc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 10.1021/acsmedchemlett.3c00175
71131322 123473 None 0 Human Binding pKi = 7.9 7.9 4 2
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 334 5 4 6 0.3 N[C@@]1(C(=O)O)C[C@H](Sc2nnc(C(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616857 123473 None 0 Human Binding pKi = 7.9 7.9 4 2
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 334 5 4 6 0.3 N[C@@]1(C(=O)O)C[C@H](Sc2nnc(C(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
60096250 159013 None 0 Human Binding pKi = 6.9 6.9 -60 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 338 4 4 4 0.6 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccc(Cl)cc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4095567 159013 None 0 Human Binding pKi = 6.9 6.9 -60 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 338 4 4 4 0.6 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccc(Cl)cc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
10197984 2421 None 36 Human Binding pKi = 7.9 7.9 2 5
Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.
ChEMBL 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10.1021/jm980616n
1394 2421 None 36 Human Binding pKi = 7.9 7.9 2 5
Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.
ChEMBL 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10.1021/jm980616n
CHEMBL275079 2421 None 36 Human Binding pKi = 7.9 7.9 2 5
Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.
ChEMBL 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10.1021/jm980616n
10197984 2421 None 36 Human Binding pKi = 7.9 7.9 2 5
Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells
ChEMBL 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10.1021/jm060917u
1394 2421 None 36 Human Binding pKi = 7.9 7.9 2 5
Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells
ChEMBL 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10.1021/jm060917u
CHEMBL275079 2421 None 36 Human Binding pKi = 7.9 7.9 2 5
Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells
ChEMBL 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10.1021/jm060917u
69669646 183785 None 0 Human Binding pKi = 7.9 7.9 1 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 351 5 4 5 1.1 Cc1ccc(SC[C@@H]2[C@@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)cc1C 10.1021/acs.jmedchem.6b01119
CHEMBL4757159 183785 None 0 Human Binding pKi = 7.9 7.9 1 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 351 5 4 5 1.1 Cc1ccc(SC[C@@H]2[C@@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)cc1C 10.1021/acs.jmedchem.6b01119
CHEMBL4802990 183785 None 0 Human Binding pKi = 7.9 7.9 1 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 351 5 4 5 1.1 Cc1ccc(SC[C@@H]2[C@@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)cc1C 10.1021/acs.jmedchem.6b01119
11348518 126362 None 0 Rat Binding pKi = 7.8 7.8 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 345 5 3 4 1.1 N[C@@]1(C(=O)O)[C@H](OCc2cc(F)ccc2F)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL365018 126362 None 0 Rat Binding pKi = 7.8 7.8 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 345 5 3 4 1.1 N[C@@]1(C(=O)O)[C@H](OCc2cc(F)ccc2F)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
66784246 156455 None 0 Human Binding pKi = 7.8 7.8 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 418 5 0 5 6.1 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C)cc2Cl)c(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4066051 156455 None 0 Human Binding pKi = 7.8 7.8 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 418 5 0 5 6.1 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C)cc2Cl)c(C)n1 10.1021/acs.jmedchem.7b00669
71136640 123469 None 0 Human Binding pKi = 6.9 6.9 1 2
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@@H](Sc2c[nH]nn2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616853 123469 None 0 Human Binding pKi = 6.9 6.9 1 2
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@@H](Sc2c[nH]nn2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
53240406 123463 None 21 Human Binding pKi = 6.8 6.8 1 2
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616847 123463 None 21 Human Binding pKi = 6.8 6.8 1 2
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
9834591 137687 None 46 Human Binding pKi = 6.8 6.8 -1 2
Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells
ChEMBL 235 2 3 5 -2.1 N[C@@]1(C(=O)O)CS(=O)(=O)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm060917u
CHEMBL375611 137687 None 46 Human Binding pKi = 6.8 6.8 -1 2
Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells
ChEMBL 235 2 3 5 -2.1 N[C@@]1(C(=O)O)CS(=O)(=O)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm060917u
89554862 144071 None 0 Human Binding pKi = 7.8 7.8 - 1
Binding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assayBinding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assay
ChEMBL 371 5 1 3 4.3 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3ccccn3)cc2n1 10.1021/acsmedchemlett.3c00175
CHEMBL3902752 144071 None 0 Human Binding pKi = 7.8 7.8 - 1
Binding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assayBinding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assay
ChEMBL 371 5 1 3 4.3 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3ccccn3)cc2n1 10.1021/acsmedchemlett.3c00175
49765871 2145 None 41 Human Binding pKi = 7.8 7.8 - 1
Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.6b00913
6317 2145 None 41 Human Binding pKi = 7.8 7.8 - 1
Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.6b00913
CHEMBL2179319 2145 None 41 Human Binding pKi = 7.8 7.8 - 1
Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)
ChEMBL 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.6b00913
11393152 67016 None 0 Rat Binding pKi = 7.8 7.8 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 324 5 4 5 0.4 Nc1cccc(CO[C@@H]2C[C@@H]3[C@H]([C@]2(N)C(=O)O)[C@@]3(F)C(=O)O)c1 10.1021/jm0400294
CHEMBL186891 67016 None 0 Rat Binding pKi = 7.8 7.8 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 324 5 4 5 0.4 Nc1cccc(CO[C@@H]2C[C@@H]3[C@H]([C@]2(N)C(=O)O)[C@@]3(F)C(=O)O)c1 10.1021/jm0400294
49822116 147080 None 14 Human Binding pKi = 6.8 6.8 - 1
Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)
ChEMBL 451 5 0 5 4.3 Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
CHEMBL3926416 147080 None 14 Human Binding pKi = 6.8 6.8 - 1
Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)
ChEMBL 451 5 0 5 4.3 Fc1ccc(N2CCN(Cc3ccn4c(CC5CC5)nnc4c3C(F)(F)F)CC2)c(F)c1 10.1021/acs.jmedchem.6b00913
9914583 142052 None 0 Rat Binding pKi = 5.8 5.8 - 1
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 517 7 0 7 5.8 COc1ccccc1C1C(C(=O)OCCN(C)C)=C(C)N=C2SC(c3c(Cl)cccc3Cl)=CN21 10.1016/s0960-894x(99)00227-9
CHEMBL38729 142052 None 0 Rat Binding pKi = 5.8 5.8 - 1
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 517 7 0 7 5.8 COc1ccccc1C1C(C(=O)OCCN(C)C)=C(C)N=C2SC(c3c(Cl)cccc3Cl)=CN21 10.1016/s0960-894x(99)00227-9
60096183 159377 None 0 Human Binding pKi = 6.8 6.8 -6 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 334 5 4 5 -0.1 COc1ccccc1C(=O)N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/acs.jmedchem.7b01481
CHEMBL4099470 159377 None 0 Human Binding pKi = 6.8 6.8 -6 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 334 5 4 5 -0.1 COc1ccccc1C(=O)N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/acs.jmedchem.7b01481
137635882 155984 None 0 Human Binding pKi = 5.8 5.8 -1 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 310 4 4 4 0.2 N[C@@]1(C(=O)O)C[C@H](NC(=O)C2CCCCC2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4060567 155984 None 0 Human Binding pKi = 5.8 5.8 -1 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 310 4 4 4 0.2 N[C@@]1(C(=O)O)C[C@H](NC(=O)C2CCCCC2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
11310142 2422 None 14 Human Binding pKi = 6.8 6.8 1 2
Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2
ChEMBL 199 2 3 3 -0.2 C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O 10.1021/jm040222y
11614 2422 None 14 Human Binding pKi = 6.8 6.8 1 2
Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2
ChEMBL 199 2 3 3 -0.2 C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O 10.1021/jm040222y
CHEMBL192051 2422 None 14 Human Binding pKi = 6.8 6.8 1 2
Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2
ChEMBL 199 2 3 3 -0.2 C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O 10.1021/jm040222y
155533313 171955 None 0 Human Binding pKi = 6.8 6.8 - 1
Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting method
ChEMBL 518 6 1 6 5.3 O=C(Nc1cccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)c1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
CHEMBL4468977 171955 None 0 Human Binding pKi = 6.8 6.8 - 1
Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting method
ChEMBL 518 6 1 6 5.3 O=C(Nc1cccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)c1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
70052526 90086 None 1 Human Binding pKi = 6.8 6.8 - 1
Displacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting methodDisplacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting method
ChEMBL 201 2 4 4 -1.5 N[C@@]1(C(=O)O)C[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1016/j.bmcl.2016.10.067
CHEMBL2381642 90086 None 1 Human Binding pKi = 6.8 6.8 - 1
Displacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting methodDisplacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting method
ChEMBL 201 2 4 4 -1.5 N[C@@]1(C(=O)O)C[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1016/j.bmcl.2016.10.067
11164815 122417 None 0 Rat Binding pKi = 7.8 7.8 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 377 5 3 4 2.1 N[C@@]1(C(=O)O)[C@@H](OCc2ccc(Cl)c(Cl)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL359973 122417 None 0 Rat Binding pKi = 7.8 7.8 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 377 5 3 4 2.1 N[C@@]1(C(=O)O)[C@@H](OCc2ccc(Cl)c(Cl)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
71137008 123471 None 0 Human Binding pKi = 6.8 6.8 -2 2
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 298 4 4 6 -0.3 Cc1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
CHEMBL3616855 123471 None 0 Human Binding pKi = 6.8 6.8 -2 2
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 298 4 4 6 -0.3 Cc1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
155548817 173944 None 0 Human Binding pKi = 6.8 6.8 - 1
Displacement of [3H]JNJ-46281222 from human mGlu2 receptor transiently expressed in CHOK1 cell membranes after 1 hr by liquid scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor transiently expressed in CHOK1 cell membranes after 1 hr by liquid scintillation counting method
ChEMBL 518 6 1 6 5.3 O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
CHEMBL4538850 173944 None 0 Human Binding pKi = 6.8 6.8 - 1
Displacement of [3H]JNJ-46281222 from human mGlu2 receptor transiently expressed in CHOK1 cell membranes after 1 hr by liquid scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor transiently expressed in CHOK1 cell membranes after 1 hr by liquid scintillation counting method
ChEMBL 518 6 1 6 5.3 O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
66785101 158137 None 0 Human Binding pKi = 7.7 7.7 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 422 6 0 5 5.9 CCc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)ccn1 10.1021/acs.jmedchem.7b00669
CHEMBL4085882 158137 None 0 Human Binding pKi = 7.7 7.7 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 422 6 0 5 5.9 CCc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)ccn1 10.1021/acs.jmedchem.7b00669
25195461 2144 None 42 Human Binding pKi = 6.8 6.8 - 1
Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
8946 2144 None 42 Human Binding pKi = 6.8 6.8 - 1
Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
CHEMBL3337527 2144 None 42 Human Binding pKi = 6.8 6.8 - 1
Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
DB12059 2144 None 42 Human Binding pKi = 6.8 6.8 - 1
Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)Displacement of [3H]8-Trifluoromethyl-3-cyclopropylmethyl-7-[(4-phenyl-1-piperidinyl)methyl]-1,2,4-triazolo[4,3-a]pyridine from mGlu2 receptor (unknown origin)
ChEMBL 344 5 0 3 4.7 CCCCn1ccc(c(c1=O)Cl)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.6b00913
1310 2315 None 61 Human Binding pKi = 5.7 5.7 -22 18
Displacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cellsDisplacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1039/C1MD00186H
1369 2315 None 61 Human Binding pKi = 5.7 5.7 -22 18
Displacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cellsDisplacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1039/C1MD00186H
33032 2315 None 61 Human Binding pKi = 5.7 5.7 -22 18
Displacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cellsDisplacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1039/C1MD00186H
44272391 2315 None 61 Human Binding pKi = 5.7 5.7 -22 18
Displacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cellsDisplacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1039/C1MD00186H
88747398 2315 None 61 Human Binding pKi = 5.7 5.7 -22 18
Displacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cellsDisplacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1039/C1MD00186H
CHEMBL575060 2315 None 61 Human Binding pKi = 5.7 5.7 -22 18
Displacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cellsDisplacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1039/C1MD00186H
DB00142 2315 None 61 Human Binding pKi = 5.7 5.7 -22 18
Displacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cellsDisplacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1039/C1MD00186H
60096246 156037 None 0 Human Binding pKi = 6.7 6.7 -40 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 334 5 4 5 -0.1 COc1ccc(C(=O)N[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)cc1 10.1021/acs.jmedchem.7b01481
CHEMBL4061162 156037 None 0 Human Binding pKi = 6.7 6.7 -40 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 334 5 4 5 -0.1 COc1ccc(C(=O)N[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)cc1 10.1021/acs.jmedchem.7b01481
89554879 153809 None 0 Human Binding pKi = 7.7 7.7 - 1
Binding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assayBinding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assay
ChEMBL 371 5 1 3 4.3 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3ccncc3)cc2n1 10.1021/acsmedchemlett.3c00175
CHEMBL3981623 153809 None 0 Human Binding pKi = 7.7 7.7 - 1
Binding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assayBinding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assay
ChEMBL 371 5 1 3 4.3 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(CCc3ccncc3)cc2n1 10.1021/acsmedchemlett.3c00175
11172339 66377 None 0 Rat Binding pKi = 6.7 6.7 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 233 3 3 4 -0.8 CO[C@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL185135 66377 None 0 Rat Binding pKi = 6.7 6.7 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 233 3 3 4 -0.8 CO[C@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O 10.1021/jm0400294
11326253 65337 None 0 Rat Binding pKi = 8.7 8.7 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 373 5 3 4 2.5 C[C@@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc2ccccc2c1 10.1021/jm0400294
CHEMBL182899 65337 None 0 Rat Binding pKi = 8.7 8.7 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 373 5 3 4 2.5 C[C@@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc2ccccc2c1 10.1021/jm0400294
68109580 158617 None 0 Human Binding pKi = 8.7 8.7 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 471 7 1 6 5.5 COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cn1 10.1021/acs.jmedchem.7b00669
CHEMBL4091370 158617 None 0 Human Binding pKi = 8.7 8.7 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 471 7 1 6 5.5 COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)cn1 10.1021/acs.jmedchem.7b00669
66786493 159773 None 0 Human Binding pKi = 8.7 8.7 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 464 5 2 5 5.7 O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4104081 159773 None 0 Human Binding pKi = 8.7 8.7 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 464 5 2 5 5.7 O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
1397 2529 None 15 Human Binding pKi = 8.7 8.7 1 5
Binding affinity to mGLUR2Binding affinity to mGLUR2
ChEMBL 377 5 3 4 2.1 OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1016/j.bmcl.2012.01.039
9886034 2529 None 15 Human Binding pKi = 8.7 8.7 1 5
Binding affinity to mGLUR2Binding affinity to mGLUR2
ChEMBL 377 5 3 4 2.1 OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1016/j.bmcl.2012.01.039
CHEMBL186453 2529 None 15 Human Binding pKi = 8.7 8.7 1 5
Binding affinity to mGLUR2Binding affinity to mGLUR2
ChEMBL 377 5 3 4 2.1 OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1016/j.bmcl.2012.01.039
49801370 157127 None 0 Human Binding pKi = 8.7 8.7 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 406 5 1 4 5.6 FC(F)(F)c1c(-c2ccc(NC3CC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
CHEMBL4073628 157127 None 0 Human Binding pKi = 8.7 8.7 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 406 5 1 4 5.6 FC(F)(F)c1c(-c2ccc(NC3CC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
11382367 66958 None 0 Rat Binding pKi = 8.6 8.6 1 2
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 345 5 3 4 1.1 N[C@@]1(C(=O)O)[C@H](OCc2ccc(F)c(F)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL186630 66958 None 0 Rat Binding pKi = 8.6 8.6 1 2
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 345 5 3 4 1.1 N[C@@]1(C(=O)O)[C@H](OCc2ccc(F)c(F)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
1397 2529 None 15 Rat Binding pKi = 8.6 8.6 -1 5
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 377 5 3 4 2.1 OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
9886034 2529 None 15 Rat Binding pKi = 8.6 8.6 -1 5
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 377 5 3 4 2.1 OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL186453 2529 None 15 Rat Binding pKi = 8.6 8.6 -1 5
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 377 5 3 4 2.1 OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
11405687 66478 None 0 Rat Binding pKi = 8.6 8.6 2 2
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 359 5 3 4 2.0 N[C@@]1(C(=O)O)[C@H](OCc2ccc3ccccc3c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL185210 66478 None 0 Rat Binding pKi = 8.6 8.6 2 2
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 359 5 3 4 2.0 N[C@@]1(C(=O)O)[C@H](OCc2ccc3ccccc3c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
70209638 157701 None 0 Human Binding pKi = 8.6 8.6 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 456 5 0 5 6.3 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4080973 157701 None 0 Human Binding pKi = 8.6 8.6 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 456 5 0 5 6.3 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
11257636 168475 None 0 Rat Binding pKi = 8.6 8.6 1 2
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 385 6 3 4 2.4 N[C@@]1(C(=O)O)[C@H](OC(c2ccccc2)c2ccccc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL434536 168475 None 0 Rat Binding pKi = 8.6 8.6 1 2
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 385 6 3 4 2.4 N[C@@]1(C(=O)O)[C@H](OC(c2ccccc2)c2ccccc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
89554797 143202 None 0 Human Binding pKi = 8.6 8.6 - 1
Binding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assayBinding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assay
ChEMBL 398 6 1 5 3.9 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)cc1 10.1021/acsmedchemlett.3c00175
CHEMBL3895570 143202 None 0 Human Binding pKi = 8.6 8.6 - 1
Binding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assayBinding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assay
ChEMBL 398 6 1 5 3.9 COc1ccc(-c2cc(C(N)=O)nc3cc(CCc4cnc(C)nc4)ccc23)cc1 10.1021/acsmedchemlett.3c00175
11375886 124423 None 0 Rat Binding pKi = 8.6 8.6 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 521 6 3 4 5.0 N[C@@]1(C(=O)O)[C@H](OC(c2ccc(Cl)c(Cl)c2)c2ccc(Cl)c(Cl)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL363724 124423 None 0 Rat Binding pKi = 8.6 8.6 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 521 6 3 4 5.0 N[C@@]1(C(=O)O)[C@H](OC(c2ccc(Cl)c(Cl)c2)c2ccc(Cl)c(Cl)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
11198402 127153 None 0 Rat Binding pKi = 8.5 8.5 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 334 5 3 5 0.7 N#Cc1cccc(CO[C@@H]2C[C@@H]3[C@H]([C@]2(N)C(=O)O)[C@@]3(F)C(=O)O)c1 10.1021/jm0400294
CHEMBL365647 127153 None 0 Rat Binding pKi = 8.5 8.5 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 334 5 3 5 0.7 N#Cc1cccc(CO[C@@H]2C[C@@H]3[C@H]([C@]2(N)C(=O)O)[C@@]3(F)C(=O)O)c1 10.1021/jm0400294
57338826 149715 None 0 Human Binding pKi = 7.7 7.7 - 1
Displacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting methodDisplacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting method
ChEMBL 375 5 4 5 1.0 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1016/j.bmcl.2016.10.067
CHEMBL3947221 149715 None 0 Human Binding pKi = 7.7 7.7 - 1
Displacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting methodDisplacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting method
ChEMBL 375 5 4 5 1.0 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1016/j.bmcl.2016.10.067
11259548 66708 None 0 Rat Binding pKi = 7.7 7.7 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 453 6 3 4 3.7 N[C@@]1(C(=O)O)[C@@H](OC(c2ccc(Cl)cc2)c2ccc(Cl)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL185456 66708 None 0 Rat Binding pKi = 7.7 7.7 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 453 6 3 4 3.7 N[C@@]1(C(=O)O)[C@@H](OC(c2ccc(Cl)cc2)c2ccc(Cl)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
162658340 183792 None 0 Human Binding pKi = 7.7 7.7 -1 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 405 6 4 5 1.9 N[C@@]1(C(=O)O)[C@H](CSCc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4760856 183792 None 0 Human Binding pKi = 7.7 7.7 -1 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 405 6 4 5 1.9 N[C@@]1(C(=O)O)[C@H](CSCc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4803084 183792 None 0 Human Binding pKi = 7.7 7.7 -1 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 405 6 4 5 1.9 N[C@@]1(C(=O)O)[C@H](CSCc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
10197984 2421 None 36 Human Binding pKi = 5.7 5.7 2 5
Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.
ChEMBL 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10.1021/jm980616n
1394 2421 None 36 Human Binding pKi = 5.7 5.7 2 5
Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.
ChEMBL 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10.1021/jm980616n
CHEMBL275079 2421 None 36 Human Binding pKi = 5.7 5.7 2 5
Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.
ChEMBL 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10.1021/jm980616n
15518713 100322 None 0 Rat Binding pKi = 5.7 5.7 - 1
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 517 7 0 7 5.8 COc1cccc(C2C(C(=O)OCCN(C)C)=C(C)N=C3SC(c4c(Cl)cccc4Cl)=CN32)c1 10.1016/s0960-894x(99)00227-9
CHEMBL288902 100322 None 0 Rat Binding pKi = 5.7 5.7 - 1
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 517 7 0 7 5.8 COc1cccc(C2C(C(=O)OCCN(C)C)=C(C)N=C3SC(c4c(Cl)cccc4Cl)=CN32)c1 10.1016/s0960-894x(99)00227-9
15461591 161991 None 0 Rat Binding pKi = 5.7 5.7 - 1
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 521 6 0 6 6.5 CC1=C(C(=O)OCCN(C)C)C(c2ccccc2Cl)N2C=C(c3c(Cl)cccc3Cl)SC2=N1 10.1016/s0960-894x(99)00227-9
CHEMBL41513 161991 None 0 Rat Binding pKi = 5.7 5.7 - 1
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 521 6 0 6 6.5 CC1=C(C(=O)OCCN(C)C)C(c2ccccc2Cl)N2C=C(c3c(Cl)cccc3Cl)SC2=N1 10.1016/s0960-894x(99)00227-9
15461594 163266 None 0 Rat Binding pKi = 5.7 5.7 - 1
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 545 8 0 7 6.6 CC1=C(C(=O)OCCN(C)C)C(c2ccccc2OC(C)C)N2C=C(c3c(Cl)cccc3Cl)SC2=N1 10.1016/s0960-894x(99)00227-9
CHEMBL41808 163266 None 0 Rat Binding pKi = 5.7 5.7 - 1
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 545 8 0 7 6.6 CC1=C(C(=O)OCCN(C)C)C(c2ccccc2OC(C)C)N2C=C(c3c(Cl)cccc3Cl)SC2=N1 10.1016/s0960-894x(99)00227-9
162658781 183797 None 0 Human Binding pKi = 7.7 7.7 -1 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 323 5 4 5 0.5 N[C@@]1(C(=O)O)[C@H](CSc2ccccc2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4759209 183797 None 0 Human Binding pKi = 7.7 7.7 -1 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 323 5 4 5 0.5 N[C@@]1(C(=O)O)[C@H](CSc2ccccc2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4803105 183797 None 0 Human Binding pKi = 7.7 7.7 -1 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 323 5 4 5 0.5 N[C@@]1(C(=O)O)[C@H](CSc2ccccc2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
66786131 157258 None 0 Human Binding pKi = 7.7 7.7 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 402 5 0 5 5.6 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4075417 157258 None 0 Human Binding pKi = 7.7 7.7 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 402 5 0 5 5.6 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
60096190 158605 None 0 Human Binding pKi = 6.7 6.7 -102 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 322 4 4 4 0.1 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2cccc(F)c2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4091203 158605 None 0 Human Binding pKi = 6.7 6.7 -102 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 322 4 4 4 0.1 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2cccc(F)c2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
60096236 158514 None 0 Human Binding pKi = 6.7 6.7 -38 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 322 4 4 4 0.1 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2F)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4090293 158514 None 0 Human Binding pKi = 6.7 6.7 -38 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 322 4 4 4 0.1 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2F)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
9815617 114563 None 3 Rat Binding pKi = 7.7 7.7 1 2
Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand
ChEMBL 203 2 3 3 -0.4 N[C@@]1(C(=O)O)CC[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm000346k
CHEMBL333519 114563 None 3 Rat Binding pKi = 7.7 7.7 1 2
Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand
ChEMBL 203 2 3 3 -0.4 N[C@@]1(C(=O)O)CC[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm000346k
68109425 158382 None 0 Human Binding pKi = 7.6 7.6 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 417 5 0 5 5.2 Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1OC1CCOCC1 10.1021/acs.jmedchem.7b00669
CHEMBL4088960 158382 None 0 Human Binding pKi = 7.6 7.6 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 417 5 0 5 5.2 Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1OC1CCOCC1 10.1021/acs.jmedchem.7b00669
45082292 115315 None 0 Human Binding pKi = 4.7 4.7 -3 3
Displacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cellsDisplacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cells
ChEMBL 159 3 3 3 -0.7 N[C@@]1(C(=O)O)C[C@@H]1CC(=O)O 10.1039/C1MD00186H
CHEMBL3347670 115315 None 0 Human Binding pKi = 4.7 4.7 -3 3
Displacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cellsDisplacement of [3H]-LY341495 from human mGluR2 receptor expressed in HEK cells
ChEMBL 159 3 3 3 -0.7 N[C@@]1(C(=O)O)C[C@@H]1CC(=O)O 10.1039/C1MD00186H
44361401 31349 None 0 Human Binding pKi = 7.6 7.6 -7 2
Binding affinity towards metabotropic glutamate receptor 2 was determinedBinding affinity towards metabotropic glutamate receptor 2 was determined
ChEMBL 175 3 4 4 -1.9 N[C@H](C(=O)O)[C@H]1[C@@H](O)[C@@H]1C(=O)O 10.1021/jm030967o
CHEMBL140197 31349 None 0 Human Binding pKi = 7.6 7.6 -7 2
Binding affinity towards metabotropic glutamate receptor 2 was determinedBinding affinity towards metabotropic glutamate receptor 2 was determined
ChEMBL 175 3 4 4 -1.9 N[C@H](C(=O)O)[C@H]1[C@@H](O)[C@@H]1C(=O)O 10.1021/jm030967o
1393 1539 None 42 Rat Binding pKi = 7.6 7.6 1 6
Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm000346k
1396 1539 None 42 Rat Binding pKi = 7.6 7.6 1 6
Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm000346k
213056 1539 None 42 Rat Binding pKi = 7.6 7.6 1 6
Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm000346k
CHEMBL8759 1539 None 42 Rat Binding pKi = 7.6 7.6 1 6
Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm000346k
11084869 90087 None 1 Human Binding pKi = 6.6 6.6 - 1
Displacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting methodDisplacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting method
ChEMBL 201 2 4 4 -1.5 N[C@@]1(C(=O)O)C[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1016/j.bmcl.2016.10.067
CHEMBL2381643 90087 None 1 Human Binding pKi = 6.6 6.6 - 1
Displacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting methodDisplacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting method
ChEMBL 201 2 4 4 -1.5 N[C@@]1(C(=O)O)C[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1016/j.bmcl.2016.10.067
155548817 173944 None 0 Human Binding pKi = 6.6 6.6 - 1
Irreversible displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 1 hr in presence of glutamate followed by compound washout and [3H]JNJ-46281222 addition measured after 1 hr by microbeta scintillation counting methodIrreversible displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 1 hr in presence of glutamate followed by compound washout and [3H]JNJ-46281222 addition measured after 1 hr by microbeta scintillation counting method
ChEMBL 518 6 1 6 5.3 O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
CHEMBL4538850 173944 None 0 Human Binding pKi = 6.6 6.6 - 1
Irreversible displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 1 hr in presence of glutamate followed by compound washout and [3H]JNJ-46281222 addition measured after 1 hr by microbeta scintillation counting methodIrreversible displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 1 hr in presence of glutamate followed by compound washout and [3H]JNJ-46281222 addition measured after 1 hr by microbeta scintillation counting method
ChEMBL 518 6 1 6 5.3 O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
69669702 183781 None 0 Human Binding pKi = 7.6 7.6 1 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 354 5 4 5 0.9 Cc1cc(SC[C@@H]2[C@@H](N)[C@H]3[C@H](C(=O)O)[C@H]3[C@]2(N)C(=O)O)ccc1F 10.1021/acs.jmedchem.6b01119
CHEMBL4756556 183781 None 0 Human Binding pKi = 7.6 7.6 1 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 354 5 4 5 0.9 Cc1cc(SC[C@@H]2[C@@H](N)[C@H]3[C@H](C(=O)O)[C@H]3[C@]2(N)C(=O)O)ccc1F 10.1021/acs.jmedchem.6b01119
CHEMBL4802948 183781 None 0 Human Binding pKi = 7.6 7.6 1 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 354 5 4 5 0.9 Cc1cc(SC[C@@H]2[C@@H](N)[C@H]3[C@H](C(=O)O)[C@H]3[C@]2(N)C(=O)O)ccc1F 10.1021/acs.jmedchem.6b01119
15518714 100378 None 0 Rat Binding pKi = 5.6 5.6 - 1
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 531 8 0 7 6.2 COc1ccccc1C1C(C(=O)OCCCN(C)C)=C(C)N=C2SC(c3c(Cl)cccc3Cl)=CN21 10.1016/s0960-894x(99)00227-9
CHEMBL289394 100378 None 0 Rat Binding pKi = 5.6 5.6 - 1
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 531 8 0 7 6.2 COc1ccccc1C1C(C(=O)OCCCN(C)C)=C(C)N=C2SC(c3c(Cl)cccc3Cl)=CN21 10.1016/s0960-894x(99)00227-9
137652500 157281 None 0 Human Binding pKi = 7.6 7.6 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 430 6 0 5 6.4 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(C)C)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4075697 157281 None 0 Human Binding pKi = 7.6 7.6 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 430 6 0 5 6.4 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(C)C)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
11361140 124385 None 0 Rat Binding pKi = 7.6 7.6 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 385 6 3 4 2.5 N[C@@]1(C(=O)O)[C@H](OCc2ccc(-c3ccccc3)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL363526 124385 None 0 Rat Binding pKi = 7.6 7.6 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 385 6 3 4 2.5 N[C@@]1(C(=O)O)[C@H](OCc2ccc(-c3ccccc3)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
59234231 2143 None 4 Human Binding pKi = 7.6 7.6 -2 2
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method
ChEMBL 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.7b00669
6330 2143 None 4 Human Binding pKi = 7.6 7.6 -2 2
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method
ChEMBL 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.7b00669
6331 2143 None 4 Human Binding pKi = 7.6 7.6 -2 2
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method
ChEMBL 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.7b00669
CHEMBL3337510 2143 None 4 Human Binding pKi = 7.6 7.6 -2 2
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method
ChEMBL 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 10.1021/acs.jmedchem.7b00669
71136655 123468 None 0 Human Binding pKi = 6.6 6.6 -1 2
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 326 5 4 6 0.5 CC(C)c1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
CHEMBL3616852 123468 None 0 Human Binding pKi = 6.6 6.6 -1 2
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 326 5 4 6 0.5 CC(C)c1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
162644419 183728 None 0 Human Binding pKi = 6.6 6.6 -1 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 323 5 4 5 0.5 N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2[C@H](O)[C@@H]1CSc1ccccc1 10.1021/acs.jmedchem.6b01119
CHEMBL4778355 183728 None 0 Human Binding pKi = 6.6 6.6 -1 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 323 5 4 5 0.5 N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2[C@H](O)[C@@H]1CSc1ccccc1 10.1021/acs.jmedchem.6b01119
CHEMBL4802356 183728 None 0 Human Binding pKi = 6.6 6.6 -1 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 323 5 4 5 0.5 N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2[C@H](O)[C@@H]1CSc1ccccc1 10.1021/acs.jmedchem.6b01119
71137011 123474 None 0 Human Binding pKi = 7.6 7.6 2 2
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 299 4 5 7 -1.0 Nc1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
CHEMBL3616858 123474 None 0 Human Binding pKi = 7.6 7.6 2 2
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 299 4 5 7 -1.0 Nc1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
10089411 7529 None 0 Human Binding pKi = 5.6 5.6 - 1
Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2
ChEMBL 353 5 3 4 2.7 NC(C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1CC1c2ccccc2Oc2ccccc21 10.1016/s0960-894x(01)00656-4
CHEMBL108735 7529 None 0 Human Binding pKi = 5.6 5.6 - 1
Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2
ChEMBL 353 5 3 4 2.7 NC(C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1CC1c2ccccc2Oc2ccccc21 10.1016/s0960-894x(01)00656-4
162663798 183825 None 0 Human Binding pKi = 6.6 6.6 -1 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 323 5 4 5 0.5 N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2[C@@H](O)[C@@H]1CSc1ccccc1 10.1021/acs.jmedchem.6b01119
CHEMBL4779554 183825 None 0 Human Binding pKi = 6.6 6.6 -1 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 323 5 4 5 0.5 N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2[C@@H](O)[C@@H]1CSc1ccccc1 10.1021/acs.jmedchem.6b01119
CHEMBL4803378 183825 None 0 Human Binding pKi = 6.6 6.6 -1 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 323 5 4 5 0.5 N[C@]1(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@@H]2[C@@H](O)[C@@H]1CSc1ccccc1 10.1021/acs.jmedchem.6b01119
11220424 159053 None 0 Human Binding pKi = 6.5 6.5 -43 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 304 4 4 4 -0.1 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4095995 159053 None 0 Human Binding pKi = 6.5 6.5 -43 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 304 4 4 4 -0.1 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
66784529 157185 None 0 Human Binding pKi = 8.5 8.5 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 430 5 2 5 5.4 O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4074421 157185 None 0 Human Binding pKi = 8.5 8.5 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 430 5 2 5 5.4 O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
11200955 64628 None 0 Rat Binding pKi = 8.5 8.5 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 419 7 3 4 3.4 CCC[C@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc(Cl)c(Cl)c1 10.1021/jm0400294
CHEMBL181710 64628 None 0 Rat Binding pKi = 8.5 8.5 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 419 7 3 4 3.4 CCC[C@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc(Cl)c(Cl)c1 10.1021/jm0400294
11177217 66697 None 0 Rat Binding pKi = 8.5 8.5 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 405 6 3 4 3.1 CC[C@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc(Cl)c(Cl)c1 10.1021/jm0400294
CHEMBL185423 66697 None 0 Rat Binding pKi = 8.5 8.5 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 405 6 3 4 3.1 CC[C@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc(Cl)c(Cl)c1 10.1021/jm0400294
1378 2417 None 39 Rat Binding pKi = 8.5 8.5 -1 10
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/jm0400294
1399 2417 None 39 Rat Binding pKi = 8.5 8.5 -1 10
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/jm0400294
9819927 2417 None 39 Rat Binding pKi = 8.5 8.5 -1 10
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/jm0400294
CHEMBL432038 2417 None 39 Rat Binding pKi = 8.5 8.5 -1 10
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/jm0400294
66785780 158836 None 0 Human Binding pKi = 8.5 8.5 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 453 7 1 6 5.4 COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2)cn1 10.1021/acs.jmedchem.7b00669
CHEMBL4093657 158836 None 0 Human Binding pKi = 8.5 8.5 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 453 7 1 6 5.4 COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2)cn1 10.1021/acs.jmedchem.7b00669
11279365 67581 None 0 Rat Binding pKi = 8.5 8.5 1 2
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 343 5 3 4 1.5 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL189814 67581 None 0 Rat Binding pKi = 8.5 8.5 1 2
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 343 5 3 4 1.5 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
11221617 67412 None 0 Rat Binding pKi = 8.5 8.5 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 343 5 3 4 1.5 N[C@@]1(C(=O)O)[C@H](OCc2cccc(Cl)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL188787 67412 None 0 Rat Binding pKi = 8.5 8.5 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 343 5 3 4 1.5 N[C@@]1(C(=O)O)[C@H](OCc2cccc(Cl)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
1395 2528 None 14 Rat Binding pKi = 8.5 8.5 2 2
Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand
ChEMBL 217 2 3 4 -1.2 O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O 10.1021/jm000346k
9837317 2528 None 14 Rat Binding pKi = 8.5 8.5 2 2
Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand
ChEMBL 217 2 3 4 -1.2 O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O 10.1021/jm000346k
CHEMBL121053 2528 None 14 Rat Binding pKi = 8.5 8.5 2 2
Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand
ChEMBL 217 2 3 4 -1.2 O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O 10.1021/jm000346k
11314439 122092 None 0 Rat Binding pKi = 8.5 8.5 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 361 5 3 4 1.6 N[C@@]1(C(=O)O)[C@H](OCc2ccc(F)c(Cl)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL359491 122092 None 0 Rat Binding pKi = 8.5 8.5 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 361 5 3 4 1.6 N[C@@]1(C(=O)O)[C@H](OCc2ccc(F)c(Cl)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
66784572 157000 None 0 Human Binding pKi = 8.4 8.4 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 468 6 0 5 6.6 Fc1cc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)ccc1Oc1ccnc(C2CC2)c1 10.1021/acs.jmedchem.7b00669
CHEMBL4072262 157000 None 0 Human Binding pKi = 8.4 8.4 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 468 6 0 5 6.6 Fc1cc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)ccc1Oc1ccnc(C2CC2)c1 10.1021/acs.jmedchem.7b00669
66785087 158232 None 0 Human Binding pKi = 8.4 8.4 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 390 5 1 4 5.1 Fc1cc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)ccc1NC1CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4087196 158232 None 0 Human Binding pKi = 8.4 8.4 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 390 5 1 4 5.1 Fc1cc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)ccc1NC1CC1 10.1021/acs.jmedchem.7b00669
11418500 122401 None 0 Rat Binding pKi = 8.4 8.4 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 411 5 3 4 2.8 N[C@@]1(C(=O)O)[C@H](OCc2cc(Cl)c(Cl)c(Cl)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL359905 122401 None 0 Rat Binding pKi = 8.4 8.4 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 411 5 3 4 2.8 N[C@@]1(C(=O)O)[C@H](OCc2cc(Cl)c(Cl)c(Cl)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
10807972 35826 None 1 Rat Binding pKi = 8.4 8.4 1 2
Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand
ChEMBL 353 5 3 4 2.8 N[C@@](CC1c2ccccc2Oc2ccccc21)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm000346k
CHEMBL144151 35826 None 1 Rat Binding pKi = 8.4 8.4 1 2
Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand
ChEMBL 353 5 3 4 2.8 N[C@@](CC1c2ccccc2Oc2ccccc21)(C(=O)O)[C@H]1C[C@@H]1C(=O)O 10.1021/jm000346k
11248009 126619 None 0 Rat Binding pKi = 8.4 8.4 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 453 6 3 4 3.7 N[C@@]1(C(=O)O)[C@H](OC(c2ccc(Cl)cc2)c2ccc(Cl)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL365244 126619 None 0 Rat Binding pKi = 8.4 8.4 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 453 6 3 4 3.7 N[C@@]1(C(=O)O)[C@H](OC(c2ccc(Cl)cc2)c2ccc(Cl)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
11153780 123898 None 0 Rat Binding pKi = 8.4 8.4 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 399 5 3 4 1.5 N[C@@]1(C(=O)O)[C@H](OCc2c(F)c(F)c(F)c(F)c2F)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL362459 123898 None 0 Rat Binding pKi = 8.4 8.4 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 399 5 3 4 1.5 N[C@@]1(C(=O)O)[C@H](OCc2c(F)c(F)c(F)c(F)c2F)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
11212336 124419 None 0 Rat Binding pKi = 8.4 8.4 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 421 6 3 4 2.7 N[C@@]1(C(=O)O)[C@H](OC(c2ccc(F)cc2)c2ccc(F)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL363696 124419 None 0 Rat Binding pKi = 8.4 8.4 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 421 6 3 4 2.7 N[C@@]1(C(=O)O)[C@H](OC(c2ccc(F)cc2)c2ccc(F)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
11485742 169577 None 0 Rat Binding pKi = 8.4 8.4 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 377 5 3 4 2.1 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)cc2Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL442967 169577 None 0 Rat Binding pKi = 8.4 8.4 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 377 5 3 4 2.1 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)cc2Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
66785300 156563 None 0 Human Binding pKi = 8.4 8.4 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 408 5 1 4 5.8 CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1Cl 10.1021/acs.jmedchem.7b00669
CHEMBL4067421 156563 None 0 Human Binding pKi = 8.4 8.4 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 408 5 1 4 5.8 CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1Cl 10.1021/acs.jmedchem.7b00669
162665071 183834 None 0 Human Binding pKi = 7.5 7.5 -1 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 323 5 4 5 0.5 N[C@@]1(C(=O)O)[C@H](CSc2ccccc2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4781638 183834 None 0 Human Binding pKi = 7.5 7.5 -1 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 323 5 4 5 0.5 N[C@@]1(C(=O)O)[C@H](CSc2ccccc2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4803454 183834 None 0 Human Binding pKi = 7.5 7.5 -1 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 323 5 4 5 0.5 N[C@@]1(C(=O)O)[C@H](CSc2ccccc2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
15518719 168583 None 0 Rat Binding pKi = 5.5 5.5 - 1
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 531 8 0 7 6.2 CCOc1ccccc1C1C(C(=O)OCCN(C)C)=C(C)N=C2SC(c3c(Cl)cccc3Cl)=CN21 10.1016/s0960-894x(99)00227-9
CHEMBL435174 168583 None 0 Rat Binding pKi = 5.5 5.5 - 1
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 531 8 0 7 6.2 CCOc1ccccc1C1C(C(=O)OCCN(C)C)=C(C)N=C2SC(c3c(Cl)cccc3Cl)=CN21 10.1016/s0960-894x(99)00227-9
60096201 158660 None 0 Human Binding pKi = 7.5 7.5 -13 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 320 4 5 5 -0.4 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2cccc(O)c2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4091735 158660 None 0 Human Binding pKi = 7.5 7.5 -13 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 320 4 5 5 -0.4 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2cccc(O)c2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
68109333 159486 None 0 Human Binding pKi = 7.5 7.5 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 459 4 1 5 5.5 O[C@H]1CC[C@@H](Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4100691 159486 None 0 Human Binding pKi = 7.5 7.5 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 459 4 1 5 5.5 O[C@H]1CC[C@@H](Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
10130658 66774 None 0 Rat Binding pKi = 7.5 7.5 2 2
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 219 2 4 4 -1.4 N[C@@]1(C(=O)O)[C@H](O)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL185822 66774 None 0 Rat Binding pKi = 7.5 7.5 2 2
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 219 2 4 4 -1.4 N[C@@]1(C(=O)O)[C@H](O)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
15518717 163468 None 0 Rat Binding pKi = 5.5 5.5 - 1
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 505 6 0 6 6.0 CC1=C(C(=O)OCCN(C)C)C(c2ccccc2F)N2C=C(c3c(Cl)cccc3Cl)SC2=N1 10.1016/s0960-894x(99)00227-9
CHEMBL41932 163468 None 0 Rat Binding pKi = 5.5 5.5 - 1
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 505 6 0 6 6.0 CC1=C(C(=O)OCCN(C)C)C(c2ccccc2F)N2C=C(c3c(Cl)cccc3Cl)SC2=N1 10.1016/s0960-894x(99)00227-9
60096204 156215 None 0 Human Binding pKi = 6.5 6.5 -75 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 322 4 4 4 0.1 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccc(F)cc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4063336 156215 None 0 Human Binding pKi = 6.5 6.5 -75 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 322 4 4 4 0.1 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccc(F)cc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
71136654 123475 None 0 Human Binding pKi = 6.5 6.5 -4 2
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 326 5 4 6 0.5 CC(C)c1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
CHEMBL3616859 123475 None 0 Human Binding pKi = 6.5 6.5 -4 2
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 326 5 4 6 0.5 CC(C)c1nnc(S[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
10197984 2421 None 36 Human Binding pKi = 7.4 7.4 2 5
Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.
ChEMBL 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10.1021/jm980616n
1394 2421 None 36 Human Binding pKi = 7.4 7.4 2 5
Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.
ChEMBL 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10.1021/jm980616n
CHEMBL275079 2421 None 36 Human Binding pKi = 7.4 7.4 2 5
Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.
ChEMBL 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10.1021/jm980616n
25125217 555 None 27 Human Binding pKi = 6.4 6.4 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method
ChEMBL 487 6 1 7 3.5 Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1 10.1021/acs.jmedchem.7b00669
7678 555 None 27 Human Binding pKi = 6.4 6.4 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method
ChEMBL 487 6 1 7 3.5 Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1 10.1021/acs.jmedchem.7b00669
CHEMBL3937907 555 None 27 Human Binding pKi = 6.4 6.4 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method
ChEMBL 487 6 1 7 3.5 Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1 10.1021/acs.jmedchem.7b00669
DB16073 555 None 27 Human Binding pKi = 6.4 6.4 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method
ChEMBL 487 6 1 7 3.5 Cc1cc(cc2c1C(=O)N(C2)Cc1ccc(cc1)OC(F)(F)F)c1onc(n1)CN1CCNCC1 10.1021/acs.jmedchem.7b00669
68109272 158710 None 0 Human Binding pKi = 7.4 7.4 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 416 5 1 5 5.2 Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CCOCC1 10.1021/acs.jmedchem.7b00669
CHEMBL4092275 158710 None 0 Human Binding pKi = 7.4 7.4 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 416 5 1 5 5.2 Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CCOCC1 10.1021/acs.jmedchem.7b00669
10192719 66135 None 0 Rat Binding pKi = 7.4 7.4 2 2
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 233 3 3 4 -0.8 CO[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL183956 66135 None 0 Rat Binding pKi = 7.4 7.4 2 2
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 233 3 3 4 -0.8 CO[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O 10.1021/jm0400294
137659992 159329 None 0 Human Binding pKi = 6.4 6.4 -14 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 338 4 4 4 0.6 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2Cl)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4098939 159329 None 0 Human Binding pKi = 6.4 6.4 -14 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 338 4 4 4 0.6 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2Cl)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
11360426 123870 None 0 Rat Binding pKi = 8.4 8.4 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 361 5 3 4 1.6 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(F)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL362325 123870 None 0 Rat Binding pKi = 8.4 8.4 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 361 5 3 4 1.6 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(F)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
11749464 125103 None 0 Rat Binding pKi = 8.4 8.4 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 385 6 3 4 2.5 N[C@@]1(C(=O)O)[C@H](OCc2ccccc2-c2ccccc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL364320 125103 None 0 Rat Binding pKi = 8.4 8.4 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 385 6 3 4 2.5 N[C@@]1(C(=O)O)[C@H](OCc2ccccc2-c2ccccc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
155567633 176104 None 0 Human Binding pKi = 8.4 8.4 - 1
Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting method
ChEMBL 532 7 1 6 5.0 O=C(NCc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
CHEMBL4589377 176104 None 0 Human Binding pKi = 8.4 8.4 - 1
Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting method
ChEMBL 532 7 1 6 5.0 O=C(NCc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
11484738 166372 None 0 Rat Binding pKi = 8.4 8.4 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 345 5 3 4 1.1 N[C@@]1(C(=O)O)[C@H](OCc2cccc(F)c2F)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL426983 166372 None 0 Rat Binding pKi = 8.4 8.4 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 345 5 3 4 1.1 N[C@@]1(C(=O)O)[C@H](OCc2cccc(F)c2F)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
11268934 67148 None 0 Rat Binding pKi = 8.4 8.4 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 377 5 3 4 2.1 N[C@@]1(C(=O)O)[C@H](OCc2c(Cl)cccc2Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL187482 67148 None 0 Rat Binding pKi = 8.4 8.4 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 377 5 3 4 2.1 N[C@@]1(C(=O)O)[C@H](OCc2c(Cl)cccc2Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
1378 2417 None 39 Human Binding pKi = 8.4 8.4 -2 10
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/acs.jmedchem.6b01119
1399 2417 None 39 Human Binding pKi = 8.4 8.4 -2 10
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/acs.jmedchem.6b01119
9819927 2417 None 39 Human Binding pKi = 8.4 8.4 -2 10
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/acs.jmedchem.6b01119
CHEMBL432038 2417 None 39 Human Binding pKi = 8.4 8.4 -2 10
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10.1021/acs.jmedchem.6b01119
11188099 66848 None 0 Rat Binding pKi = 8.4 8.4 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 377 5 3 4 2.1 N[C@@]1(C(=O)O)[C@H](OCc2cccc(Cl)c2Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL186107 66848 None 0 Rat Binding pKi = 8.4 8.4 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 377 5 3 4 2.1 N[C@@]1(C(=O)O)[C@H](OCc2cccc(Cl)c2Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
10353365 83279 None 1 Human Binding pKi = 8.4 8.4 -5 2
Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells
ChEMBL 219 2 3 4 -1.8 N[C@@]1(C(=O)O)C[S+]([O-])[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm060917u
CHEMBL218710 83279 None 1 Human Binding pKi = 8.4 8.4 -5 2
Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells
ChEMBL 219 2 3 4 -1.8 N[C@@]1(C(=O)O)C[S+]([O-])[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm060917u
172467224 196652 None 0 Human Binding pKi = 8.4 8.4 - 1
Binding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assayBinding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assay
ChEMBL 402 6 1 5 3.7 COc1ncc(CCc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 10.1021/acsmedchemlett.3c00175
CHEMBL5429002 196652 None 0 Human Binding pKi = 8.4 8.4 - 1
Binding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assayBinding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assay
ChEMBL 402 6 1 5 3.7 COc1ncc(CCc2ccc3c(-c4ccc(F)cc4)cc(C(N)=O)nc3c2)cn1 10.1021/acsmedchemlett.3c00175
11255753 122341 None 0 Rat Binding pKi = 8.3 8.3 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 323 5 3 4 1.1 Cc1cccc(CO[C@@H]2C[C@@H]3[C@H]([C@]2(N)C(=O)O)[C@@]3(F)C(=O)O)c1 10.1021/jm0400294
CHEMBL359805 122341 None 0 Rat Binding pKi = 8.3 8.3 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 323 5 3 4 1.1 Cc1cccc(CO[C@@H]2C[C@@H]3[C@H]([C@]2(N)C(=O)O)[C@@]3(F)C(=O)O)c1 10.1021/jm0400294
11290903 67359 None 0 Rat Binding pKi = 8.3 8.3 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 345 5 3 4 1.1 N[C@@]1(C(=O)O)[C@H](OCc2ccc(F)cc2F)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL188511 67359 None 0 Rat Binding pKi = 8.3 8.3 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 345 5 3 4 1.1 N[C@@]1(C(=O)O)[C@H](OCc2ccc(F)cc2F)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
11188380 67487 None 0 Rat Binding pKi = 8.3 8.3 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 387 5 3 4 1.6 N[C@@]1(C(=O)O)[C@H](OCc2cccc(Br)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL189186 67487 None 0 Rat Binding pKi = 8.3 8.3 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 387 5 3 4 1.6 N[C@@]1(C(=O)O)[C@H](OCc2cccc(Br)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
11163717 123737 None 0 Rat Binding pKi = 8.3 8.3 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 343 5 3 4 1.5 N[C@@]1(C(=O)O)[C@H](OCc2ccccc2Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL362092 123737 None 0 Rat Binding pKi = 8.3 8.3 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 343 5 3 4 1.5 N[C@@]1(C(=O)O)[C@H](OCc2ccccc2Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
89544007 147134 None 0 Human Binding pKi = 7.4 7.4 - 1
Binding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assayBinding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assay
ChEMBL 358 4 1 4 3.5 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cc3cncnc3)cc2n1 10.1021/acsmedchemlett.3c00175
CHEMBL3926904 147134 None 0 Human Binding pKi = 7.4 7.4 - 1
Binding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assayBinding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assay
ChEMBL 358 4 1 4 3.5 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cc3cncnc3)cc2n1 10.1021/acsmedchemlett.3c00175
10198133 208966 None 10 Human Binding pKi = 7.4 7.4 -6 2
Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.
ChEMBL 203 2 3 4 -0.8 N[C@@]1(C(=O)O)CS[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm980616n
CHEMBL8839 208966 None 10 Human Binding pKi = 7.4 7.4 -6 2
Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.
ChEMBL 203 2 3 4 -0.8 N[C@@]1(C(=O)O)CS[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm980616n
10198133 208966 None 10 Human Binding pKi = 7.4 7.4 -6 2
Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells
ChEMBL 203 2 3 4 -0.8 N[C@@]1(C(=O)O)CS[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm060917u
CHEMBL8839 208966 None 10 Human Binding pKi = 7.4 7.4 -6 2
Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells
ChEMBL 203 2 3 4 -0.8 N[C@@]1(C(=O)O)CS[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm060917u
15518715 100375 None 0 Rat Binding pKi = 5.4 5.4 - 1
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 545 8 0 7 6.5 COc1ccccc1C1C(C(=O)OCCN(C)C)=C(C(C)C)N=C2SC(c3c(Cl)cccc3Cl)=CN21 10.1016/s0960-894x(99)00227-9
CHEMBL289388 100375 None 0 Rat Binding pKi = 5.4 5.4 - 1
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 545 8 0 7 6.5 COc1ccccc1C1C(C(=O)OCCN(C)C)=C(C(C)C)N=C2SC(c3c(Cl)cccc3Cl)=CN21 10.1016/s0960-894x(99)00227-9
15518712 100548 None 0 Rat Binding pKi = 5.4 5.4 - 1
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 483 7 0 7 5.2 COc1ccccc1C1C(C(=O)OCCN(C)C)=C(C)N=C2SC(c3ccc(Cl)cc3)=CN21 10.1016/s0960-894x(99)00227-9
CHEMBL291017 100548 None 0 Rat Binding pKi = 5.4 5.4 - 1
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 483 7 0 7 5.2 COc1ccccc1C1C(C(=O)OCCN(C)C)=C(C)N=C2SC(c3ccc(Cl)cc3)=CN21 10.1016/s0960-894x(99)00227-9
15392100 169198 None 0 Rat Binding pKi = 5.4 5.4 - 1
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 474 5 0 6 6.3 CCOC(=O)C1=C(C)N=C2SC(c3c(Cl)cccc3Cl)=CN2C1c1ccccc1OC 10.1016/s0960-894x(99)00227-9
CHEMBL439925 169198 None 0 Rat Binding pKi = 5.4 5.4 - 1
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 474 5 0 6 6.3 CCOC(=O)C1=C(C)N=C2SC(c3c(Cl)cccc3Cl)=CN2C1c1ccccc1OC 10.1016/s0960-894x(99)00227-9
11310142 2422 None 14 Human Binding pKi = 6.4 6.4 1 2
Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2
ChEMBL 199 2 3 3 -0.2 C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O 10.1021/jm040222y
11614 2422 None 14 Human Binding pKi = 6.4 6.4 1 2
Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2
ChEMBL 199 2 3 3 -0.2 C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O 10.1021/jm040222y
CHEMBL192051 2422 None 14 Human Binding pKi = 6.4 6.4 1 2
Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2
ChEMBL 199 2 3 3 -0.2 C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O 10.1021/jm040222y
60096231 157747 None 19 Human Binding pKi = 6.4 6.4 -446 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 334 5 4 5 -0.1 COc1cccc(C(=O)N[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)c1 10.1021/acs.jmedchem.7b01481
CHEMBL4081453 157747 None 19 Human Binding pKi = 6.4 6.4 -446 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 334 5 4 5 -0.1 COc1cccc(C(=O)N[C@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)c1 10.1021/acs.jmedchem.7b01481
10979251 90094 None 0 Human Binding pKi = 6.4 6.4 -3 2
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 293 4 3 4 1.3 N[C@@]1(C(=O)O)C[C@@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL2381650 90094 None 0 Human Binding pKi = 6.4 6.4 -3 2
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 293 4 3 4 1.3 N[C@@]1(C(=O)O)C[C@@H](Sc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
162666357 183837 None 0 Human Binding pKi = 7.4 7.4 -1 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 341 5 4 5 0.6 N[C@@]1(C(=O)O)[C@H](CSc2cccc(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4784701 183837 None 0 Human Binding pKi = 7.4 7.4 -1 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 341 5 4 5 0.6 N[C@@]1(C(=O)O)[C@H](CSc2cccc(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4803523 183837 None 0 Human Binding pKi = 7.4 7.4 -1 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 341 5 4 5 0.6 N[C@@]1(C(=O)O)[C@H](CSc2cccc(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
11275666 90091 None 1 Human Binding pKi = 5.4 5.4 -15 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 200 2 4 4 -1.6 N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/acs.jmedchem.7b01481
CHEMBL2381647 90091 None 1 Human Binding pKi = 5.4 5.4 -15 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 200 2 4 4 -1.6 N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/acs.jmedchem.7b01481
9815616 114864 None 4 Rat Binding pKi = 7.3 7.3 1 2
Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand
ChEMBL 203 2 3 3 -0.5 N[C@@]1(C(=O)O)[C@@H](F)C[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm000346k
CHEMBL334014 114864 None 4 Rat Binding pKi = 7.3 7.3 1 2
Tested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligandTested for binding affinity against Metabotropic glutamate receptor 2 in CHO cells using [3H]-7 as radioligand
ChEMBL 203 2 3 3 -0.5 N[C@@]1(C(=O)O)[C@@H](F)C[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm000346k
66787355 156316 None 0 Human Binding pKi = 8.3 8.3 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 450 5 1 5 5.6 FC(F)(F)c1c(-c2ccc(NC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
CHEMBL4064589 156316 None 0 Human Binding pKi = 8.3 8.3 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 450 5 1 5 5.6 FC(F)(F)c1c(-c2ccc(NC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
11196276 168443 None 0 Rat Binding pKi = 8.3 8.3 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 261 5 3 4 0.0 CCCO[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL434338 168443 None 0 Rat Binding pKi = 8.3 8.3 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 261 5 3 4 0.0 CCCO[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O 10.1021/jm0400294
67637415 183793 None 0 Human Binding pKi = 8.3 8.3 -1 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 438 7 4 7 1.9 Cc1cc(SC[C@@H]2[C@@H](Sc3nc[nH]n3)[C@H]3[C@H](C(=O)O)[C@H]3[C@]2(N)C(=O)O)ccc1F 10.1021/acs.jmedchem.6b01119
CHEMBL4759992 183793 None 0 Human Binding pKi = 8.3 8.3 -1 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 438 7 4 7 1.9 Cc1cc(SC[C@@H]2[C@@H](Sc3nc[nH]n3)[C@H]3[C@H](C(=O)O)[C@H]3[C@]2(N)C(=O)O)ccc1F 10.1021/acs.jmedchem.6b01119
CHEMBL4803099 183793 None 0 Human Binding pKi = 8.3 8.3 -1 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 438 7 4 7 1.9 Cc1cc(SC[C@@H]2[C@@H](Sc3nc[nH]n3)[C@H]3[C@H](C(=O)O)[C@H]3[C@]2(N)C(=O)O)ccc1F 10.1021/acs.jmedchem.6b01119
66786069 156552 None 0 Human Binding pKi = 8.3 8.3 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 451 5 0 5 5.6 FC(F)(F)c1c(-c2ccc(OC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
CHEMBL4067290 156552 None 0 Human Binding pKi = 8.3 8.3 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 451 5 0 5 5.6 FC(F)(F)c1c(-c2ccc(OC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
69669747 183759 None 14 Human Binding pKi = 8.3 8.3 -2 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 359 5 4 5 0.8 N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)c(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4751065 183759 None 14 Human Binding pKi = 8.3 8.3 -2 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 359 5 4 5 0.8 N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)c(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4802733 183759 None 14 Human Binding pKi = 8.3 8.3 -2 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 359 5 4 5 0.8 N[C@@]1(C(=O)O)[C@H](CSc2ccc(F)c(F)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
11268363 124806 None 0 Rat Binding pKi = 8.3 8.3 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 359 5 3 4 2.0 N[C@@]1(C(=O)O)[C@H](OCc2cccc3ccccc23)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL364201 124806 None 0 Rat Binding pKi = 8.3 8.3 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 359 5 3 4 2.0 N[C@@]1(C(=O)O)[C@H](OCc2cccc3ccccc23)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
11450243 67479 None 0 Rat Binding pKi = 8.3 8.3 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 327 5 3 4 0.9 N[C@@]1(C(=O)O)[C@H](OCc2ccc(F)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL189139 67479 None 0 Rat Binding pKi = 8.3 8.3 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 327 5 3 4 0.9 N[C@@]1(C(=O)O)[C@H](OCc2ccc(F)cc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
11451742 124512 None 0 Rat Binding pKi = 8.3 8.3 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 377 5 3 4 2.1 N[C@@]1(C(=O)O)[C@H](OCc2cc(Cl)cc(Cl)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL363980 124512 None 0 Rat Binding pKi = 8.3 8.3 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 377 5 3 4 2.1 N[C@@]1(C(=O)O)[C@H](OCc2cc(Cl)cc(Cl)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
11349412 67565 None 0 Rat Binding pKi = 8.2 8.2 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 377 5 3 4 1.8 N[C@@]1(C(=O)O)[C@H](OCc2cccc(C(F)(F)F)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL189710 67565 None 0 Rat Binding pKi = 8.2 8.2 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 377 5 3 4 1.8 N[C@@]1(C(=O)O)[C@H](OCc2cccc(C(F)(F)F)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
155567633 176104 None 0 Human Binding pKi = 8.2 8.2 - 1
Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting method
ChEMBL 532 7 1 6 5.0 O=C(NCc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
CHEMBL4589377 176104 None 0 Human Binding pKi = 8.2 8.2 - 1
Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting method
ChEMBL 532 7 1 6 5.0 O=C(NCc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
11338331 65555 None 0 Rat Binding pKi = 8.2 8.2 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 391 5 3 4 2.7 C[C@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc(Cl)c(Cl)c1 10.1021/jm0400294
CHEMBL183073 65555 None 0 Rat Binding pKi = 8.2 8.2 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 391 5 3 4 2.7 C[C@H](O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O)c1ccc(Cl)c(Cl)c1 10.1021/jm0400294
11313770 123942 None 0 Rat Binding pKi = 8.2 8.2 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 339 6 3 5 0.8 COc1cccc(CO[C@@H]2C[C@@H]3[C@H]([C@]2(N)C(=O)O)[C@@]3(F)C(=O)O)c1 10.1021/jm0400294
CHEMBL362708 123942 None 0 Rat Binding pKi = 8.2 8.2 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 339 6 3 5 0.8 COc1cccc(CO[C@@H]2C[C@@H]3[C@H]([C@]2(N)C(=O)O)[C@@]3(F)C(=O)O)c1 10.1021/jm0400294
10353365 83279 None 1 Human Binding pKi = 6.3 6.3 -5 2
Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells
ChEMBL 219 2 3 4 -1.8 N[C@@]1(C(=O)O)C[S+]([O-])[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm060917u
CHEMBL218710 83279 None 1 Human Binding pKi = 6.3 6.3 -5 2
Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells
ChEMBL 219 2 3 4 -1.8 N[C@@]1(C(=O)O)C[S+]([O-])[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm060917u
66785182 157270 None 0 Human Binding pKi = 7.3 7.3 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 434 6 0 5 6.2 Fc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1Oc1ccnc(C2CC2)c1 10.1021/acs.jmedchem.7b00669
CHEMBL4075593 157270 None 0 Human Binding pKi = 7.3 7.3 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 434 6 0 5 6.2 Fc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1Oc1ccnc(C2CC2)c1 10.1021/acs.jmedchem.7b00669
60096228 156879 None 0 Human Binding pKi = 7.3 7.3 -5 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 320 4 5 5 -0.4 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccc(O)cc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4070866 156879 None 0 Human Binding pKi = 7.3 7.3 -5 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 320 4 5 5 -0.4 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccc(O)cc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
60096224 156636 None 0 Human Binding pKi = 7.2 7.2 -32 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 320 4 5 5 -0.4 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2O)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4068189 156636 None 0 Human Binding pKi = 7.2 7.2 -32 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 320 4 5 5 -0.4 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2ccccc2O)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL5076351 216918 None 0 Human Binding pKi = 7.2 7.2 - 1
Binding affinity to human recombinant mGlur2 assessed as inhibition constant by cAMP Glosensor assayBinding affinity to human recombinant mGlur2 assessed as inhibition constant by cAMP Glosensor assay
ChEMBL None None None CC1(C)CCc2c(-c3ccc(F)cc3F)cc(C(N)=O)nc2O1 10.1021/acs.jmedchem.1c02004
CHEMBL5076351 216918 None 0 Human Binding pKi = 7.2 7.2 - 1
Binding affinity to human recombinant mGlur2 assessed as inhibition constant by cAMP Glosensor assayBinding affinity to human recombinant mGlur2 assessed as inhibition constant by cAMP Glosensor assay
ChEMBL None None None CC1(C)CCc2c(-c3ccc(F)cc3F)cc(C(N)=O)nc2O1 10.1021/acs.jmedchem.1c02004
137634033 156732 None 0 Human Binding pKi = 6.2 6.2 -2 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 332 6 4 4 0.2 N[C@@]1(C(=O)O)C[C@H](NC(=O)CCc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4069251 156732 None 0 Human Binding pKi = 6.2 6.2 -2 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 332 6 4 4 0.2 N[C@@]1(C(=O)O)C[C@H](NC(=O)CCc2ccccc2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
68109335 157203 None 0 Human Binding pKi = 8.2 8.2 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 438 5 0 5 6.5 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2Cl)c(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4074664 157203 None 0 Human Binding pKi = 8.2 8.2 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 438 5 0 5 6.5 Cc1ccc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2Cl)c(C)n1 10.1021/acs.jmedchem.7b00669
68109677 157285 None 0 Human Binding pKi = 8.2 8.2 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 458 4 2 5 5.5 O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4075762 157285 None 0 Human Binding pKi = 8.2 8.2 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 458 4 2 5 5.5 O[C@H]1CC[C@H](Nc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
155548817 173944 None 0 Human Binding pKi = 8.2 8.2 - 1
Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting method
ChEMBL 518 6 1 6 5.3 O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
CHEMBL4538850 173944 None 0 Human Binding pKi = 8.2 8.2 - 1
Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting method
ChEMBL 518 6 1 6 5.3 O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
66786816 158448 None 0 Human Binding pKi = 8.2 8.2 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 426 6 0 6 5.5 CCOCc1nnc2c(Cl)c(-c3ccc(Oc4ccc(C)nc4C)c(F)c3)ccn12 10.1021/acs.jmedchem.7b00669
CHEMBL4089612 158448 None 0 Human Binding pKi = 8.2 8.2 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 426 6 0 6 5.5 CCOCc1nnc2c(Cl)c(-c3ccc(Oc4ccc(C)nc4C)c(F)c3)ccn12 10.1021/acs.jmedchem.7b00669
44396480 66858 None 0 Rat Binding pKi = 8.2 8.2 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 275 5 3 4 0.4 CCC(C)O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL186145 66858 None 0 Rat Binding pKi = 8.2 8.2 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 275 5 3 4 0.4 CCC(C)O[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O 10.1021/jm0400294
89554847 145009 None 0 Human Binding pKi = 8.2 8.2 - 1
Binding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assayBinding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assay
ChEMBL 357 4 1 3 4.1 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cc3cccnc3)cc2n1 10.1021/acsmedchemlett.3c00175
CHEMBL3910265 145009 None 0 Human Binding pKi = 8.2 8.2 - 1
Binding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assayBinding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assay
ChEMBL 357 4 1 3 4.1 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cc3cccnc3)cc2n1 10.1021/acsmedchemlett.3c00175
66785010 155953 None 0 Human Binding pKi = 8.2 8.2 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 372 5 1 4 5.2 Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4060306 155953 None 0 Human Binding pKi = 8.2 8.2 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 372 5 1 4 5.2 Clc1cc(-c2ccn3c(CC4CC4)nnc3c2Cl)ccc1NC1CC1 10.1021/acs.jmedchem.7b00669
3954 664 None 44 Human Binding pKi = 7.2 7.2 46 2
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method
ChEMBL 454 6 1 3 6.8 Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1 10.1021/acs.jmedchem.7b00669
9868580 664 None 44 Human Binding pKi = 7.2 7.2 46 2
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method
ChEMBL 454 6 1 3 6.8 Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1 10.1021/acs.jmedchem.7b00669
CHEMBL593013 664 None 44 Human Binding pKi = 7.2 7.2 46 2
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method
ChEMBL 454 6 1 3 6.8 Cc1c(OCc2cccc(c2)c2ccc(cc2)C(=O)O)cc2c(c1C)C(=O)C(C2)C1CCCC1 10.1021/acs.jmedchem.7b00669
71136653 123470 None 0 Human Binding pKi = 7.2 7.2 2 2
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616854 123470 None 0 Human Binding pKi = 7.2 7.2 2 2
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 284 4 4 6 -0.6 N[C@@]1(C(=O)O)C[C@H](Sc2nnc[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
49858117 1089 None 4 Human Binding pKi = 6.2 6.2 - 1
Binding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assayBinding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assay
ChEMBL 308 2 2 4 3.0 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)C 10.1021/jm101069m
6223 1089 None 4 Human Binding pKi = 6.2 6.2 - 1
Binding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assayBinding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assay
ChEMBL 308 2 2 4 3.0 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)C 10.1021/jm101069m
CHEMBL1630806 1089 None 4 Human Binding pKi = 6.2 6.2 - 1
Binding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assayBinding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assay
ChEMBL 308 2 2 4 3.0 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)C 10.1021/jm101069m
66784890 156141 None 0 Human Binding pKi = 7.2 7.2 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 358 5 1 4 5.0 CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2Cl)cc1F 10.1021/acs.jmedchem.7b00669
CHEMBL4062535 156141 None 0 Human Binding pKi = 7.2 7.2 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 358 5 1 4 5.0 CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2Cl)cc1F 10.1021/acs.jmedchem.7b00669
68109379 157317 None 0 Human Binding pKi = 7.2 7.2 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 464 6 1 5 5.3 FC(F)(F)c1c(-c2ccc(CNC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
CHEMBL4076286 157317 None 0 Human Binding pKi = 7.2 7.2 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 464 6 1 5 5.3 FC(F)(F)c1c(-c2ccc(CNC3CCOCC3)c(Cl)c2)ccn2c(CC3CC3)nnc12 10.1021/acs.jmedchem.7b00669
155548817 173944 None 0 Human Binding pKi = 7.2 7.2 - 1
Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting method
ChEMBL 518 6 1 6 5.3 O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
CHEMBL4538850 173944 None 0 Human Binding pKi = 7.2 7.2 - 1
Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting method
ChEMBL 518 6 1 6 5.3 O=C(Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1)c1ccc(S(=O)(=O)F)cc1 10.1021/acs.jmedchem.8b00051
137656301 158774 None 0 Human Binding pKi = 6.2 6.2 -1 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 324 5 4 4 0.6 N[C@@]1(C(=O)O)C[C@H](NC(=O)CC2CCCCC2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4093017 158774 None 0 Human Binding pKi = 6.2 6.2 -1 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 324 5 4 4 0.6 N[C@@]1(C(=O)O)C[C@H](NC(=O)CC2CCCCC2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL5089623 217707 None 3 Human Binding pKi = 7.2 7.2 - 1
Binding affinity to human recombinant mGlur2 assessed as inhibition constant by cAMP Glosensor assayBinding affinity to human recombinant mGlur2 assessed as inhibition constant by cAMP Glosensor assay
ChEMBL None None None COc1ccc(-c2cc(C(N)=O)nc3c2CCC(C)(C)O3)c(F)c1 10.1021/acs.jmedchem.1c02004
CHEMBL5089623 217707 None 3 Human Binding pKi = 7.2 7.2 - 1
Binding affinity to human recombinant mGlur2 assessed as inhibition constant by cAMP Glosensor assayBinding affinity to human recombinant mGlur2 assessed as inhibition constant by cAMP Glosensor assay
ChEMBL None None None COc1ccc(-c2cc(C(N)=O)nc3c2CCC(C)(C)O3)c(F)c1 10.1021/acs.jmedchem.1c02004
49801371 158833 None 0 Human Binding pKi = 7.2 7.2 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 408 5 0 5 5.6 Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)ccn1 10.1021/acs.jmedchem.7b00669
CHEMBL4093620 158833 None 0 Human Binding pKi = 7.2 7.2 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 408 5 0 5 5.6 Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2F)ccn1 10.1021/acs.jmedchem.7b00669
11344646 126844 None 0 Human Binding pKi = 6.2 6.2 -1 2
Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2
ChEMBL 199 2 3 3 -0.2 C[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/jm040222y
CHEMBL365368 126844 None 0 Human Binding pKi = 6.2 6.2 -1 2
Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2
ChEMBL 199 2 3 3 -0.2 C[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/jm040222y
1310 2315 None 61 Human Binding pKi = 5.2 5.2 -22 18
Displacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cellsDisplacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmc.2008.11.015
1369 2315 None 61 Human Binding pKi = 5.2 5.2 -22 18
Displacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cellsDisplacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmc.2008.11.015
33032 2315 None 61 Human Binding pKi = 5.2 5.2 -22 18
Displacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cellsDisplacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmc.2008.11.015
44272391 2315 None 61 Human Binding pKi = 5.2 5.2 -22 18
Displacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cellsDisplacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmc.2008.11.015
88747398 2315 None 61 Human Binding pKi = 5.2 5.2 -22 18
Displacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cellsDisplacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmc.2008.11.015
CHEMBL575060 2315 None 61 Human Binding pKi = 5.2 5.2 -22 18
Displacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cellsDisplacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmc.2008.11.015
DB00142 2315 None 61 Human Binding pKi = 5.2 5.2 -22 18
Displacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cellsDisplacement of [3H]Quisqualate from human mGluR2 receptor expressed in BHK cells
ChEMBL 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10.1016/j.bmc.2008.11.015
49858116 56364 None 0 Human Binding pKi = 5.2 5.2 - 1
Binding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assayBinding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assay
ChEMBL 312 2 2 4 2.8 O=C(Nc1ccc(F)cc1)C12CC1/C(=N\O)c1ccccc1O2 10.1021/jm101069m
CHEMBL1630804 56364 None 0 Human Binding pKi = 5.2 5.2 - 1
Binding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assayBinding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assay
ChEMBL 312 2 2 4 2.8 O=C(Nc1ccc(F)cc1)C12CC1/C(=N\O)c1ccccc1O2 10.1021/jm101069m
71137012 123467 None 0 Human Binding pKi = 7.2 7.2 -1 2
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 299 4 5 7 -1.0 Nc1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
CHEMBL3616851 123467 None 0 Human Binding pKi = 7.2 7.2 -1 2
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 299 4 5 7 -1.0 Nc1nnc(S[C@@H]2C[C@@](N)(C(=O)O)[C@@H]3[C@@H](C(=O)O)[C@H]23)[nH]1 10.1021/acs.jmedchem.5b01124
10198133 208966 None 10 Human Binding pKi = 7.2 7.2 -6 2
Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.
ChEMBL 203 2 3 4 -0.8 N[C@@]1(C(=O)O)CS[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm980616n
CHEMBL8839 208966 None 10 Human Binding pKi = 7.2 7.2 -6 2
Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.
ChEMBL 203 2 3 4 -0.8 N[C@@]1(C(=O)O)CS[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm980616n
172461011 196525 None 0 Human Binding pKi = 8.2 8.2 - 1
Binding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assayBinding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assay
ChEMBL 357 4 1 3 4.1 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cc3ccncc3)cc2n1 10.1021/acsmedchemlett.3c00175
CHEMBL5425858 196525 None 0 Human Binding pKi = 8.2 8.2 - 1
Binding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assayBinding affinity to human mGluR2 expressed in cell membrane incubated for 1 hr in presence of tritium labeled [3H]-7-((2,5-dioxopyrrolidin-1-yl)methyl)-4-(4-fluorophenyl)quinoline-2-carboxamide by competitive radioligand binding assay
ChEMBL 357 4 1 3 4.1 NC(=O)c1cc(-c2ccc(F)cc2)c2ccc(Cc3ccncc3)cc2n1 10.1021/acsmedchemlett.3c00175
11484739 123169 None 0 Rat Binding pKi = 8.2 8.2 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 345 5 3 4 1.1 N[C@@]1(C(=O)O)[C@H](OCc2c(F)cccc2F)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL361051 123169 None 0 Rat Binding pKi = 8.2 8.2 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 345 5 3 4 1.1 N[C@@]1(C(=O)O)[C@H](OCc2c(F)cccc2F)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
11817779 66229 None 0 Rat Binding pKi = 8.2 8.2 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 259 5 3 4 -0.2 C=CCO[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL184441 66229 None 0 Rat Binding pKi = 8.2 8.2 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 259 5 3 4 -0.2 C=CCO[C@@H]1C[C@@H]2[C@H]([C@]1(N)C(=O)O)[C@@]2(F)C(=O)O 10.1021/jm0400294
49801368 159752 None 0 Human Binding pKi = 8.2 8.2 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 442 5 0 5 6.0 Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)ccn1 10.1021/acs.jmedchem.7b00669
CHEMBL4103808 159752 None 0 Human Binding pKi = 8.2 8.2 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 442 5 0 5 6.0 Cc1cc(Oc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2F)ccn1 10.1021/acs.jmedchem.7b00669
11347391 66873 None 0 Rat Binding pKi = 8.2 8.2 2 2
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 309 5 3 4 0.8 N[C@@]1(C(=O)O)[C@H](OCc2ccccc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL186214 66873 None 0 Rat Binding pKi = 8.2 8.2 2 2
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 309 5 3 4 0.8 N[C@@]1(C(=O)O)[C@H](OCc2ccccc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
11258119 67341 None 0 Rat Binding pKi = 8.2 8.2 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 401 7 3 5 2.6 N[C@@]1(C(=O)O)[C@H](OCc2cccc(Oc3ccccc3)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL188425 67341 None 0 Rat Binding pKi = 8.2 8.2 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 401 7 3 5 2.6 N[C@@]1(C(=O)O)[C@H](OCc2cccc(Oc3ccccc3)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
66785393 156986 None 0 Human Binding pKi = 8.1 8.1 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 419 7 1 6 5.0 COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2)cn1 10.1021/acs.jmedchem.7b00669
CHEMBL4072134 156986 None 0 Human Binding pKi = 8.1 8.1 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 419 7 1 6 5.0 COc1ccc(CNc2ccc(-c3ccn4c(CC5CC5)nnc4c3Cl)cc2)cn1 10.1021/acs.jmedchem.7b00669
67705089 152344 None 0 Human Binding pKi = 8.1 8.1 -2 2
Displacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting methodDisplacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting method
ChEMBL 458 7 4 7 1.9 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@@H](Sc2nc[nH]n2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1016/j.bmcl.2016.10.067
CHEMBL3969063 152344 None 0 Human Binding pKi = 8.1 8.1 -2 2
Displacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting methodDisplacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting method
ChEMBL 458 7 4 7 1.9 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@@H](Sc2nc[nH]n2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1016/j.bmcl.2016.10.067
49822115 2146 None 24 Human Binding pKi = 8.1 8.1 - 1
Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting method
ChEMBL 414 5 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.8b00051
8947 2146 None 24 Human Binding pKi = 8.1 8.1 - 1
Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting method
ChEMBL 414 5 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.8b00051
CHEMBL3947764 2146 None 24 Human Binding pKi = 8.1 8.1 - 1
Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes after 1 hr by microbeta scintillation counting method
ChEMBL 414 5 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.8b00051
49822115 2146 None 24 Human Binding pKi = 8.1 8.1 - 1
Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting method
ChEMBL 414 5 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.8b00051
8947 2146 None 24 Human Binding pKi = 8.1 8.1 - 1
Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting method
ChEMBL 414 5 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.8b00051
CHEMBL3947764 2146 None 24 Human Binding pKi = 8.1 8.1 - 1
Displacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting methodDisplacement of [3H]JNJ-46281222 from human mGlu2 receptor expressed in CHOK1 cell membranes preincubated for 3 hrs followed by [3H]JNJ-46281222 addition and measured after 1 hr by microbeta scintillation counting method
ChEMBL 414 5 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F 10.1021/acs.jmedchem.8b00051
11772601 127575 None 0 Rat Binding pKi = 8.1 8.1 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 354 6 3 6 0.7 N[C@@]1(C(=O)O)[C@H](OCc2cccc([N+](=O)[O-])c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL366152 127575 None 0 Rat Binding pKi = 8.1 8.1 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 354 6 3 6 0.7 N[C@@]1(C(=O)O)[C@H](OCc2cccc([N+](=O)[O-])c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
49801369 158841 None 0 Human Binding pKi = 8.1 8.1 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 450 4 0 5 6.1 Cc1ccc(Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
CHEMBL4093792 158841 None 0 Human Binding pKi = 8.1 8.1 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 450 4 0 5 6.1 Cc1ccc(Oc2ccc(-c3ccn4c(CC(F)(F)F)nnc4c3Cl)cc2F)c(C)n1 10.1021/acs.jmedchem.7b00669
15392101 100493 None 0 Rat Binding pKi = 5.2 5.2 - 1
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 517 7 0 7 5.8 COc1ccc(C2C(C(=O)OCCN(C)C)=C(C)N=C3SC(c4c(Cl)cccc4Cl)=CN32)cc1 10.1016/s0960-894x(99)00227-9
CHEMBL290509 100493 None 0 Rat Binding pKi = 5.2 5.2 - 1
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 517 7 0 7 5.8 COc1ccc(C2C(C(=O)OCCN(C)C)=C(C)N=C3SC(c4c(Cl)cccc4Cl)=CN32)cc1 10.1016/s0960-894x(99)00227-9
1393 1539 None 42 Human Binding pKi = 7.1 7.1 -2 6
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/acs.jmedchem.5b01124
1396 1539 None 42 Human Binding pKi = 7.1 7.1 -2 6
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/acs.jmedchem.5b01124
213056 1539 None 42 Human Binding pKi = 7.1 7.1 -2 6
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/acs.jmedchem.5b01124
CHEMBL8759 1539 None 42 Human Binding pKi = 7.1 7.1 -2 6
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/acs.jmedchem.5b01124
1393 1539 None 42 Human Binding pKi = 7.1 7.1 -2 6
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/acs.jmedchem.7b01481
1396 1539 None 42 Human Binding pKi = 7.1 7.1 -2 6
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/acs.jmedchem.7b01481
213056 1539 None 42 Human Binding pKi = 7.1 7.1 -2 6
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/acs.jmedchem.7b01481
CHEMBL8759 1539 None 42 Human Binding pKi = 7.1 7.1 -2 6
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/acs.jmedchem.7b01481
162654849 183776 None 0 Human Binding pKi = 6.1 6.1 -1 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 341 5 4 5 0.6 N[C@@]1(C(=O)O)[C@H](CSc2ccccc2F)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4755204 183776 None 0 Human Binding pKi = 6.1 6.1 -1 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 341 5 4 5 0.6 N[C@@]1(C(=O)O)[C@H](CSc2ccccc2F)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4802906 183776 None 0 Human Binding pKi = 6.1 6.1 -1 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 341 5 4 5 0.6 N[C@@]1(C(=O)O)[C@H](CSc2ccccc2F)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
1393 1539 None 42 Human Binding pKi = 7.1 7.1 -2 6
Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm040222y
1396 1539 None 42 Human Binding pKi = 7.1 7.1 -2 6
Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm040222y
213056 1539 None 42 Human Binding pKi = 7.1 7.1 -2 6
Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm040222y
CHEMBL8759 1539 None 42 Human Binding pKi = 7.1 7.1 -2 6
Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm040222y
1393 1539 None 42 Human Binding pKi = 7.1 7.1 -2 6
Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm980616n
1396 1539 None 42 Human Binding pKi = 7.1 7.1 -2 6
Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm980616n
213056 1539 None 42 Human Binding pKi = 7.1 7.1 -2 6
Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm980616n
CHEMBL8759 1539 None 42 Human Binding pKi = 7.1 7.1 -2 6
Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm980616n
1393 1539 None 42 Human Binding pKi = 7.1 7.1 -2 6
Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm060917u
1396 1539 None 42 Human Binding pKi = 7.1 7.1 -2 6
Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm060917u
213056 1539 None 42 Human Binding pKi = 7.1 7.1 -2 6
Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm060917u
CHEMBL8759 1539 None 42 Human Binding pKi = 7.1 7.1 -2 6
Displacement of [3H]LY341495 from human recombinant mGluR2 in RGT cellsDisplacement of [3H]LY341495 from human recombinant mGluR2 in RGT cells
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm060917u
134132133 144877 None 0 Human Binding pKi = 7.1 7.1 - 1
Displacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting methodDisplacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting method
ChEMBL 375 5 4 5 1.0 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1016/j.bmcl.2016.10.067
CHEMBL3909237 144877 None 0 Human Binding pKi = 7.1 7.1 - 1
Displacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting methodDisplacement of [3H]-LY459477 from human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing human EAAT1 after 90 mins by liquid scintillation counting method
ChEMBL 375 5 4 5 1.0 N[C@@]1(C(=O)O)[C@H](OCc2ccc(Cl)c(Cl)c2)[C@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1016/j.bmcl.2016.10.067
44595851 3802 None 6 Human Binding pKi = 7.1 7.1 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method
ChEMBL 475 8 2 6 4.5 Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C 10.1021/acs.jmedchem.7b00669
6259 3802 None 6 Human Binding pKi = 7.1 7.1 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method
ChEMBL 475 8 2 6 4.5 Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C 10.1021/acs.jmedchem.7b00669
CHEMBL4092105 3802 None 6 Human Binding pKi = 7.1 7.1 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting methodDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by liquid scintillation counting method
ChEMBL 475 8 2 6 4.5 Cn1cnc(c1)C(=O)NCc1ccc(cc1)COc1ccc(c(c1C(F)(F)F)O)C(=O)C(C)C 10.1021/acs.jmedchem.7b00669
67633284 183753 None 0 Human Binding pKi = 8.1 8.1 1 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 391 5 4 5 1.8 N[C@@]1(C(=O)O)[C@H](CSc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4748699 183753 None 0 Human Binding pKi = 8.1 8.1 1 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 391 5 4 5 1.8 N[C@@]1(C(=O)O)[C@H](CSc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
CHEMBL4802655 183753 None 0 Human Binding pKi = 8.1 8.1 1 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 391 5 4 5 1.8 N[C@@]1(C(=O)O)[C@H](CSc2ccc(Cl)c(Cl)c2)[C@@H](O)[C@@H]2[C@H]1[C@H]2C(=O)O 10.1021/acs.jmedchem.6b01119
90098428 123472 None 0 Human Binding pKi = 8.1 8.1 5 2
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 352 4 4 6 0.4 N[C@@]1(C(=O)O)C[C@H](Sc2nnc(C(F)(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616856 123472 None 0 Human Binding pKi = 8.1 8.1 5 2
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 352 4 4 6 0.4 N[C@@]1(C(=O)O)C[C@H](Sc2nnc(C(F)(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
11449064 124461 None 0 Rat Binding pKi = 8.1 8.1 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 287 4 3 4 0.5 N[C@@]1(C(=O)O)[C@H](OC2CCCC2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL363940 124461 None 0 Rat Binding pKi = 8.1 8.1 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 287 4 3 4 0.5 N[C@@]1(C(=O)O)[C@H](OC2CCCC2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
137652320 157366 None 0 Human Binding pKi = 8.1 8.1 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 454 7 0 6 5.4 COc1ccc(COc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2)cn1 10.1021/acs.jmedchem.7b00669
CHEMBL4076786 157366 None 0 Human Binding pKi = 8.1 8.1 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 454 7 0 6 5.4 COc1ccc(COc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2)cn1 10.1021/acs.jmedchem.7b00669
11267024 66680 None 0 Rat Binding pKi = 8.1 8.1 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 315 5 3 5 0.9 N[C@@]1(C(=O)O)[C@H](OCc2cccs2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL185335 66680 None 0 Rat Binding pKi = 8.1 8.1 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 315 5 3 5 0.9 N[C@@]1(C(=O)O)[C@H](OCc2cccs2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
67633340 183827 None 0 Human Binding pKi = 8.1 8.1 -1 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 355 5 4 5 0.9 Cc1cc(SC[C@@H]2[C@@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)ccc1F 10.1021/acs.jmedchem.6b01119
CHEMBL4780402 183827 None 0 Human Binding pKi = 8.1 8.1 -1 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 355 5 4 5 0.9 Cc1cc(SC[C@@H]2[C@@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)ccc1F 10.1021/acs.jmedchem.6b01119
CHEMBL4803381 183827 None 0 Human Binding pKi = 8.1 8.1 -1 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 355 5 4 5 0.9 Cc1cc(SC[C@@H]2[C@@H](O)[C@@H]3[C@@H]([C@H]3C(=O)O)[C@]2(N)C(=O)O)ccc1F 10.1021/acs.jmedchem.6b01119
66784262 158323 None 0 Human Binding pKi = 8.1 8.1 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 392 5 1 4 5.3 CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1F 10.1021/acs.jmedchem.7b00669
CHEMBL4088239 158323 None 0 Human Binding pKi = 8.1 8.1 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 392 5 1 4 5.3 CC(C)Nc1ccc(-c2ccn3c(CC4CC4)nnc3c2C(F)(F)F)cc1F 10.1021/acs.jmedchem.7b00669
49858118 1110 None 0 Human Binding pKi = 6.1 6.1 - 1
Binding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assayBinding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assay
ChEMBL 324 3 2 5 2.7 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)OC 10.1021/jm101069m
6224 1110 None 0 Human Binding pKi = 6.1 6.1 - 1
Binding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assayBinding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assay
ChEMBL 324 3 2 5 2.7 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)OC 10.1021/jm101069m
CHEMBL1630807 1110 None 0 Human Binding pKi = 6.1 6.1 - 1
Binding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assayBinding affinity to GFP tagged human mGluR2 containing truncated N-terminal region expressed in HEK cells by FRET assay
ChEMBL 324 3 2 5 2.7 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)OC 10.1021/jm101069m
15518718 100277 None 0 Rat Binding pKi = 5.1 5.1 - 1
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 501 6 0 6 6.1 CC1=C(C(=O)OCCN(C)C)C(c2ccccc2C)N2C=C(c3c(Cl)cccc3Cl)SC2=N1 10.1016/s0960-894x(99)00227-9
CHEMBL288472 100277 None 0 Rat Binding pKi = 5.1 5.1 - 1
Inhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cellsInhibition of 1S,3R-ACPD (10 uM) -stimulated GTP gamma 35S binding on rat Metabotropic glutamate receptor 2 transfected in CHO cells
ChEMBL 501 6 0 6 6.1 CC1=C(C(=O)OCCN(C)C)C(c2ccccc2C)N2C=C(c3c(Cl)cccc3Cl)SC2=N1 10.1016/s0960-894x(99)00227-9
10198133 208966 None 10 Human Binding pKi = 6.1 6.1 -6 2
Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.
ChEMBL 203 2 3 4 -0.8 N[C@@]1(C(=O)O)CS[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm980616n
CHEMBL8839 208966 None 10 Human Binding pKi = 6.1 6.1 -6 2
Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.Ability to displace [3H]LY-341,495 from recombinant human Metabotropic glutamate receptor 2 subtypes expressed in RGT cells.
ChEMBL 203 2 3 4 -0.8 N[C@@]1(C(=O)O)CS[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/jm980616n
71137010 123465 None 0 Human Binding pKi = 7.1 7.1 -1 2
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 352 4 4 6 0.4 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc(C(F)(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616849 123465 None 0 Human Binding pKi = 7.1 7.1 -1 2
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 352 4 4 6 0.4 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc(C(F)(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
1393 1539 None 42 Human Binding pKi = 7.1 7.1 -2 6
Inhibition of [3H]LY-341,495 binding to recombinant human mGlu2 receptorsInhibition of [3H]LY-341,495 binding to recombinant human mGlu2 receptors
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm050235r
1396 1539 None 42 Human Binding pKi = 7.1 7.1 -2 6
Inhibition of [3H]LY-341,495 binding to recombinant human mGlu2 receptorsInhibition of [3H]LY-341,495 binding to recombinant human mGlu2 receptors
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm050235r
213056 1539 None 42 Human Binding pKi = 7.1 7.1 -2 6
Inhibition of [3H]LY-341,495 binding to recombinant human mGlu2 receptorsInhibition of [3H]LY-341,495 binding to recombinant human mGlu2 receptors
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm050235r
CHEMBL8759 1539 None 42 Human Binding pKi = 7.1 7.1 -2 6
Inhibition of [3H]LY-341,495 binding to recombinant human mGlu2 receptorsInhibition of [3H]LY-341,495 binding to recombinant human mGlu2 receptors
ChEMBL 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10.1021/jm050235r
9885546 110601 None 0 Human Binding pKi = 7.1 7.1 - 1
Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2
ChEMBL 367 6 3 4 3.1 NC(C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1CCC1c2ccccc2Oc2ccccc21 10.1016/s0960-894x(01)00656-4
CHEMBL325140 110601 None 0 Human Binding pKi = 7.1 7.1 - 1
Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2Antagonistic activity against stimulation of GTP (gamma) 35 S binding by glutamate in membranes from CHO cells expressing human Metabotropic glutamate receptor 2
ChEMBL 367 6 3 4 3.1 NC(C(=O)O)[C@@H]1[C@@H](C(=O)O)[C@@H]1CCC1c2ccccc2Oc2ccccc21 10.1016/s0960-894x(01)00656-4
60096178 156973 None 0 Human Binding pKi = 7.1 7.1 -181 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 338 4 4 4 0.6 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2cccc(Cl)c2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
CHEMBL4071962 156973 None 0 Human Binding pKi = 7.1 7.1 -181 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 338 4 4 4 0.6 N[C@@]1(C(=O)O)C[C@H](NC(=O)c2cccc(Cl)c2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.7b01481
60096211 90093 None 0 Human Binding pKi = 6.1 6.1 -5 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 242 3 4 4 -1.4 CC(=O)N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/acs.jmedchem.7b01481
CHEMBL2381649 90093 None 0 Human Binding pKi = 6.1 6.1 -5 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation countingDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in HEK cell membranes after 90 mins by liquid scintillation counting
ChEMBL 242 3 4 4 -1.4 CC(=O)N[C@H]1C[C@@](N)(C(=O)O)[C@@H]2[C@@H](C(=O)O)[C@H]12 10.1021/acs.jmedchem.7b01481
69669820 183746 None 0 Human Binding pKi = 8.0 8.0 -1 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 396 6 4 5 1.1 CC(=O)N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1CSc1ccc(F)c(C)c1 10.1021/acs.jmedchem.6b01119
CHEMBL4746125 183746 None 0 Human Binding pKi = 8.0 8.0 -1 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 396 6 4 5 1.1 CC(=O)N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1CSc1ccc(F)c(C)c1 10.1021/acs.jmedchem.6b01119
CHEMBL4802570 183746 None 0 Human Binding pKi = 8.0 8.0 -1 2
Displacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation methodDisplacement of [3H]-LY459477 from recombinant human mGlu2 receptor expressed in hamster AV12 cell membranes co-expressing rat EAAT1 incubated for 90 mins by top count scintillation method
ChEMBL 396 6 4 5 1.1 CC(=O)N[C@H]1[C@H]2[C@H](C(=O)O)[C@H]2[C@](N)(C(=O)O)[C@@H]1CSc1ccc(F)c(C)c1 10.1021/acs.jmedchem.6b01119
66786493 157352 None 0 Human Binding pKi = 8.0 8.0 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 464 5 2 5 5.7 O[C@H]1CC[C@@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
CHEMBL4076639 157352 None 0 Human Binding pKi = 8.0 8.0 - 1
Displacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysisDisplacement of [3H]-JNJ46281222 from human metabotropic glutamate receptor 2 expressed in CHOK1 cell membranes after 60 mins by microbeta counting analysis
ChEMBL 464 5 2 5 5.7 O[C@H]1CC[C@@H](Nc2ccc(-c3ccn4c(CC5CC5)nnc4c3C(F)(F)F)cc2Cl)CC1 10.1021/acs.jmedchem.7b00669
11749463 66243 None 0 Rat Binding pKi = 8.0 8.0 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 385 6 3 4 2.5 N[C@@]1(C(=O)O)[C@H](OCc2cccc(-c3ccccc3)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL184504 66243 None 0 Rat Binding pKi = 8.0 8.0 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 385 6 3 4 2.5 N[C@@]1(C(=O)O)[C@H](OCc2cccc(-c3ccccc3)c2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
11209918 66874 None 0 Rat Binding pKi = 8.0 8.0 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 337 7 3 4 1.2 N[C@@]1(C(=O)O)[C@H](OCCCc2ccccc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
CHEMBL186215 66874 None 0 Rat Binding pKi = 8.0 8.0 - 1
Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008Binding affinity towards metabotropic glutamate receptor 2 of rat expressed in CHO cells was determined by using [3H]MGS-0008
ChEMBL 337 7 3 4 1.2 N[C@@]1(C(=O)O)[C@H](OCCCc2ccccc2)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 10.1021/jm0400294
71137034 123466 None 0 Human Binding pKi = 7.0 7.0 -1 2
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 334 5 4 6 0.3 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc(C(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
CHEMBL3616850 123466 None 0 Human Binding pKi = 7.0 7.0 -1 2
Displacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation countingDisplacement of [3H]-459477 from human recombinant mGlu2 receptor expressed in AV12 cells after 90 mins by liquid scintillation counting
ChEMBL 334 5 4 6 0.3 N[C@@]1(C(=O)O)C[C@@H](Sc2nnc(C(F)F)[nH]2)[C@H]2[C@H](C(=O)O)[C@H]21 10.1021/acs.jmedchem.5b01124
11298568 69397 None 1 Human Binding pKi = 6.0 6.0 -6 2
Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2
ChEMBL 199 2 3 3 -0.2 C[C@@H]1C[C@H]2[C@H](C(=O)O)[C@H]2[C@]1(N)C(=O)O 10.1021/jm040222y
CHEMBL192977 69397 None 1 Human Binding pKi = 6.0 6.0 -6 2
Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2Displacement of [3H]-341495 binding to membranes expressing recombinant human Metabotropic glutamate receptor 2
ChEMBL 199 2 3 3 -0.2 C[C@@H]1C[C@H]2[C@H](C(=O)O)[C@H]2[C@]1(N)C(=O)O 10.1021/jm040222y
49822115 2146 None 24 Human Binding pKd = 8.8 8.8 - 1
Saturation binding experiment using tritiated compound, and membranes from CHO-K1 cells stably expressing the human mGlu<sub>2</sub> receptor.Saturation binding experiment using tritiated compound, and membranes from CHO-K1 cells stably expressing the human mGlu<sub>2</sub> receptor.
Guide to Pharmacology 414 5 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F 26589404
8947 2146 None 24 Human Binding pKd = 8.8 8.8 - 1
Saturation binding experiment using tritiated compound, and membranes from CHO-K1 cells stably expressing the human mGlu<sub>2</sub> receptor.Saturation binding experiment using tritiated compound, and membranes from CHO-K1 cells stably expressing the human mGlu<sub>2</sub> receptor.
Guide to Pharmacology 414 5 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F 26589404
CHEMBL3947764 2146 None 24 Human Binding pKd = 8.8 8.8 - 1
Saturation binding experiment using tritiated compound, and membranes from CHO-K1 cells stably expressing the human mGlu<sub>2</sub> receptor.Saturation binding experiment using tritiated compound, and membranes from CHO-K1 cells stably expressing the human mGlu<sub>2</sub> receptor.
Guide to Pharmacology 414 5 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F 26589404
59234231 2143 None 4 Human Binding pKd = 7.9 7.9 -2 2
UnclassifiedUnclassified
Guide to Pharmacology 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 23766542
6330 2143 None 4 Human Binding pKd = 7.9 7.9 -2 2
UnclassifiedUnclassified
Guide to Pharmacology 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 23766542
6331 2143 None 4 Human Binding pKd = 7.9 7.9 -2 2
UnclassifiedUnclassified
Guide to Pharmacology 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 23766542
CHEMBL3337510 2143 None 4 Human Binding pKd = 7.9 7.9 -2 2
UnclassifiedUnclassified
Guide to Pharmacology 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 23766542
59234231 2143 None 4 Rat Binding pKd = 8 8.0 2 2
UnclassifiedUnclassified
Guide to Pharmacology 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 23766542
6330 2143 None 4 Rat Binding pKd = 8 8.0 2 2
UnclassifiedUnclassified
Guide to Pharmacology 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 23766542
6331 2143 None 4 Rat Binding pKd = 8 8.0 2 2
UnclassifiedUnclassified
Guide to Pharmacology 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 23766542
CHEMBL3337510 2143 None 4 Rat Binding pKd = 8 8.0 2 2
UnclassifiedUnclassified
Guide to Pharmacology 333 4 0 4 3.5 N#Cc1c(ccn(c1=O)CC1CC1)N1CCC(CC1)c1ccccc1 23766542
11362035 42 None 1 Rat Binding pKd = 8.4 8.4 - 1
UnclassifiedUnclassified
Guide to Pharmacology 416 9 0 4 4.5 CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C 21470207
6328 42 None 1 Rat Binding pKd = 8.4 8.4 - 1
UnclassifiedUnclassified
Guide to Pharmacology 416 9 0 4 4.5 CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C 21470207
6329 42 None 1 Rat Binding pKd = 8.4 8.4 - 1
UnclassifiedUnclassified
Guide to Pharmacology 416 9 0 4 4.5 CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C 21470207
CHEMBL105296 42 None 1 Rat Binding pKd = 8.4 8.4 - 1
UnclassifiedUnclassified
Guide to Pharmacology 416 9 0 4 4.5 CCCC(Oc1cccc(c1)N(S(=O)(=O)CC(F)(F)F)Cc1cccnc1)C 21470207
1393 1539 None 42 Rat Binding pKd None 7.7 7.7 1 6
UnclassifiedUnclassified
Guide to Pharmacology 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10884552
1396 1539 None 42 Rat Binding pKd None 7.7 7.7 1 6
UnclassifiedUnclassified
Guide to Pharmacology 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10884552
213056 1539 None 42 Rat Binding pKd None 7.7 7.7 1 6
UnclassifiedUnclassified
Guide to Pharmacology 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10884552
CHEMBL8759 1539 None 42 Rat Binding pKd None 7.7 7.7 1 6
UnclassifiedUnclassified
Guide to Pharmacology 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10884552
1378 2417 None 39 Human Binding pKd None 8.8 8.8 -2 10
UnclassifiedUnclassified
Guide to Pharmacology 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10530814
1399 2417 None 39 Human Binding pKd None 8.8 8.8 -2 10
UnclassifiedUnclassified
Guide to Pharmacology 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10530814
9819927 2417 None 39 Human Binding pKd None 8.8 8.8 -2 10
UnclassifiedUnclassified
Guide to Pharmacology 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10530814
CHEMBL432038 2417 None 39 Human Binding pKd None 8.8 8.8 -2 10
UnclassifiedUnclassified
Guide to Pharmacology 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10530814
None 218820 3H-LY354740 0 Rat Binding pKi = 8 8.0 - 1
NoneNone
PDSP KiDatabase 323 5 5 9 -1.3 C1C(C1C(CN2C=NC3=C2N=C(N=C3O)O)(C(=O)O)N)C(=O)O None
12310764 1970 Functional 46 Human Binding pKi = 5 5.0 -14 8
NoneNone
PDSP KiDatabase 158 2 3 4 -0.9 OC(=O)C(c1o[nH]c(=O)c1)N None
12310764 1970 3H-LY354740 46 Rat Binding pKi = 5 5.0 -14 8
NoneNone
PDSP KiDatabase 158 2 3 4 -0.9 OC(=O)C(c1o[nH]c(=O)c1)N None
12310764 1970 Functional 46 Rat Binding pKi = 5 5.0 -14 8
NoneNone
PDSP KiDatabase 158 2 3 4 -0.9 OC(=O)C(c1o[nH]c(=O)c1)N None
1233 1970 Functional 46 Human Binding pKi = 5 5.0 -14 8
NoneNone
PDSP KiDatabase 158 2 3 4 -0.9 OC(=O)C(c1o[nH]c(=O)c1)N None
1233 1970 3H-LY354740 46 Rat Binding pKi = 5 5.0 -14 8
NoneNone
PDSP KiDatabase 158 2 3 4 -0.9 OC(=O)C(c1o[nH]c(=O)c1)N None
1233 1970 Functional 46 Rat Binding pKi = 5 5.0 -14 8
NoneNone
PDSP KiDatabase 158 2 3 4 -0.9 OC(=O)C(c1o[nH]c(=O)c1)N None
1371 1970 Functional 46 Human Binding pKi = 5 5.0 -14 8
NoneNone
PDSP KiDatabase 158 2 3 4 -0.9 OC(=O)C(c1o[nH]c(=O)c1)N None
1371 1970 3H-LY354740 46 Rat Binding pKi = 5 5.0 -14 8
NoneNone
PDSP KiDatabase 158 2 3 4 -0.9 OC(=O)C(c1o[nH]c(=O)c1)N None
1371 1970 Functional 46 Rat Binding pKi = 5 5.0 -14 8
NoneNone
PDSP KiDatabase 158 2 3 4 -0.9 OC(=O)C(c1o[nH]c(=O)c1)N None
CHEMBL284895 1970 Functional 46 Human Binding pKi = 5 5.0 -14 8
NoneNone
PDSP KiDatabase 158 2 3 4 -0.9 OC(=O)C(c1o[nH]c(=O)c1)N None
CHEMBL284895 1970 3H-LY354740 46 Rat Binding pKi = 5 5.0 -14 8
NoneNone
PDSP KiDatabase 158 2 3 4 -0.9 OC(=O)C(c1o[nH]c(=O)c1)N None
CHEMBL284895 1970 Functional 46 Rat Binding pKi = 5 5.0 -14 8
NoneNone
PDSP KiDatabase 158 2 3 4 -0.9 OC(=O)C(c1o[nH]c(=O)c1)N None
1310 2315 Functional 61 Rat Binding pKi = 5 5.0 -13 18
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
1369 2315 Functional 61 Rat Binding pKi = 5 5.0 -13 18
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
33032 2315 Functional 61 Rat Binding pKi = 5 5.0 -13 18
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
44272391 2315 Functional 61 Rat Binding pKi = 5 5.0 -13 18
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
88747398 2315 Functional 61 Rat Binding pKi = 5 5.0 -13 18
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
CHEMBL575060 2315 Functional 61 Rat Binding pKi = 5 5.0 -13 18
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
DB00142 2315 Functional 61 Rat Binding pKi = 5 5.0 -13 18
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
134 2514 Functional 19 Rat Binding pKi = 5 5.0 -8511 67
NoneNone
PDSP KiDatabase 353 4 2 4 1.9 CC[C@H](NC(=O)[C@H]1CN(C)[C@H]2C(=C1)c1cccc3c1c(C2)cn3C)CO None
1775 2514 Functional 19 Rat Binding pKi = 5 5.0 -8511 67
NoneNone
PDSP KiDatabase 353 4 2 4 1.9 CC[C@H](NC(=O)[C@H]1CN(C)[C@H]2C(=C1)c1cccc3c1c(C2)cn3C)CO None
9681 2514 Functional 19 Rat Binding pKi = 5 5.0 -8511 67
NoneNone
PDSP KiDatabase 353 4 2 4 1.9 CC[C@H](NC(=O)[C@H]1CN(C)[C@H]2C(=C1)c1cccc3c1c(C2)cn3C)CO None
9681.0 2514 Functional 19 Rat Binding pKi = 5 5.0 -8511 67
NoneNone
PDSP KiDatabase 353 4 2 4 1.9 CC[C@H](NC(=O)[C@H]1CN(C)[C@H]2C(=C1)c1cccc3c1c(C2)cn3C)CO None
CHEMBL1065 2514 Functional 19 Rat Binding pKi = 5 5.0 -8511 67
NoneNone
PDSP KiDatabase 353 4 2 4 1.9 CC[C@H](NC(=O)[C@H]1CN(C)[C@H]2C(=C1)c1cccc3c1c(C2)cn3C)CO None
DB00247 2514 Functional 19 Rat Binding pKi = 5 5.0 -8511 67
NoneNone
PDSP KiDatabase 353 4 2 4 1.9 CC[C@H](NC(=O)[C@H]1CN(C)[C@H]2C(=C1)c1cccc3c1c(C2)cn3C)CO None
15897 2862 Functional 0 Rat Binding pKi = 5 5.0 -354 36
NoneNone
PDSP KiDatabase 203 2 1 1 2.6 CC(Cc1cccc(c1)C(F)(F)F)N None
215 2862 Functional 0 Rat Binding pKi = 5 5.0 -354 36
NoneNone
PDSP KiDatabase 203 2 1 1 2.6 CC(Cc1cccc(c1)C(F)(F)F)N None
CHEMBL1979333 2862 Functional 0 Rat Binding pKi = 5 5.0 -354 36
NoneNone
PDSP KiDatabase 203 2 1 1 2.6 CC(Cc1cccc(c1)C(F)(F)F)N None
1370 3263 Functional 42 Human Binding pKi = 5 5.0 -602 8
NoneNone
PDSP KiDatabase 189 3 3 6 -2.5 OC(=O)[C@H](Cn1oc(=O)[nH]c1=O)N None
1370 3263 3H-LY354740 42 Rat Binding pKi = 5 5.0 -602 8
NoneNone
PDSP KiDatabase 189 3 3 6 -2.5 OC(=O)[C@H](Cn1oc(=O)[nH]c1=O)N None
1372 3263 Functional 42 Human Binding pKi = 5 5.0 -602 8
NoneNone
PDSP KiDatabase 189 3 3 6 -2.5 OC(=O)[C@H](Cn1oc(=O)[nH]c1=O)N None
1372 3263 3H-LY354740 42 Rat Binding pKi = 5 5.0 -602 8
NoneNone
PDSP KiDatabase 189 3 3 6 -2.5 OC(=O)[C@H](Cn1oc(=O)[nH]c1=O)N None
40539 3263 Functional 42 Human Binding pKi = 5 5.0 -602 8
NoneNone
PDSP KiDatabase 189 3 3 6 -2.5 OC(=O)[C@H](Cn1oc(=O)[nH]c1=O)N None
40539 3263 3H-LY354740 42 Rat Binding pKi = 5 5.0 -602 8
NoneNone
PDSP KiDatabase 189 3 3 6 -2.5 OC(=O)[C@H](Cn1oc(=O)[nH]c1=O)N None
6971145 3263 Functional 42 Human Binding pKi = 5 5.0 -602 8
NoneNone
PDSP KiDatabase 189 3 3 6 -2.5 OC(=O)[C@H](Cn1oc(=O)[nH]c1=O)N None
6971145 3263 3H-LY354740 42 Rat Binding pKi = 5 5.0 -602 8
NoneNone
PDSP KiDatabase 189 3 3 6 -2.5 OC(=O)[C@H](Cn1oc(=O)[nH]c1=O)N None
CHEMBL279956 3263 Functional 42 Human Binding pKi = 5 5.0 -602 8
NoneNone
PDSP KiDatabase 189 3 3 6 -2.5 OC(=O)[C@H](Cn1oc(=O)[nH]c1=O)N None
CHEMBL279956 3263 3H-LY354740 42 Rat Binding pKi = 5 5.0 -602 8
NoneNone
PDSP KiDatabase 189 3 3 6 -2.5 OC(=O)[C@H](Cn1oc(=O)[nH]c1=O)N None
DB02999 3263 Functional 42 Human Binding pKi = 5 5.0 -602 8
NoneNone
PDSP KiDatabase 189 3 3 6 -2.5 OC(=O)[C@H](Cn1oc(=O)[nH]c1=O)N None
DB02999 3263 3H-LY354740 42 Rat Binding pKi = 5 5.0 -602 8
NoneNone
PDSP KiDatabase 189 3 3 6 -2.5 OC(=O)[C@H](Cn1oc(=O)[nH]c1=O)N None
128563 3464 Functional 24 Human Binding pKi = 5 5.0 -2344 41
NoneNone
PDSP KiDatabase 432 3 0 8 3.0 COC(=O)[C@@H]1C[C@H](OC(=O)C)C(=O)[C@H]2[C@@]1(C)CC[C@@H]1[C@]2(C)C[C@H](OC1=O)c1cocc1 None
1666 3464 Functional 24 Human Binding pKi = 5 5.0 -2344 41
NoneNone
PDSP KiDatabase 432 3 0 8 3.0 COC(=O)[C@@H]1C[C@H](OC(=O)C)C(=O)[C@H]2[C@@]1(C)CC[C@@H]1[C@]2(C)C[C@H](OC1=O)c1cocc1 None
CHEMBL445332 3464 Functional 24 Human Binding pKi = 5 5.0 -2344 41
NoneNone
PDSP KiDatabase 432 3 0 8 3.0 COC(=O)[C@@H]1C[C@H](OC(=O)C)C(=O)[C@H]2[C@@]1(C)CC[C@@H]1[C@]2(C)C[C@H](OC1=O)c1cocc1 None
DB12327 3464 Functional 24 Human Binding pKi = 5 5.0 -2344 41
NoneNone
PDSP KiDatabase 432 3 0 8 3.0 COC(=O)[C@@H]1C[C@H](OC(=O)C)C(=O)[C@H]2[C@@]1(C)CC[C@@H]1[C@]2(C)C[C@H](OC1=O)c1cocc1 None
10297 27120 Functional 13 Rat Binding pKi = 5 5.0 -38 42
NoneNone
PDSP KiDatabase 151 2 2 2 1.1 C[C@H](N)[C@H](O)c1ccccc1 None
CHEMBL136560 27120 Functional 13 Rat Binding pKi = 5 5.0 -38 42
NoneNone
PDSP KiDatabase 151 2 2 2 1.1 C[C@H](N)[C@H](O)c1ccccc1 None
2207 99919 3H-LY354740 47 Rat Binding pKi = 5 5.0 -25 7
NoneNone
PDSP KiDatabase 183 4 4 3 -1.0 NC(CCP(=O)(O)O)C(=O)O None
CHEMBL285843 99919 3H-LY354740 47 Rat Binding pKi = 5 5.0 -25 7
NoneNone
PDSP KiDatabase 183 4 4 3 -1.0 NC(CCP(=O)(O)O)C(=O)O None
1222 101792 Functional 46 Rat Binding pKi = 5 5.0 5 3
NoneNone
PDSP KiDatabase 209 3 3 3 0.6 CC(N)(C(=O)O)c1ccc(C(=O)O)cc1 None
CHEMBL299683 101792 Functional 46 Rat Binding pKi = 5 5.0 5 3
NoneNone
PDSP KiDatabase 209 3 3 3 0.6 CC(N)(C(=O)O)c1ccc(C(=O)O)cc1 None
5115 112110 Functional 33 Human Binding pKi = 5 5.0 1 5
NoneNone
PDSP KiDatabase 195 3 3 3 0.5 NC(C(=O)O)c1ccc(C(=O)O)cc1 None
5115 112110 3H-GLUTAMATE 33 Rat Binding pKi = 5 5.0 -1 5
NoneNone
PDSP KiDatabase 195 3 3 3 0.5 NC(C(=O)O)c1ccc(C(=O)O)cc1 None
5115 112110 Functional 33 Rat Binding pKi = 5 5.0 -1 5
NoneNone
PDSP KiDatabase 195 3 3 3 0.5 NC(C(=O)O)c1ccc(C(=O)O)cc1 None
CHEMBL328984 112110 Functional 33 Human Binding pKi = 5 5.0 1 5
NoneNone
PDSP KiDatabase 195 3 3 3 0.5 NC(C(=O)O)c1ccc(C(=O)O)cc1 None
CHEMBL328984 112110 3H-GLUTAMATE 33 Rat Binding pKi = 5 5.0 -1 5
NoneNone
PDSP KiDatabase 195 3 3 3 0.5 NC(C(=O)O)c1ccc(C(=O)O)cc1 None
CHEMBL328984 112110 Functional 33 Rat Binding pKi = 5 5.0 -1 5
NoneNone
PDSP KiDatabase 195 3 3 3 0.5 NC(C(=O)O)c1ccc(C(=O)O)cc1 None
446220 133590 Functional 7 Rat Binding pKi = 5 5.0 -1778 45
NoneNone
PDSP KiDatabase 303 3 0 5 1.9 COC(=O)[C@H]1[C@@H](OC(=O)c2ccccc2)C[C@@H]2CC[C@H]1N2C None
CHEMBL370805 133590 Functional 7 Rat Binding pKi = 5 5.0 -1778 45
NoneNone
PDSP KiDatabase 303 3 0 5 1.9 COC(=O)[C@H]1[C@@H](OC(=O)c2ccccc2)C[C@@H]2CC[C@H]1N2C None
19702198 161416 Functional 11 Human Binding pKi = 5 5.0 1 2
NoneNone
PDSP KiDatabase 173 3 3 3 -0.5 CC(N)(C(=O)O)C1CC1C(=O)O None
19702198 161416 3H-LY354740 11 Rat Binding pKi = 5 5.0 -1 2
NoneNone
PDSP KiDatabase 173 3 3 3 -0.5 CC(N)(C(=O)O)C1CC1C(=O)O None
19702198 161416 Functional 11 Rat Binding pKi = 5 5.0 -1 2
NoneNone
PDSP KiDatabase 173 3 3 3 -0.5 CC(N)(C(=O)O)C1CC1C(=O)O None
CHEMBL412445 161416 Functional 11 Human Binding pKi = 5 5.0 1 2
NoneNone
PDSP KiDatabase 173 3 3 3 -0.5 CC(N)(C(=O)O)C1CC1C(=O)O None
CHEMBL412445 161416 3H-LY354740 11 Rat Binding pKi = 5 5.0 -1 2
NoneNone
PDSP KiDatabase 173 3 3 3 -0.5 CC(N)(C(=O)O)C1CC1C(=O)O None
CHEMBL412445 161416 Functional 11 Rat Binding pKi = 5 5.0 -1 2
NoneNone
PDSP KiDatabase 173 3 3 3 -0.5 CC(N)(C(=O)O)C1CC1C(=O)O None
1615 167894 Functional 12 Rat Binding pKi = 5 5.0 -26 44
NoneNone
PDSP KiDatabase 193 3 1 3 1.6 CNC(C)Cc1ccc2c(c1)OCO2 None
CHEMBL43048 167894 Functional 12 Rat Binding pKi = 5 5.0 -26 44
NoneNone
PDSP KiDatabase 193 3 1 3 1.6 CNC(C)Cc1ccc2c(c1)OCO2 None
1297 170355 Functional 23 Human Binding pKi = 5 5.0 -1 4
NoneNone
PDSP KiDatabase 211 3 4 4 0.2 NC(C(=O)O)c1ccc(C(=O)O)c(O)c1 None
1297 170355 Functional 23 Rat Binding pKi = 5 5.0 -1 4
NoneNone
PDSP KiDatabase 211 3 4 4 0.2 NC(C(=O)O)c1ccc(C(=O)O)c(O)c1 None
CHEMBL444589 170355 Functional 23 Human Binding pKi = 5 5.0 -1 4
NoneNone
PDSP KiDatabase 211 3 4 4 0.2 NC(C(=O)O)c1ccc(C(=O)O)c(O)c1 None
CHEMBL444589 170355 Functional 23 Rat Binding pKi = 5 5.0 -1 4
NoneNone
PDSP KiDatabase 211 3 4 4 0.2 NC(C(=O)O)c1ccc(C(=O)O)c(O)c1 None
162265 204731 Functional 11 Rat Binding pKi = 5 5.0 -1949 44
NoneNone
PDSP KiDatabase 151 2 2 2 1.1 CC(N)C(O)c1ccccc1 None
4786 204731 Functional 11 Rat Binding pKi = 5 5.0 -1949 44
NoneNone
PDSP KiDatabase 151 2 2 2 1.1 CC(N)C(O)c1ccccc1 None
CHEMBL61006 204731 Functional 11 Rat Binding pKi = 5 5.0 -1949 44
NoneNone
PDSP KiDatabase 151 2 2 2 1.1 CC(N)C(O)c1ccccc1 None
139054390 207381 Functional 56 Human Binding pKi = 5 5.0 1 5
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 N[C@H](CCC(=O)O)C(=O)O None
139054390 207381 3H-LY354740 56 Rat Binding pKi = 5 5.0 -1 5
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 N[C@H](CCC(=O)O)C(=O)O None
139054390 207381 Functional 56 Rat Binding pKi = 5 5.0 -1 5
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 N[C@H](CCC(=O)O)C(=O)O None
23327 207381 Functional 56 Human Binding pKi = 5 5.0 1 5
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 N[C@H](CCC(=O)O)C(=O)O None
23327 207381 3H-LY354740 56 Rat Binding pKi = 5 5.0 -1 5
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 N[C@H](CCC(=O)O)C(=O)O None
23327 207381 Functional 56 Rat Binding pKi = 5 5.0 -1 5
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 N[C@H](CCC(=O)O)C(=O)O None
CHEMBL76232 207381 Functional 56 Human Binding pKi = 5 5.0 1 5
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 N[C@H](CCC(=O)O)C(=O)O None
CHEMBL76232 207381 3H-LY354740 56 Rat Binding pKi = 5 5.0 -1 5
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 N[C@H](CCC(=O)O)C(=O)O None
CHEMBL76232 207381 Functional 56 Rat Binding pKi = 5 5.0 -1 5
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 N[C@H](CCC(=O)O)C(=O)O None
3337 208825 Functional 14 Rat Binding pKi = 5 5.0 -1513 40
NoneNone
PDSP KiDatabase 231 4 1 1 3.2 CCNC(C)Cc1cccc(C(F)(F)F)c1 None
3337.0 208825 Functional 14 Rat Binding pKi = 5 5.0 -1513 40
NoneNone
PDSP KiDatabase 231 4 1 1 3.2 CCNC(C)Cc1cccc(C(F)(F)F)c1 None
65801 208825 Functional 14 Rat Binding pKi = 5 5.0 -1513 40
NoneNone
PDSP KiDatabase 231 4 1 1 3.2 CCNC(C)Cc1cccc(C(F)(F)F)c1 None
66264 208825 Functional 14 Rat Binding pKi = 5 5.0 -1513 40
NoneNone
PDSP KiDatabase 231 4 1 1 3.2 CCNC(C)Cc1cccc(C(F)(F)F)c1 None
91452 208825 Functional 14 Rat Binding pKi = 5 5.0 -1513 40
NoneNone
PDSP KiDatabase 231 4 1 1 3.2 CCNC(C)Cc1cccc(C(F)(F)F)c1 None
CHEMBL87493 208825 Functional 14 Rat Binding pKi = 5 5.0 -1513 40
NoneNone
PDSP KiDatabase 231 4 1 1 3.2 CCNC(C)Cc1cccc(C(F)(F)F)c1 None
DB00574 208825 Functional 14 Rat Binding pKi = 5 5.0 -1513 40
NoneNone
PDSP KiDatabase 231 4 1 1 3.2 CCNC(C)Cc1cccc(C(F)(F)F)c1 None
11954224 218443 Functional 0 Rat Binding pKi = 5 5.0 -141253 59
NoneNone
PDSP KiDatabase 581 4 3 6 2.0 CC1(C(=O)N2C(C(=O)N3CCCC3C2(O1)O)CC4=CC=CC=C4)NC(=O)C5CN(C6CC7=CNC8=CC=CC(=C78)C6=C5)C None
3251 218443 Functional 0 Rat Binding pKi = 5 5.0 -141253 59
NoneNone
PDSP KiDatabase 581 4 3 6 2.0 CC1(C(=O)N2C(C(=O)N3CCCC3C2(O1)O)CC4=CC=CC=C4)NC(=O)C5CN(C6CC7=CNC8=CC=CC(=C78)C6=C5)C None
3251.0 218443 Functional 0 Rat Binding pKi = 5 5.0 -141253 59
NoneNone
PDSP KiDatabase 581 4 3 6 2.0 CC1(C(=O)N2C(C(=O)N3CCCC3C2(O1)O)CC4=CC=CC=C4)NC(=O)C5CN(C6CC7=CNC8=CC=CC(=C78)C6=C5)C None
CHEMBL1982133 218443 Functional 0 Rat Binding pKi = 5 5.0 -141253 59
NoneNone
PDSP KiDatabase 581 4 3 6 2.0 CC1(C(=O)N2C(C(=O)N3CCCC3C2(O1)O)CC4=CC=CC=C4)NC(=O)C5CN(C6CC7=CNC8=CC=CC(=C78)C6=C5)C None
DB00696 218443 Functional 0 Rat Binding pKi = 5 5.0 -141253 59
NoneNone
PDSP KiDatabase 581 4 3 6 2.0 CC1(C(=O)N2C(C(=O)N3CCCC3C2(O1)O)CC4=CC=CC=C4)NC(=O)C5CN(C6CC7=CNC8=CC=CC(=C78)C6=C5)C None
6971132 218499 3H-LY341495 0 Human Binding pKi = 5 5.0 -2570 14
NoneNone
PDSP KiDatabase 268 1 2 2 2.1 CN1CC(C=C2C1CC3=CNC4=CC=CC2=C34)C(=O)O None
None 218660 Functional 0 Human Binding pKi = 5 5.0 -2 7
NoneNone
PDSP KiDatabase 173 2 3 3 -0.3 C1CC(CC1C(=O)O)(C(=O)O)N None
None 218660 Functional 0 Rat Binding pKi = 5 5.0 1 7
NoneNone
PDSP KiDatabase 173 2 3 3 -0.3 C1CC(CC1C(=O)O)(C(=O)O)N None
25137849 218667 Functional 0 Rat Binding pKi = 5 5.0 -4 40
NoneNone
PDSP KiDatabase 165 3 2 2 1.3 CC(C(C1=CC=CC=C1)O)NC None
71290 218667 Functional 0 Rat Binding pKi = 5 5.0 -4 40
NoneNone
PDSP KiDatabase 165 3 2 2 1.3 CC(C(C1=CC=CC=C1)O)NC None
None 218803 Functional 0 Rat Binding pKi = 5 5.0 -1 39
NoneNone
PDSP KiDatabase 153 3 3 3 -1.4 C(C(C(=O)O)N)S(=O)O None
None 218804 Functional 0 Rat Binding pKi = 5 5.0 -1 38
NoneNone
PDSP KiDatabase 169 3 3 4 -1.7 C(C(C(=O)O)N)S(=O)(=O)O None
None 218812 Functional 0 Rat Binding pKi = 5 5.0 -13 40
NoneNone
PDSP KiDatabase 149 2 1 2 1.2 CC(C(=O)C1=CC=CC=C1)N None
1576 218813 Functional 0 Rat Binding pKi = 5 5.0 -16 40
NoneNone
PDSP KiDatabase 163 3 1 2 1.5 CC(C(=O)C1=CC=CC=C1)NC None
177120 218823 3H-LY354740 0 Rat Binding pKi = 5 5.0 - 1
NoneNone
PDSP KiDatabase 169 3 4 3 -1.4 C(C(C(=O)O)N)P(=O)(O)O None
194385 218832 Functional 0 Human Binding pKi = 5 5.0 1 2
NoneNone
PDSP KiDatabase 172 3 3 4 -1.1 C1=C(ONC1=O)CC(C(=O)O)N None
194385 218832 Functional 0 Rat Binding pKi = 5 5.0 -1 2
NoneNone
PDSP KiDatabase 172 3 3 4 -1.1 C1=C(ONC1=O)CC(C(=O)O)N None
6604769 218849 Functional 0 Human Binding pKi = 5 5.0 1 2
NoneNone
PDSP KiDatabase 145 2 3 3 -1.1 C1C(NC1C(=O)O)C(=O)O None
6604769 218849 Functional 0 Rat Binding pKi = 5 5.0 -1 2
NoneNone
PDSP KiDatabase 145 2 3 3 -1.1 C1C(NC1C(=O)O)C(=O)O None
None 218850 Functional 0 Human Binding pKi = 5 5.0 1 3
NoneNone
PDSP KiDatabase 245 3 3 4 0.2 CC(C1=CC=C(C=C1)S(=O)(=O)O)(C(=O)O)N None
None 218850 Functional 0 Rat Binding pKi = 5 5.0 -1 3
NoneNone
PDSP KiDatabase 245 3 3 4 0.2 CC(C1=CC=C(C=C1)S(=O)(=O)O)(C(=O)O)N None
None 218851 Functional 0 Human Binding pKi = 5 5.0 1 2
NoneNone
PDSP KiDatabase 233 3 2 6 -0.1 CC(C1=CC=C(C=C1)N2C=NN=N2)(C(=O)O)N None
None 218851 Functional 0 Rat Binding pKi = 5 5.0 -1 2
NoneNone
PDSP KiDatabase 233 3 2 6 -0.1 CC(C1=CC=C(C=C1)N2C=NN=N2)(C(=O)O)N None
None 218852 Functional 0 Human Binding pKi = 5 5.0 1 3
NoneNone
PDSP KiDatabase 197 4 4 3 -0.6 CC(CCP(=O)(O)O)(C(=O)O)N None
None 218852 Functional 0 Rat Binding pKi = 5 5.0 -1 3
NoneNone
PDSP KiDatabase 197 4 4 3 -0.6 CC(CCP(=O)(O)O)(C(=O)O)N None
None 218887 Functional 0 Human Binding pKi = 5 5.0 - 1
NoneNone
PDSP KiDatabase 396 2 0 4 4.7 CC(=O)C1(C(=C)CC2C1(CCC3C2CC(=C)C4=CC(=O)CCC34C)C)OC(=O)C None
None 218896 Functional 0 Human Binding pKi = 5 5.0 1 2
NoneNone
PDSP KiDatabase 250 3 3 4 -0.3 C(C1=C(C(=O)NO1)Br)C(C(=O)O)N None
None 218896 Functional 0 Rat Binding pKi = 5 5.0 -1 2
NoneNone
PDSP KiDatabase 250 3 3 4 -0.3 C(C1=C(C(=O)NO1)Br)C(C(=O)O)N None
None 218976 Functional 0 Rat Binding pKi = 5 5.0 1 2
NoneNone
PDSP KiDatabase 144 2 2 2 -0.7 CC(C(=O)NC)NC(=O)C None
None 218977 Functional 0 Rat Binding pKi = 5 5.0 1 2
NoneNone
PDSP KiDatabase 161 5 3 3 -0.3 C(CC(C(=O)O)N)CC(=O)O None
1376 321 3H-M-MPEP 33 Rat Binding pKi = 6.0 6.0 91 2
NoneNone
PDSP KiDatabase 221 2 3 3 0.6 OC(=O)c1ccc2c(c1)CCC2(N)C(=O)O None
2071 321 3H-M-MPEP 33 Rat Binding pKi = 6.0 6.0 91 2
NoneNone
PDSP KiDatabase 221 2 3 3 0.6 OC(=O)c1ccc2c(c1)CCC2(N)C(=O)O None
CHEMBL313938 321 3H-M-MPEP 33 Rat Binding pKi = 6.0 6.0 91 2
NoneNone
PDSP KiDatabase 221 2 3 3 0.6 OC(=O)c1ccc2c(c1)CCC2(N)C(=O)O None
1310 2315 3H-LY354740 61 Rat Binding pKi = 6.0 6.0 -13 18
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
1369 2315 3H-LY354740 61 Rat Binding pKi = 6.0 6.0 -13 18
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
33032 2315 3H-LY354740 61 Rat Binding pKi = 6.0 6.0 -13 18
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
44272391 2315 3H-LY354740 61 Rat Binding pKi = 6.0 6.0 -13 18
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
88747398 2315 3H-LY354740 61 Rat Binding pKi = 6.0 6.0 -13 18
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
CHEMBL575060 2315 3H-LY354740 61 Rat Binding pKi = 6.0 6.0 -13 18
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
DB00142 2315 3H-LY354740 61 Rat Binding pKi = 6.0 6.0 -13 18
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
1310 2315 Functional 61 Rat Binding pKi = 5.9 5.9 -13 18
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
1369 2315 Functional 61 Rat Binding pKi = 5.9 5.9 -13 18
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
33032 2315 Functional 61 Rat Binding pKi = 5.9 5.9 -13 18
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
44272391 2315 Functional 61 Rat Binding pKi = 5.9 5.9 -13 18
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
88747398 2315 Functional 61 Rat Binding pKi = 5.9 5.9 -13 18
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
CHEMBL575060 2315 Functional 61 Rat Binding pKi = 5.9 5.9 -13 18
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
DB00142 2315 Functional 61 Rat Binding pKi = 5.9 5.9 -13 18
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
None 218660 3H-LY354740 0 Rat Binding pKi = 5.7 5.7 1 7
NoneNone
PDSP KiDatabase 173 2 3 3 -0.3 C1CC(CC1C(=O)O)(C(=O)O)N None
None 218660 Functional 0 Rat Binding pKi = 5.7 5.7 1 7
NoneNone
PDSP KiDatabase 173 2 3 3 -0.3 C1CC(CC1C(=O)O)(C(=O)O)N None
None 218821 Functional 0 Human Binding pKi = 6.5 6.5 -5 3
NoneNone
PDSP KiDatabase 203 4 4 4 -1.6 C1(C(C1C(=O)O)C(=O)O)C(C(=O)O)N None
None 218886 Functional 0 Human Binding pKi = 5.5 5.5 - 1
NoneNone
PDSP KiDatabase 174 2 4 4 -1.8 C1C(NCC1(C(=O)O)N)C(=O)O None
1310 2315 Functional 61 Human Binding pKi = 5.4 5.4 -22 18
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
1369 2315 Functional 61 Human Binding pKi = 5.4 5.4 -22 18
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
33032 2315 Functional 61 Human Binding pKi = 5.4 5.4 -22 18
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
44272391 2315 Functional 61 Human Binding pKi = 5.4 5.4 -22 18
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
88747398 2315 Functional 61 Human Binding pKi = 5.4 5.4 -22 18
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
CHEMBL575060 2315 Functional 61 Human Binding pKi = 5.4 5.4 -22 18
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
DB00142 2315 Functional 61 Human Binding pKi = 5.4 5.4 -22 18
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
None 218821 3H-LY354740 0 Rat Binding pKi = 7.2 7.2 3 3
NoneNone
PDSP KiDatabase 203 4 4 4 -1.6 C1(C(C1C(=O)O)C(=O)O)C(C(=O)O)N None
None 218822 3H-LY354740 0 Rat Binding pKi = 7.2 7.2 - 1
NoneNone
PDSP KiDatabase 159 3 3 3 -0.9 C1C(C1C(=O)O)C(C(=O)O)N None
114827 218819 3H-LY341495 0 Rat Binding pKi = 7.1 7.1 3 3
NoneNone
PDSP KiDatabase 185 2 3 3 -0.5 C1CC(C2C1C2C(=O)O)(C(=O)O)N None
114827 218819 3H-LY341495 0 Human Binding pKi = 7.1 7.1 -3 3
NoneNone
PDSP KiDatabase 185 2 3 3 -0.5 C1CC(C2C1C2C(=O)O)(C(=O)O)N None
1310 2315 Functional 61 Rat Binding pKi = 5.1 5.1 -13 18
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
1369 2315 Functional 61 Rat Binding pKi = 5.1 5.1 -13 18
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
33032 2315 Functional 61 Rat Binding pKi = 5.1 5.1 -13 18
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
44272391 2315 Functional 61 Rat Binding pKi = 5.1 5.1 -13 18
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
88747398 2315 Functional 61 Rat Binding pKi = 5.1 5.1 -13 18
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
CHEMBL575060 2315 Functional 61 Rat Binding pKi = 5.1 5.1 -13 18
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
DB00142 2315 Functional 61 Rat Binding pKi = 5.1 5.1 -13 18
NoneNone
PDSP KiDatabase 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N None
114827 218819 3H-LY354740 0 Rat Binding pKi = 8.1 8.1 3 3
NoneNone
PDSP KiDatabase 185 2 3 3 -0.5 C1CC(C2C1C2C(=O)O)(C(=O)O)N None
49822115 2146 None 24 Human Binding pKi = 8.3 8.3 - 1
Homologous displacement assay.Homologous displacement assay.
Guide to Pharmacology 414 5 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F 26589404
8947 2146 None 24 Human Binding pKi = 8.3 8.3 - 1
Homologous displacement assay.Homologous displacement assay.
Guide to Pharmacology 414 5 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F 26589404
CHEMBL3947764 2146 None 24 Human Binding pKi = 8.3 8.3 - 1
Homologous displacement assay.Homologous displacement assay.
Guide to Pharmacology 414 5 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)CN1CCC(CC1)c1ccccc1)(F)F 26589404
49836087 1061 None 0 Human Binding pKi = 6 6.0 - 1
UnclassifiedUnclassified
Guide to Pharmacology 328 2 2 4 3.3 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)Cl 21105727
6222 1061 None 0 Human Binding pKi = 6 6.0 - 1
UnclassifiedUnclassified
Guide to Pharmacology 328 2 2 4 3.3 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)Cl 21105727
CHEMBL1630805 1061 None 0 Human Binding pKi = 6 6.0 - 1
UnclassifiedUnclassified
Guide to Pharmacology 328 2 2 4 3.3 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)Cl 21105727
49858118 1110 None 0 Human Binding pKi = 6.1 6.1 - 1
UnclassifiedUnclassified
Guide to Pharmacology 324 3 2 5 2.7 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)OC 21105727
6224 1110 None 0 Human Binding pKi = 6.1 6.1 - 1
UnclassifiedUnclassified
Guide to Pharmacology 324 3 2 5 2.7 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)OC 21105727
CHEMBL1630807 1110 None 0 Human Binding pKi = 6.1 6.1 - 1
UnclassifiedUnclassified
Guide to Pharmacology 324 3 2 5 2.7 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)OC 21105727
49858117 1089 None 4 Human Binding pKi = 6.2 6.2 - 1
UnclassifiedUnclassified
Guide to Pharmacology 308 2 2 4 3.0 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)C 21105727
6223 1089 None 4 Human Binding pKi = 6.2 6.2 - 1
UnclassifiedUnclassified
Guide to Pharmacology 308 2 2 4 3.0 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)C 21105727
CHEMBL1630806 1089 None 4 Human Binding pKi = 6.2 6.2 - 1
UnclassifiedUnclassified
Guide to Pharmacology 308 2 2 4 3.0 O/N=C\1/c2ccccc2OC2(C1C2)C(=O)Nc1ccc(cc1)C 21105727
11310142 2422 None 14 Human Binding pKi = 6.8 6.8 1 2
UnclassifiedUnclassified
Guide to Pharmacology 199 2 3 3 -0.2 C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O 26341392
11614 2422 None 14 Human Binding pKi = 6.8 6.8 1 2
UnclassifiedUnclassified
Guide to Pharmacology 199 2 3 3 -0.2 C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O 26341392
CHEMBL192051 2422 None 14 Human Binding pKi = 6.8 6.8 1 2
UnclassifiedUnclassified
Guide to Pharmacology 199 2 3 3 -0.2 C[C@@H]1C[C@@]([C@H]2[C@@H]1[C@@H]2C(=O)O)(N)C(=O)O 26341392
11158623 3351 None 11 Human Binding pKi = 7.3 7.3 -8 2
UnclassifiedUnclassified
Guide to Pharmacology 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 22091727
6226 3351 None 11 Human Binding pKi = 7.3 7.3 -8 2
UnclassifiedUnclassified
Guide to Pharmacology 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 22091727
CHEMBL1629855 3351 None 11 Human Binding pKi = 7.3 7.3 -8 2
UnclassifiedUnclassified
Guide to Pharmacology 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 22091727
49765871 2145 None 41 Human Binding pKi = 7.8 7.8 - 1
UnclassifiedUnclassified
Guide to Pharmacology 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 23072213
6317 2145 None 41 Human Binding pKi = 7.8 7.8 - 1
UnclassifiedUnclassified
Guide to Pharmacology 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 23072213
CHEMBL2179319 2145 None 41 Human Binding pKi = 7.8 7.8 - 1
UnclassifiedUnclassified
Guide to Pharmacology 400 4 0 4 5.1 FC(c1c(ccn2c1nnc2CC1CC1)N1CCC(CC1)c1ccccc1)(F)F 23072213
11158623 3351 None 11 Rat Binding pKi = 8.3 8.3 8 2
UnclassifiedUnclassified
Guide to Pharmacology 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 22091727
6226 3351 None 11 Rat Binding pKi = 8.3 8.3 8 2
UnclassifiedUnclassified
Guide to Pharmacology 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 22091727
CHEMBL1629855 3351 None 11 Rat Binding pKi = 8.3 8.3 8 2
UnclassifiedUnclassified
Guide to Pharmacology 423 2 1 3 6.2 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cc(C)nc(c1)C 22091727
6325 3358 None 0 Rat Binding pKi = 8.3 8.3 - 1
UnclassifiedUnclassified
Guide to Pharmacology 474 3 2 4 5.4 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cccc(c1)S(=O)(=O)O 21470207
73755206 3358 None 0 Rat Binding pKi = 8.3 8.3 - 1
UnclassifiedUnclassified
Guide to Pharmacology 474 3 2 4 5.4 O=C1CC(=Nc2c(N1)cc(c(c2)C)C(F)(F)F)c1cccc(c1)c1cccc(c1)S(=O)(=O)O 21470207
6324 3353 None 0 Rat Binding pKi = 8.6 8.6 - 1
UnclassifiedUnclassified
Guide to Pharmacology 512 2 1 6 4.5 FC(c1cc(nc2n1ncc2C#Cc1cncc(c1)S(=O)(=O)O)c1ccc(cc1)C(F)(F)F)(F)F 21470207
73755205 3353 None 0 Rat Binding pKi = 8.6 8.6 - 1
UnclassifiedUnclassified
Guide to Pharmacology 512 2 1 6 4.5 FC(c1cc(nc2n1ncc2C#Cc1cncc(c1)S(=O)(=O)O)c1ccc(cc1)C(F)(F)F)(F)F 21470207
1373 2475 None 35 Human Binding pKi None 3.8 3.8 -6 5
UnclassifiedUnclassified
Guide to Pharmacology 209 3 3 3 0.6 OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C 10530814
139055582 2475 None 35 Human Binding pKi None 3.8 3.8 -6 5
UnclassifiedUnclassified
Guide to Pharmacology 209 3 3 3 0.6 OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C 10530814
446355 2475 None 35 Human Binding pKi None 3.8 3.8 -6 5
UnclassifiedUnclassified
Guide to Pharmacology 209 3 3 3 0.6 OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C 10530814
CHEMBL257626 2475 None 35 Human Binding pKi None 3.8 3.8 -6 5
UnclassifiedUnclassified
Guide to Pharmacology 209 3 3 3 0.6 OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C 10530814
DB04256 2475 None 35 Human Binding pKi None 3.8 3.8 -6 5
UnclassifiedUnclassified
Guide to Pharmacology 209 3 3 3 0.6 OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C 10530814
104766 33 None 30 Human Binding pKi None 4.2 4.2 -11 11
UnclassifiedUnclassified
Guide to Pharmacology 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10530814
1365 33 None 30 Human Binding pKi None 4.2 4.2 -11 11
UnclassifiedUnclassified
Guide to Pharmacology 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10530814
CHEMBL34453 33 None 30 Human Binding pKi None 4.2 4.2 -11 11
UnclassifiedUnclassified
Guide to Pharmacology 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10530814
1400 1538 None 0 Rat Binding pKi None 4.5 4.5 -7 2
UnclassifiedUnclassified
Guide to Pharmacology 175 5 3 3 0.0 CC[C@@](C(=O)O)(CCC(=O)O)N 10884552
1400 1538 None 0 Rat Binding pKi None 4.5 4.5 -7 2
UnclassifiedUnclassified
Guide to Pharmacology 175 5 3 3 0.0 CC[C@@](C(=O)O)(CCC(=O)O)N 9504391
5311079 1538 None 0 Rat Binding pKi None 4.5 4.5 -7 2
UnclassifiedUnclassified
Guide to Pharmacology 175 5 3 3 0.0 CC[C@@](C(=O)O)(CCC(=O)O)N 10884552
5311079 1538 None 0 Rat Binding pKi None 4.5 4.5 -7 2
UnclassifiedUnclassified
Guide to Pharmacology 175 5 3 3 0.0 CC[C@@](C(=O)O)(CCC(=O)O)N 9504391
CHEMBL1450466 1538 None 0 Rat Binding pKi None 4.5 4.5 -7 2
UnclassifiedUnclassified
Guide to Pharmacology 175 5 3 3 0.0 CC[C@@](C(=O)O)(CCC(=O)O)N 10884552
CHEMBL1450466 1538 None 0 Rat Binding pKi None 4.5 4.5 -7 2
UnclassifiedUnclassified
Guide to Pharmacology 175 5 3 3 0.0 CC[C@@](C(=O)O)(CCC(=O)O)N 9504391
1373 2475 None 35 Rat Binding pKi None 4.6 4.6 6 5
UnclassifiedUnclassified
Guide to Pharmacology 209 3 3 3 0.6 OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C 9504391
139055582 2475 None 35 Rat Binding pKi None 4.6 4.6 6 5
UnclassifiedUnclassified
Guide to Pharmacology 209 3 3 3 0.6 OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C 9504391
446355 2475 None 35 Rat Binding pKi None 4.6 4.6 6 5
UnclassifiedUnclassified
Guide to Pharmacology 209 3 3 3 0.6 OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C 9504391
CHEMBL257626 2475 None 35 Rat Binding pKi None 4.6 4.6 6 5
UnclassifiedUnclassified
Guide to Pharmacology 209 3 3 3 0.6 OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C 9504391
DB04256 2475 None 35 Rat Binding pKi None 4.6 4.6 6 5
UnclassifiedUnclassified
Guide to Pharmacology 209 3 3 3 0.6 OC(=O)c1ccc(cc1)[C@@](C(=O)O)(N)C 9504391
1374 2081 None 25 Rat Binding pKi None 4.8 4.8 -12 2
UnclassifiedUnclassified
Guide to Pharmacology 211 3 4 4 0.2 N[C@@H](c1ccc(c(c1)O)C(=O)O)C(=O)O 9504391
5311455 2081 None 25 Rat Binding pKi None 4.8 4.8 -12 2
UnclassifiedUnclassified
Guide to Pharmacology 211 3 4 4 0.2 N[C@@H](c1ccc(c(c1)O)C(=O)O)C(=O)O 9504391
CHEMBL39372 2081 None 25 Rat Binding pKi None 4.8 4.8 -12 2
UnclassifiedUnclassified
Guide to Pharmacology 211 3 4 4 0.2 N[C@@H](c1ccc(c(c1)O)C(=O)O)C(=O)O 9504391
1310 2315 None 61 Human Binding pKi None 4.9 4.9 -22 18
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10530814
1369 2315 None 61 Human Binding pKi None 4.9 4.9 -22 18
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10530814
33032 2315 None 61 Human Binding pKi None 4.9 4.9 -22 18
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10530814
44272391 2315 None 61 Human Binding pKi None 4.9 4.9 -22 18
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10530814
88747398 2315 None 61 Human Binding pKi None 4.9 4.9 -22 18
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10530814
CHEMBL575060 2315 None 61 Human Binding pKi None 4.9 4.9 -22 18
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10530814
DB00142 2315 None 61 Human Binding pKi None 4.9 4.9 -22 18
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10530814
1392 73 None 32 Human Binding pKi None 5 5.0 -1 2
UnclassifiedUnclassified
Guide to Pharmacology 174 2 4 4 -1.8 OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O 10530814
5310984 73 None 32 Human Binding pKi None 5 5.0 -1 2
UnclassifiedUnclassified
Guide to Pharmacology 174 2 4 4 -1.8 OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O 10530814
CHEMBL40086 73 None 32 Human Binding pKi None 5 5.0 -1 2
UnclassifiedUnclassified
Guide to Pharmacology 174 2 4 4 -1.8 OC(=O)[C@@H]1NC[C@@](C1)(N)C(=O)O 10530814
104766 33 None 30 Rat Binding pKi None 5.2 5.2 -3 11
UnclassifiedUnclassified
Guide to Pharmacology 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10884552
104766 33 None 30 Rat Binding pKi None 5.2 5.2 -3 11
UnclassifiedUnclassified
Guide to Pharmacology 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 9504391
1365 33 None 30 Rat Binding pKi None 5.2 5.2 -3 11
UnclassifiedUnclassified
Guide to Pharmacology 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10884552
1365 33 None 30 Rat Binding pKi None 5.2 5.2 -3 11
UnclassifiedUnclassified
Guide to Pharmacology 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 9504391
CHEMBL34453 33 None 30 Rat Binding pKi None 5.2 5.2 -3 11
UnclassifiedUnclassified
Guide to Pharmacology 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 10884552
CHEMBL34453 33 None 30 Rat Binding pKi None 5.2 5.2 -3 11
UnclassifiedUnclassified
Guide to Pharmacology 173 2 3 3 -0.3 OC(=O)[C@@H]1CC[C@@](C1)(N)C(=O)O 9504391
1398 365 None 0 Rat Binding pKi None 5.3 5.3 7 2
UnclassifiedUnclassified
Guide to Pharmacology 199 4 4 4 -1.1 OC(=O)C(COP(=O)(O)O)(N)C 9504391
3964633 365 None 0 Rat Binding pKi None 5.3 5.3 7 2
UnclassifiedUnclassified
Guide to Pharmacology 199 4 4 4 -1.1 OC(=O)C(COP(=O)(O)O)(N)C 9504391
CHEMBL1437137 365 None 0 Rat Binding pKi None 5.3 5.3 7 2
UnclassifiedUnclassified
Guide to Pharmacology 199 4 4 4 -1.1 OC(=O)C(COP(=O)(O)O)(N)C 9504391
1310 2315 None 61 Rat Binding pKi None 5.7 5.7 -13 18
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10652549
1310 2315 None 61 Rat Binding pKi None 5.7 5.7 -13 18
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 8022410
1369 2315 None 61 Rat Binding pKi None 5.7 5.7 -13 18
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10652549
1369 2315 None 61 Rat Binding pKi None 5.7 5.7 -13 18
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 8022410
33032 2315 None 61 Rat Binding pKi None 5.7 5.7 -13 18
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10652549
33032 2315 None 61 Rat Binding pKi None 5.7 5.7 -13 18
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 8022410
44272391 2315 None 61 Rat Binding pKi None 5.7 5.7 -13 18
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10652549
44272391 2315 None 61 Rat Binding pKi None 5.7 5.7 -13 18
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 8022410
88747398 2315 None 61 Rat Binding pKi None 5.7 5.7 -13 18
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10652549
88747398 2315 None 61 Rat Binding pKi None 5.7 5.7 -13 18
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 8022410
CHEMBL575060 2315 None 61 Rat Binding pKi None 5.7 5.7 -13 18
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10652549
CHEMBL575060 2315 None 61 Rat Binding pKi None 5.7 5.7 -13 18
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 8022410
DB00142 2315 None 61 Rat Binding pKi None 5.7 5.7 -13 18
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 10652549
DB00142 2315 None 61 Rat Binding pKi None 5.7 5.7 -13 18
UnclassifiedUnclassified
Guide to Pharmacology 147 4 3 3 -0.7 OC(=O)CC[C@@H](C(=O)O)N 8022410
1368 2290 None 30 Human Binding pKi None 6.3 6.3 -3 11
UnclassifiedUnclassified
Guide to Pharmacology 159 3 3 3 -0.9 N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O 10530814
5310956 2290 None 30 Human Binding pKi None 6.3 6.3 -3 11
UnclassifiedUnclassified
Guide to Pharmacology 159 3 3 3 -0.9 N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O 10530814
CHEMBL280563 2290 None 30 Human Binding pKi None 6.3 6.3 -3 11
UnclassifiedUnclassified
Guide to Pharmacology 159 3 3 3 -0.9 N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O 10530814
1377 1340 None 23 Human Binding pKi None 6.5 6.5 -2 6
UnclassifiedUnclassified
Guide to Pharmacology 203 4 4 4 -1.6 N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O 10530814
5310979 1340 None 23 Human Binding pKi None 6.5 6.5 -2 6
UnclassifiedUnclassified
Guide to Pharmacology 203 4 4 4 -1.6 N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O 10530814
CHEMBL284193 1340 None 23 Human Binding pKi None 6.5 6.5 -2 6
UnclassifiedUnclassified
Guide to Pharmacology 203 4 4 4 -1.6 N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O 10530814
1368 2290 None 30 Rat Binding pKi None 6.9 6.9 1 11
UnclassifiedUnclassified
Guide to Pharmacology 159 3 3 3 -0.9 N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O 10884552
1368 2290 None 30 Rat Binding pKi None 6.9 6.9 1 11
UnclassifiedUnclassified
Guide to Pharmacology 159 3 3 3 -0.9 N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O 9504391
5310956 2290 None 30 Rat Binding pKi None 6.9 6.9 1 11
UnclassifiedUnclassified
Guide to Pharmacology 159 3 3 3 -0.9 N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O 10884552
5310956 2290 None 30 Rat Binding pKi None 6.9 6.9 1 11
UnclassifiedUnclassified
Guide to Pharmacology 159 3 3 3 -0.9 N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O 9504391
CHEMBL280563 2290 None 30 Rat Binding pKi None 6.9 6.9 1 11
UnclassifiedUnclassified
Guide to Pharmacology 159 3 3 3 -0.9 N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O 10884552
CHEMBL280563 2290 None 30 Rat Binding pKi None 6.9 6.9 1 11
UnclassifiedUnclassified
Guide to Pharmacology 159 3 3 3 -0.9 N[C@@H]([C@H]1C[C@@H]1C(=O)O)C(=O)O 9504391
1393 1539 None 42 Human Binding pKi None 6.9 6.9 -2 6
UnclassifiedUnclassified
Guide to Pharmacology 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10530814
1396 1539 None 42 Human Binding pKi None 6.9 6.9 -2 6
UnclassifiedUnclassified
Guide to Pharmacology 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10530814
213056 1539 None 42 Human Binding pKi None 6.9 6.9 -2 6
UnclassifiedUnclassified
Guide to Pharmacology 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10530814
CHEMBL8759 1539 None 42 Human Binding pKi None 6.9 6.9 -2 6
UnclassifiedUnclassified
Guide to Pharmacology 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10530814
1377 1340 None 23 Rat Binding pKi None 7 7.0 -1 6
UnclassifiedUnclassified
Guide to Pharmacology 203 4 4 4 -1.6 N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O 10884552
1377 1340 None 23 Rat Binding pKi None 7 7.0 -1 6
UnclassifiedUnclassified
Guide to Pharmacology 203 4 4 4 -1.6 N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O 9504391
5310979 1340 None 23 Rat Binding pKi None 7 7.0 -1 6
UnclassifiedUnclassified
Guide to Pharmacology 203 4 4 4 -1.6 N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O 10884552
5310979 1340 None 23 Rat Binding pKi None 7 7.0 -1 6
UnclassifiedUnclassified
Guide to Pharmacology 203 4 4 4 -1.6 N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O 9504391
CHEMBL284193 1340 None 23 Rat Binding pKi None 7 7.0 -1 6
UnclassifiedUnclassified
Guide to Pharmacology 203 4 4 4 -1.6 N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O 10884552
CHEMBL284193 1340 None 23 Rat Binding pKi None 7 7.0 -1 6
UnclassifiedUnclassified
Guide to Pharmacology 203 4 4 4 -1.6 N[C@@H](C1[C@H]([C@@H]1C(=O)O)C(=O)O)C(=O)O 9504391
1393 1539 None 42 Rat Binding pKi None 7.9 7.9 1 6
UnclassifiedUnclassified
Guide to Pharmacology 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10884552
1393 1539 None 42 Rat Binding pKi None 7.9 7.9 1 6
UnclassifiedUnclassified
Guide to Pharmacology 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 9504391
1396 1539 None 42 Rat Binding pKi None 7.9 7.9 1 6
UnclassifiedUnclassified
Guide to Pharmacology 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10884552
1396 1539 None 42 Rat Binding pKi None 7.9 7.9 1 6
UnclassifiedUnclassified
Guide to Pharmacology 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 9504391
213056 1539 None 42 Rat Binding pKi None 7.9 7.9 1 6
UnclassifiedUnclassified
Guide to Pharmacology 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10884552
213056 1539 None 42 Rat Binding pKi None 7.9 7.9 1 6
UnclassifiedUnclassified
Guide to Pharmacology 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 9504391
CHEMBL8759 1539 None 42 Rat Binding pKi None 7.9 7.9 1 6
UnclassifiedUnclassified
Guide to Pharmacology 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 10884552
CHEMBL8759 1539 None 42 Rat Binding pKi None 7.9 7.9 1 6
UnclassifiedUnclassified
Guide to Pharmacology 185 2 3 3 -0.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CC2)(N)C(=O)O 9504391
10197984 2421 None 36 Human Binding pKi None 7.9 7.9 2 5
UnclassifiedUnclassified
Guide to Pharmacology 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10090786
1394 2421 None 36 Human Binding pKi None 7.9 7.9 2 5
UnclassifiedUnclassified
Guide to Pharmacology 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10090786
CHEMBL275079 2421 None 36 Human Binding pKi None 7.9 7.9 2 5
UnclassifiedUnclassified
Guide to Pharmacology 187 2 3 4 -1.5 OC(=O)[C@H]1[C@H]2[C@@H]1[C@](CO2)(N)C(=O)O 10090786
1378 2417 None 39 Rat Binding pKi None 8.4 8.4 -1 10
UnclassifiedUnclassified
Guide to Pharmacology 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10884552
1378 2417 None 39 Rat Binding pKi None 8.4 8.4 -1 10
UnclassifiedUnclassified
Guide to Pharmacology 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 9504391
1399 2417 None 39 Rat Binding pKi None 8.4 8.4 -1 10
UnclassifiedUnclassified
Guide to Pharmacology 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10884552
1399 2417 None 39 Rat Binding pKi None 8.4 8.4 -1 10
UnclassifiedUnclassified
Guide to Pharmacology 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 9504391
9819927 2417 None 39 Rat Binding pKi None 8.4 8.4 -1 10
UnclassifiedUnclassified
Guide to Pharmacology 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10884552
9819927 2417 None 39 Rat Binding pKi None 8.4 8.4 -1 10
UnclassifiedUnclassified
Guide to Pharmacology 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 9504391
CHEMBL432038 2417 None 39 Rat Binding pKi None 8.4 8.4 -1 10
UnclassifiedUnclassified
Guide to Pharmacology 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10884552
CHEMBL432038 2417 None 39 Rat Binding pKi None 8.4 8.4 -1 10
UnclassifiedUnclassified
Guide to Pharmacology 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 9504391
1378 2417 None 39 Human Binding pKi None 8.6 8.6 -2 10
UnclassifiedUnclassified
Guide to Pharmacology 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10530814
1399 2417 None 39 Human Binding pKi None 8.6 8.6 -2 10
UnclassifiedUnclassified
Guide to Pharmacology 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10530814
9819927 2417 None 39 Human Binding pKi None 8.6 8.6 -2 10
UnclassifiedUnclassified
Guide to Pharmacology 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10530814
CHEMBL432038 2417 None 39 Human Binding pKi None 8.6 8.6 -2 10
UnclassifiedUnclassified
Guide to Pharmacology 353 5 3 4 2.8 OC(=O)[C@H]1C[C@@H]1[C@](C(=O)O)(CC1c2ccccc2Oc2c1cccc2)N 10530814
1397 2529 None 15 Rat Binding pKi None 8.7 8.7 -1 5
UnclassifiedUnclassified
Guide to Pharmacology 377 5 3 4 2.1 OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 14975669
1397 2529 None 15 Rat Binding pKi None 8.7 8.7 -1 5
UnclassifiedUnclassified
Guide to Pharmacology 377 5 3 4 2.1 OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 15317467
9886034 2529 None 15 Rat Binding pKi None 8.7 8.7 -1 5
UnclassifiedUnclassified
Guide to Pharmacology 377 5 3 4 2.1 OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 14975669
9886034 2529 None 15 Rat Binding pKi None 8.7 8.7 -1 5
UnclassifiedUnclassified
Guide to Pharmacology 377 5 3 4 2.1 OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 15317467
CHEMBL186453 2529 None 15 Rat Binding pKi None 8.7 8.7 -1 5
UnclassifiedUnclassified
Guide to Pharmacology 377 5 3 4 2.1 OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 14975669
CHEMBL186453 2529 None 15 Rat Binding pKi None 8.7 8.7 -1 5
UnclassifiedUnclassified
Guide to Pharmacology 377 5 3 4 2.1 OC(=O)[C@]1(N)[C@H](OCc2ccc(c(c2)Cl)Cl)C[C@@H]2[C@H]1[C@@]2(F)C(=O)O 15317467
1395 2528 None 14 Rat Binding pKi None 9.2 9.2 2 2
UnclassifiedUnclassified
Guide to Pharmacology 217 2 3 4 -1.2 O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O 11123999
9837317 2528 None 14 Rat Binding pKi None 9.2 9.2 2 2
UnclassifiedUnclassified
Guide to Pharmacology 217 2 3 4 -1.2 O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O 11123999
CHEMBL121053 2528 None 14 Rat Binding pKi None 9.2 9.2 2 2
UnclassifiedUnclassified
Guide to Pharmacology 217 2 3 4 -1.2 O=C1C[C@@]([C@H]2[C@@H]1[C@]2(F)C(=O)O)(N)C(=O)O 11123999
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