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Volumn 14, Issue , 2013, Pages

Allosteric transition: A comparison of two models

Author keywords

[No Author keywords available]

Indexed keywords

ALLOSTERIC TWO STATE MODEL; ALLOSTERISM; ARTICLE; BINDING SITE; CONCENTRATION RESPONSE; CONFORMATION; EXTENDED OPERATIONAL MODEL; INTERMETHOD COMPARISON; LIGAND BINDING; MODEL; SIMULATION; CHEMICAL STRUCTURE; METABOLISM;

EID: 84879835462     PISSN: 20506511     EISSN: None     Source Type: Journal    
DOI: 10.1186/2050-6511-14-4     Document Type: Article
Times cited : (5)

References (60)
  • 1
    • 79959556142 scopus 로고    scopus 로고
    • Drug buddies
    • 10.1038/474433a, 21697923
    • Ledford H. Drug buddies. Nature 2011, 474:433-434. 10.1038/474433a, 21697923.
    • (2011) Nature , vol.474 , pp. 433-434
    • Ledford, H.1
  • 2
    • 79951504081 scopus 로고    scopus 로고
    • Pharmaceutical industry must take its medicine
    • 10.1038/470141a, 21307893
    • Macilwain C. Pharmaceutical industry must take its medicine. Nature 2011, 470:141. 10.1038/470141a, 21307893.
    • (2011) Nature , vol.470 , pp. 141
    • Macilwain, C.1
  • 3
    • 84857743319 scopus 로고    scopus 로고
    • Diagnosing the decline in pharmaceutical R&D efficiency
    • 10.1038/nrd3681, 22378269
    • Scannell JW, Blanckley A, Boldon H, Warrington B. Diagnosing the decline in pharmaceutical R&D efficiency. Nat Rev Drug Discov 2012, 11:191-200. 10.1038/nrd3681, 22378269.
    • (2012) Nat Rev Drug Discov , vol.11 , pp. 191-200
    • Scannell, J.W.1    Blanckley, A.2    Boldon, H.3    Warrington, B.4
  • 4
    • 82055186696 scopus 로고    scopus 로고
    • A hydrazide linker strategy for heterobivalent compounds as ortho- and allosteric ligands of acetylcholine-binding proteins
    • 10.2174/156802611798184427, 22039876
    • Elsinghorst PW, Härtig W, Gündisch D, Mohr K, Tränkle C, Gütschow M. A hydrazide linker strategy for heterobivalent compounds as ortho- and allosteric ligands of acetylcholine-binding proteins. Curr Top Med Chem 2011, 11:2731-2748. 10.2174/156802611798184427, 22039876.
    • (2011) Curr Top Med Chem , vol.11 , pp. 2731-2748
    • Elsinghorst, P.W.1    Härtig, W.2    Gündisch, D.3    Mohr, K.4    Tränkle, C.5    Gütschow, M.6
  • 5
    • 80051544311 scopus 로고    scopus 로고
    • Functionally biased modulation of A(3) adenosine receptor agonist efficacy and potency by imidazoquinolinamine allosteric enhancers
    • 10.1016/j.bcp.2011.06.017, 3152598, 21718691
    • Gao ZG, Verzijl D, Zweemer A, Ye K, Göblyös A, Ijzerman AP. Functionally biased modulation of A(3) adenosine receptor agonist efficacy and potency by imidazoquinolinamine allosteric enhancers. Biochem Pharmacol 2011, 82:658-668. 10.1016/j.bcp.2011.06.017, 3152598, 21718691.
    • (2011) Biochem Pharmacol , vol.82 , pp. 658-668
    • Gao, Z.G.1    Verzijl, D.2    Zweemer, A.3    Ye, K.4    Göblyös, A.5    Ijzerman, A.P.6
  • 6
    • 84859730971 scopus 로고    scopus 로고
    • Reversed binding of a small molecule ligand in homologous chemokine receptors - differential role of extracellular loop 2
    • 10.1111/j.1476-5381.2011.01771.x, 3415653, 22050085
    • Jensen PC, Thiele S, Steen A, Elder A, Kolbeck R, Ghosh S. Reversed binding of a small molecule ligand in homologous chemokine receptors - differential role of extracellular loop 2. Br J Pharmacol 2012, 166:258-275. 10.1111/j.1476-5381.2011.01771.x, 3415653, 22050085.
    • (2012) Br J Pharmacol , vol.166 , pp. 258-275
    • Jensen, P.C.1    Thiele, S.2    Steen, A.3    Elder, A.4    Kolbeck, R.5    Ghosh, S.6
  • 7
    • 84857375139 scopus 로고    scopus 로고
    • Allosteric modulation of seven transmembrane spanning receptors: theory, practice, and opportunities for central nervous system drug discovery
    • 10.1021/jm201139r, 3349997, 22148748
    • Melancon BJ, Hopkins CR, Wood MR, Emmitte KA, Niswender CM, Christopoulos A. Allosteric modulation of seven transmembrane spanning receptors: theory, practice, and opportunities for central nervous system drug discovery. J Med Chem 2012, 55:1445-1464. 10.1021/jm201139r, 3349997, 22148748.
    • (2012) J Med Chem , vol.55 , pp. 1445-1464
    • Melancon, B.J.1    Hopkins, C.R.2    Wood, M.R.3    Emmitte, K.A.4    Niswender, C.M.5    Christopoulos, A.6
  • 8
    • 84455173446 scopus 로고    scopus 로고
    • Probe dependence in the allosteric modulation of a G protein-coupled receptor: Implications for detection and validation of allosteric ligand effects
    • 10.1124/mol.111.074872, 21989256
    • Valant C, Felder CC, Sexton PM, Christopoulos A. Probe dependence in the allosteric modulation of a G protein-coupled receptor: Implications for detection and validation of allosteric ligand effects. Mol Pharmacol 2012, 81:41-52. 10.1124/mol.111.074872, 21989256.
    • (2012) Mol Pharmacol , vol.81 , pp. 41-52
    • Valant, C.1    Felder, C.C.2    Sexton, P.M.3    Christopoulos, A.4
  • 9
    • 77955799768 scopus 로고    scopus 로고
    • Protein-protein interactions monitored in cells from transgenic mice using bioluminescence resonance energy transfer
    • 10.1096/fj.09-144816, 20335229
    • Audet M, Lagacé M, Silversides DW, Bouvier M. Protein-protein interactions monitored in cells from transgenic mice using bioluminescence resonance energy transfer. FASEB J 2010, 24:2829-2838. 10.1096/fj.09-144816, 20335229.
    • (2010) FASEB J , vol.24 , pp. 2829-2838
    • Audet, M.1    Lagacé, M.2    Silversides, D.W.3    Bouvier, M.4
  • 10
    • 80053357815 scopus 로고    scopus 로고
    • Conformational changes in the G protein Gs induced by the ß2 adrenergic receptor
    • 10.1038/nature10488, 3448949, 21956331
    • Chung KY, Rasmussen SG, Liu T, Li S, Devree BT, Chae PS. Conformational changes in the G protein Gs induced by the ß2 adrenergic receptor. Nature 2011, 477:611-615. 10.1038/nature10488, 3448949, 21956331.
    • (2011) Nature , vol.477 , pp. 611-615
    • Chung, K.Y.1    Rasmussen, S.G.2    Liu, T.3    Li, S.4    Devree, B.T.5    Chae, P.S.6
  • 11
    • 79958785452 scopus 로고    scopus 로고
    • The oligomeric state sets GABA(B) receptor signalling efficacy
    • 10.1038/emboj.2011.143, 3116278, 21552208
    • Comps-Agrar L, Kniazeff J, Nørskov-Lauritsen L, Maurel D, Gassmann M, Gregor N. The oligomeric state sets GABA(B) receptor signalling efficacy. EMBO J 2011, 30:2336-2349. 10.1038/emboj.2011.143, 3116278, 21552208.
    • (2011) EMBO J , vol.30 , pp. 2336-2349
    • Comps-Agrar, L.1    Kniazeff, J.2    Nørskov-Lauritsen, L.3    Maurel, D.4    Gassmann, M.5    Gregor, N.6
  • 12
    • 84856627191 scopus 로고    scopus 로고
    • 3D-QSAR and 3D-QSSR models of negative allosteric modulators facilitate the design of a novel selective antagonist of human a4ß2 neuronal nicotinic acetylcholine receptors
    • 10.1016/j.bmcl.2011.11.051, 3274641, 22285942
    • Henderson BJ, Orac CM, Maciagiewicz I, Bergmeier SC, McKay DB. 3D-QSAR and 3D-QSSR models of negative allosteric modulators facilitate the design of a novel selective antagonist of human a4ß2 neuronal nicotinic acetylcholine receptors. Bioorg Med Chem Lett 2012, 22:1797-1813. 10.1016/j.bmcl.2011.11.051, 3274641, 22285942.
    • (2012) Bioorg Med Chem Lett , vol.22 , pp. 1797-1813
    • Henderson, B.J.1    Orac, C.M.2    Maciagiewicz, I.3    Bergmeier, S.C.4    McKay, D.B.5
  • 13
    • 77953488648 scopus 로고    scopus 로고
    • Conserved water-mediated hydrogen bond network between TM-I, -II, -VI, and -VII in 7TM receptor activation
    • 10.1074/jbc.M110.106021, 2885241, 20395291
    • Nygaard R, Valentin-Hansen L, Mokrosinski J, Frimurer TM, Schwartz TW. Conserved water-mediated hydrogen bond network between TM-I, -II, -VI, and -VII in 7TM receptor activation. J Biol Chem 2010, 285:19625-19636. 10.1074/jbc.M110.106021, 2885241, 20395291.
    • (2010) J Biol Chem , vol.285 , pp. 19625-19636
    • Nygaard, R.1    Valentin-Hansen, L.2    Mokrosinski, J.3    Frimurer, T.M.4    Schwartz, T.W.5
  • 14
    • 84860671694 scopus 로고    scopus 로고
    • The role of the second and third extracellular loops of the adenosine A1 receptor in activation and allosteric modulation
    • 10.1016/j.bcp.2012.03.008, 22449615
    • Peeters MC, Wisse LE, Dinaj A, Vroling B, Vriend G, Ijzerman AP. The role of the second and third extracellular loops of the adenosine A1 receptor in activation and allosteric modulation. Biochem Pharmacol 2012, 84:76-87. 10.1016/j.bcp.2012.03.008, 22449615.
    • (2012) Biochem Pharmacol , vol.84 , pp. 76-87
    • Peeters, M.C.1    Wisse, L.E.2    Dinaj, A.3    Vroling, B.4    Vriend, G.5    Ijzerman, A.P.6
  • 15
    • 84857432572 scopus 로고    scopus 로고
    • Lateral Allosterism in the Glucagon Receptor Family: GLP-1 Induces GPCR Heteromer Formation
    • 10.1124/mol.111.074757, 22108912
    • Schelshorn DW, Joly F, Mutel S, Hampe C, Breton B, Mutel V. Lateral Allosterism in the Glucagon Receptor Family: GLP-1 Induces GPCR Heteromer Formation. Mol Pharmacol 2012, 81:309-318. 10.1124/mol.111.074757, 22108912.
    • (2012) Mol Pharmacol , vol.81 , pp. 309-318
    • Schelshorn, D.W.1    Joly, F.2    Mutel, S.3    Hampe, C.4    Breton, B.5    Mutel, V.6
  • 16
    • 79959343623 scopus 로고    scopus 로고
    • Interaction of a G protein with an activated receptor opens the interdomain interface in the alpha subunit
    • 10.1073/pnas.1105810108, 3111277, 21606326
    • Van Eps N, Preininger AM, Alexander N, Kaya AI, Meier S, Meiler J. Interaction of a G protein with an activated receptor opens the interdomain interface in the alpha subunit. Proc Natl Acad Sci USA 2011, 108:9420-9424. 10.1073/pnas.1105810108, 3111277, 21606326.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 9420-9424
    • Van Eps, N.1    Preininger, A.M.2    Alexander, N.3    Kaya, A.I.4    Meier, S.5    Meiler, J.6
  • 17
    • 78149496159 scopus 로고    scopus 로고
    • Allosteric modulation of G protein-coupled receptors: a pharmacological perspective
    • 10.1016/j.neuropharm.2010.07.010, 20637785
    • Keov P, Sexton PM, Christopoulos A. Allosteric modulation of G protein-coupled receptors: a pharmacological perspective. Neuropharmacology 2011, 60:24-35. 10.1016/j.neuropharm.2010.07.010, 20637785.
    • (2011) Neuropharmacology , vol.60 , pp. 24-35
    • Keov, P.1    Sexton, P.M.2    Christopoulos, A.3
  • 19
    • 77951985712 scopus 로고    scopus 로고
    • Allosteric ligands for G protein-coupled receptors: a novel strategy with attractive therapeutic opportunities
    • De Amici M, Dallanoce C, Holzgrabe U, Tränkle C, Mohr K. Allosteric ligands for G protein-coupled receptors: a novel strategy with attractive therapeutic opportunities. Med Res Rev 2010, 30:463-549.
    • (2010) Med Res Rev , vol.30 , pp. 463-549
    • De Amici, M.1    Dallanoce, C.2    Holzgrabe, U.3    Tränkle, C.4    Mohr, K.5
  • 20
    • 44249089997 scopus 로고    scopus 로고
    • Two-state models and the analysis of the allosteric effect of gallamine at the m2 muscarinic receptor
    • 10.1124/jpet.108.136960, 18305010
    • Ehlert FJ, Griffin MT. Two-state models and the analysis of the allosteric effect of gallamine at the m2 muscarinic receptor. J Pharmacol Exp Ther 2008, 325:1039-1060. 10.1124/jpet.108.136960, 18305010.
    • (2008) J Pharmacol Exp Ther , vol.325 , pp. 1039-1060
    • Ehlert, F.J.1    Griffin, M.T.2
  • 21
    • 79956317677 scopus 로고    scopus 로고
    • G protein-coupled receptor heteromerization: a role in allosteric modulation of ligand binding
    • 10.1124/mol.110.070847, 3102551, 21415307
    • Gomes I, Ijzerman AP, Ye K, Maillet EL, Devi LA. G protein-coupled receptor heteromerization: a role in allosteric modulation of ligand binding. Mol Pharmacol 2011, 79:1044-1052. 10.1124/mol.110.070847, 3102551, 21415307.
    • (2011) Mol Pharmacol , vol.79 , pp. 1044-1052
    • Gomes, I.1    Ijzerman, A.P.2    Ye, K.3    Maillet, E.L.4    Devi, L.A.5
  • 22
    • 0033669603 scopus 로고    scopus 로고
    • Modeling the functional effects of allosteric modulators at pharmacological receptors: an extension of the two-state model of receptor activation
    • Hall DA. Modeling the functional effects of allosteric modulators at pharmacological receptors: an extension of the two-state model of receptor activation. Mol Pharmacol 2000, 58:1412-1423.
    • (2000) Mol Pharmacol , vol.58 , pp. 1412-1423
    • Hall, D.A.1
  • 23
    • 36849071252 scopus 로고    scopus 로고
    • Allosteric small molecules unveil a role of an extracellular E2/transmembrane helix 7 junction for G protein-coupled receptor activation
    • Jäger D, Schmalenbach C, Prilla S, Schrobang J, Kebig A, Sennwitz M. Allosteric small molecules unveil a role of an extracellular E2/transmembrane helix 7 junction for G protein-coupled receptor activation. J Biol Chem 2007, 30:34968-34976.
    • (2007) J Biol Chem , vol.30 , pp. 34968-34976
    • Jäger, D.1    Schmalenbach, C.2    Prilla, S.3    Schrobang, J.4    Kebig, A.5    Sennwitz, M.6
  • 24
    • 69649097791 scopus 로고    scopus 로고
    • '7TM receptor allostery: putting numbers to shapeshifting proteins
    • 10.1016/j.tips.2009.06.007, 19729207
    • Kenakin TP. '7TM receptor allostery: putting numbers to shapeshifting proteins. Trends Pharmacol Sci 2009, 30:460-469. 10.1016/j.tips.2009.06.007, 19729207.
    • (2009) Trends Pharmacol Sci , vol.30 , pp. 460-469
    • Kenakin, T.P.1
  • 25
    • 80052018338 scopus 로고    scopus 로고
    • Allosteric modulation of the M3 muscarinic receptor by amiodarone and N-ethylamiodarone: application of the four-ligand allosteric two-state model
    • 10.1124/mol.111.072991, 3164337, 21602476
    • Stahl E, Elmslie G, Ellis J. Allosteric modulation of the M3 muscarinic receptor by amiodarone and N-ethylamiodarone: application of the four-ligand allosteric two-state model. Mol Pharmacol 2011, 80:378-388. 10.1124/mol.111.072991, 3164337, 21602476.
    • (2011) Mol Pharmacol , vol.80 , pp. 378-388
    • Stahl, E.1    Elmslie, G.2    Ellis, J.3
  • 26
    • 34447632041 scopus 로고    scopus 로고
    • Allosteric GPCR modulators: taking advantage of permissive receptor pharmacology. Supplementary data
    • 10.1016/j.tips.2007.06.004, 17629965
    • Leach K, Sexton PM, Christopoulos A. Allosteric GPCR modulators: taking advantage of permissive receptor pharmacology. Supplementary data. Trends Pharmacol Sci 2007, 28:382-389. 10.1016/j.tips.2007.06.004, 17629965.
    • (2007) Trends Pharmacol Sci , vol.28 , pp. 382-389
    • Leach, K.1    Sexton, P.M.2    Christopoulos, A.3
  • 27
    • 0021058380 scopus 로고
    • Operational models of pharmacological agonism
    • 10.1098/rspb.1983.0093, 6141562
    • Black JW, Leff P. Operational models of pharmacological agonism. Proc R Soc Lond B 1983, 220:141-162. 10.1098/rspb.1983.0093, 6141562.
    • (1983) Proc R Soc Lond B , vol.220 , pp. 141-162
    • Black, J.W.1    Leff, P.2
  • 29
    • 0019137579 scopus 로고
    • A ternary complex model explains the agonist specific binding properties of the adenylate cyclase coupled beta- adrenergic receptor
    • De Lean A, Stadel JM, Lefkowitz RJ. A ternary complex model explains the agonist specific binding properties of the adenylate cyclase coupled beta- adrenergic receptor. J Biol Chem 1980, 255:7108-7117.
    • (1980) J Biol Chem , vol.255 , pp. 7108-7117
    • De Lean, A.1    Stadel, J.M.2    Lefkowitz, R.J.3
  • 30
    • 0020533362 scopus 로고
    • Modification of the binding properties of muscarinic receptors by gallamine
    • Stockton JM, Birdsall NJ, Burgen AS, Hulme EC. Modification of the binding properties of muscarinic receptors by gallamine. Mol Pharmacol 1983, 23:551-557.
    • (1983) Mol Pharmacol , vol.23 , pp. 551-557
    • Stockton, J.M.1    Birdsall, N.J.2    Burgen, A.S.3    Hulme, E.C.4
  • 31
    • 0023958554 scopus 로고
    • Estimation of the affinities of allosteric ligands using radioligand binding and pharmacological null methods
    • Ehlert FJ. Estimation of the affinities of allosteric ligands using radioligand binding and pharmacological null methods. Mol Pharmacol 1988, 33:187-194.
    • (1988) Mol Pharmacol , vol.33 , pp. 187-194
    • Ehlert, F.J.1
  • 32
    • 79954988501 scopus 로고    scopus 로고
    • Quantitative analysis reveals multiple mechanisms of allosteric modulation of the mGlu5 receptor in rat astroglia
    • 10.1124/mol.110.068882, 3082933, 21321061
    • Bradley SJ, Langmead CJ, Watson JM, Challiss RA. Quantitative analysis reveals multiple mechanisms of allosteric modulation of the mGlu5 receptor in rat astroglia. Mol Pharmacol 2011, 79:874-885. 10.1124/mol.110.068882, 3082933, 21321061.
    • (2011) Mol Pharmacol , vol.79 , pp. 874-885
    • Bradley, S.J.1    Langmead, C.J.2    Watson, J.M.3    Challiss, R.A.4
  • 33
    • 84855290525 scopus 로고    scopus 로고
    • A Monod-Wyman-Changeux mechanism can explain G protein-coupled receptor (GPCR) allosteric modulation
    • 10.1074/jbc.M111.314278, 3249119, 22086918
    • Canals M, Lane JR, Wen A, Scammells PJ, Sexton PM, Christopoulos A. A Monod-Wyman-Changeux mechanism can explain G protein-coupled receptor (GPCR) allosteric modulation. J Biol Chem 2012, 287:650-659. 10.1074/jbc.M111.314278, 3249119, 22086918.
    • (2012) J Biol Chem , vol.287 , pp. 650-659
    • Canals, M.1    Lane, J.R.2    Wen, A.3    Scammells, P.J.4    Sexton, P.M.5    Christopoulos, A.6
  • 34
    • 84857497773 scopus 로고    scopus 로고
    • Biased signaling and allosteric machines; new vistas and challenges for drug discovery
    • 10.1111/j.1476-5381.2011.01749.x, 3372820, 22023017
    • Kenakin TP. Biased signaling and allosteric machines; new vistas and challenges for drug discovery. Br J Pharmacol 2012, 165:1659-1669. 10.1111/j.1476-5381.2011.01749.x, 3372820, 22023017.
    • (2012) Br J Pharmacol , vol.165 , pp. 1659-1669
    • Kenakin, T.P.1
  • 35
    • 79954987479 scopus 로고    scopus 로고
    • The role of transmembrane domain 3 in the actions of orthosteric, allosteric, and atypical agonists of the M4 muscarinic acetylcholine receptor
    • 10.1124/mol.111.070938, 21300722
    • Leach K, Davey AE, Felder CC, Sexton PM, Christopoulos A. The role of transmembrane domain 3 in the actions of orthosteric, allosteric, and atypical agonists of the M4 muscarinic acetylcholine receptor. Mol Pharmacol 2011, 79:855-865. 10.1124/mol.111.070938, 21300722.
    • (2011) Mol Pharmacol , vol.79 , pp. 855-865
    • Leach, K.1    Davey, A.E.2    Felder, C.C.3    Sexton, P.M.4    Christopoulos, A.5
  • 36
    • 79959309348 scopus 로고    scopus 로고
    • Extracellular loop 2 of the free fatty acid receptor 2 mediates allosterism of a phenylacetamide ago-allosteric modulator
    • 10.1124/mol.110.070789, 3127537, 21498659
    • Smith NJ, Ward RJ, Stoddart LA, Hudson BD, Kostenis E, Ulven T. Extracellular loop 2 of the free fatty acid receptor 2 mediates allosterism of a phenylacetamide ago-allosteric modulator. Mol Pharmacol 2011, 80:163-173. 10.1124/mol.110.070789, 3127537, 21498659.
    • (2011) Mol Pharmacol , vol.80 , pp. 163-173
    • Smith, N.J.1    Ward, R.J.2    Stoddart, L.A.3    Hudson, B.D.4    Kostenis, E.5    Ulven, T.6
  • 37
    • 79952396557 scopus 로고    scopus 로고
    • Impact of species variability and 'probe-dependence' on the detection and in vivo validation of allosteric modulation at the M4 muscarinic acetylcholine receptor
    • 10.1111/j.1476-5381.2010.01184.x, 3057301, 21198541
    • Suratman S, Leach K, Sexton P, Felder C, Loiacono R, Christopoulos A. Impact of species variability and 'probe-dependence' on the detection and in vivo validation of allosteric modulation at the M4 muscarinic acetylcholine receptor. Br J Pharmacol 2011, 162:1659-1670. 10.1111/j.1476-5381.2010.01184.x, 3057301, 21198541.
    • (2011) Br J Pharmacol , vol.162 , pp. 1659-1670
    • Suratman, S.1    Leach, K.2    Sexton, P.3    Felder, C.4    Loiacono, R.5    Christopoulos, A.6
  • 38
    • 84863950667 scopus 로고    scopus 로고
    • Allosteric modulation of endogenous metabolites as an avenue for drug discovery
    • 10.1124/mol.112.079319, 22576254
    • Wootten D, Savage EE, Valant C, May LT, Sloop KW, Ficorilli J. Allosteric modulation of endogenous metabolites as an avenue for drug discovery. Mol Pharmacol 2012, 82:281-290. 10.1124/mol.112.079319, 22576254.
    • (2012) Mol Pharmacol , vol.82 , pp. 281-290
    • Wootten, D.1    Savage, E.E.2    Valant, C.3    May, L.T.4    Sloop, K.W.5    Ficorilli, J.6
  • 39
    • 77958152523 scopus 로고    scopus 로고
    • Class A GPCR heterodimers: evidence from binding studies
    • 10.1016/j.tips.2010.08.003, 20870299
    • Birdsall NJ. Class A GPCR heterodimers: evidence from binding studies. Trends Pharmacol Sci 2010, 31:499-508. 10.1016/j.tips.2010.08.003, 20870299.
    • (2010) Trends Pharmacol Sci , vol.31 , pp. 499-508
    • Birdsall, N.J.1
  • 40
    • 79551486842 scopus 로고    scopus 로고
    • Negative cooperativity in binding of muscarinic receptor agonists and GDP as a measure of agonist efficacy
    • 10.1111/j.1476-5381.2010.01081.x, 3051377,3051377, 20958290
    • Jakubík J, Janícková H, El-Fakahany EE, Doležal V. Negative cooperativity in binding of muscarinic receptor agonists and GDP as a measure of agonist efficacy. Br J Pharmacol 2011, 162:1029-1044. 10.1111/j.1476-5381.2010.01081.x, 3051377,3051377, 20958290.
    • (2011) Br J Pharmacol , vol.162 , pp. 1029-1044
    • Jakubík, J.1    Janícková, H.2    El-Fakahany, E.E.3    Doležal, V.4
  • 41
    • 60749092852 scopus 로고    scopus 로고
    • Harmonic oscillator model of the insulin and IGF1 receptors' allosteric binding and activation
    • Kiselyov VV, Versteyhe S, Gauguin L, De Meyts P. Harmonic oscillator model of the insulin and IGF1 receptors' allosteric binding and activation. Mol Syst Biol 2009, 5:1-12.
    • (2009) Mol Syst Biol , vol.5 , pp. 1-12
    • Kiselyov, V.V.1    Versteyhe, S.2    Gauguin, L.3    De Meyts, P.4
  • 42
    • 42449160650 scopus 로고    scopus 로고
    • Modeling the binding and function of metabotropic glutamate receptors
    • 10.1124/jpet.107.133967, 18287211
    • Rovira X, Roche D, Serra J, Kniazeff J, Pin JP, Giraldo J. Modeling the binding and function of metabotropic glutamate receptors. J Pharmacol Exp Ther 2008, 325:443-456. 10.1124/jpet.107.133967, 18287211.
    • (2008) J Pharmacol Exp Ther , vol.325 , pp. 443-456
    • Rovira, X.1    Roche, D.2    Serra, J.3    Kniazeff, J.4    Pin, J.P.5    Giraldo, J.6
  • 43
    • 0019332443 scopus 로고
    • A two-state model of an enzyme with an allosteric regulator site capable of metabolizing the regulatory ligand
    • Birnbaumer L, Bearer CF, Iyengar R. A two-state model of an enzyme with an allosteric regulator site capable of metabolizing the regulatory ligand. J Biol Chem 1980, 255:3552-3557.
    • (1980) J Biol Chem , vol.255 , pp. 3552-3557
    • Birnbaumer, L.1    Bearer, C.F.2    Iyengar, R.3
  • 44
    • 0028950255 scopus 로고
    • The twostate model of receptor activation
    • 10.1016/S0165-6147(00)88989-0, 7540781
    • Leff P. The twostate model of receptor activation. Trends Pharmacol Sci 1995, 16:89-97. 10.1016/S0165-6147(00)88989-0, 7540781.
    • (1995) Trends Pharmacol Sci , vol.16 , pp. 89-97
    • Leff, P.1
  • 45
    • 0010673662 scopus 로고
    • A modification of receptor theory
    • Stephenson RP. A modification of receptor theory. Br J Pharmacol 1956, 11:379-393.
    • (1956) Br J Pharmacol , vol.11 , pp. 379-393
    • Stephenson, R.P.1
  • 46
    • 0027665006 scopus 로고
    • Allosteric proteins: from regulatory enzymes to receptors - personal recollections
    • 10.1002/bies.950150909, 8240316
    • Changeux JP. Allosteric proteins: from regulatory enzymes to receptors - personal recollections. Bioessays 1993, 15:625-634. 10.1002/bies.950150909, 8240316.
    • (1993) Bioessays , vol.15 , pp. 625-634
    • Changeux, J.P.1
  • 47
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: a plausible model
    • 10.1016/S0022-2836(65)80285-6, 14343300
    • Monod J, Wyman J, Changeux J-P. On the nature of allosteric transitions: a plausible model. J Mol Biol 1965, 12:88-118. 10.1016/S0022-2836(65)80285-6, 14343300.
    • (1965) J Mol Biol , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.-P.3
  • 48
    • 79959334490 scopus 로고    scopus 로고
    • 50th anniversary of the word "allosteric"
    • 10.1002/pro.658, 3149185, 21574197
    • Changeux JP. 50th anniversary of the word "allosteric". Protein Sci 2011, 20:1119-1124. 10.1002/pro.658, 3149185, 21574197.
    • (2011) Protein Sci , vol.20 , pp. 1119-1124
    • Changeux, J.P.1
  • 49
    • 0001858251 scopus 로고
    • Application of a theory of enzyme specificity to protein synthesis
    • 10.1073/pnas.44.2.98, 335371, 16590179
    • Koshland DE. Application of a theory of enzyme specificity to protein synthesis. Proc Natl Acad Sci 1958, 44:98-104. 10.1073/pnas.44.2.98, 335371, 16590179.
    • (1958) Proc Natl Acad Sci , vol.44 , pp. 98-104
    • Koshland, D.E.1
  • 50
    • 84965075853 scopus 로고
    • A study of the desensitization produced by acetylcholine at the motor end-plate
    • 1363030, 13463799
    • Katz B, Thesleff S. A study of the desensitization produced by acetylcholine at the motor end-plate. J Physiol 1957, 138:63-80. 1363030, 13463799.
    • (1957) J Physiol , vol.138 , pp. 63-80
    • Katz, B.1    Thesleff, S.2
  • 52
    • 0002355204 scopus 로고
    • The use of β-haloalkylamines in the differentiation of receptors and in the determination of dissociation constants of receptor-agonist complexes
    • Furchgott RF. The use of β-haloalkylamines in the differentiation of receptors and in the determination of dissociation constants of receptor-agonist complexes. Adv Drug Res 1966, 3:21-55.
    • (1966) Adv Drug Res , vol.3 , pp. 21-55
    • Furchgott, R.F.1
  • 53
    • 0018909079 scopus 로고
    • Is prenalterol (H133/80) really a selective beta 1 adrenoceptor agonist? Tissue selectivity resulting from differences in stimulus-response relationships
    • Kenakin TP, Beek D. Is prenalterol (H133/80) really a selective beta 1 adrenoceptor agonist? Tissue selectivity resulting from differences in stimulus-response relationships. J Pharmacol Exp Ther 1980, 213:406-413.
    • (1980) J Pharmacol Exp Ther , vol.213 , pp. 406-413
    • Kenakin, T.P.1    Beek, D.2
  • 54
    • 84863224949 scopus 로고    scopus 로고
    • Development of operational models of receptor activation including constitutive receptor activity and their use to determine the efficacy of the chemokine TARC at the CC-chemokine receptor CCR4
    • 10.1111/j.1476-5381.2012.01901.x, 22335621
    • Slack RJ, Hall DA. Development of operational models of receptor activation including constitutive receptor activity and their use to determine the efficacy of the chemokine TARC at the CC-chemokine receptor CCR4. Br J Pharmacol 2012, 166:1774-1792. 10.1111/j.1476-5381.2012.01901.x, 22335621.
    • (2012) Br J Pharmacol , vol.166 , pp. 1774-1792
    • Slack, R.J.1    Hall, D.A.2
  • 55
    • 79960487917 scopus 로고    scopus 로고
    • Analysis of agonism and inverse agonism in functional assays with constitutive activity: estimation of orthosteric ligand affinity constants for active and inactive receptor states
    • 10.1124/jpet.111.179309, 3141894, 21576379
    • Ehlert FJ, Suga H, Griffin MT. Analysis of agonism and inverse agonism in functional assays with constitutive activity: estimation of orthosteric ligand affinity constants for active and inactive receptor states. J Pharmacol Exp Ther 2011, 338:671-686. 10.1124/jpet.111.179309, 3141894, 21576379.
    • (2011) J Pharmacol Exp Ther , vol.338 , pp. 671-686
    • Ehlert, F.J.1    Suga, H.2    Griffin, M.T.3
  • 56
    • 80051788130 scopus 로고    scopus 로고
    • In vitro and in vivo characterization of the novel GABAB receptor positive allosteric modulator, 2-{1-[2-(4-chlorophenyl)-5-methylpyrazolo[1,5-a]pyrimidin-7-yl]-2-piperidinyl}ethanol (CMPPE)
    • 10.1016/j.neuropharm.2011.06.024, 21756923
    • Perdona E, Costantini VJ, Tessari M, Martinelli P, Carignani C, Valerio E. In vitro and in vivo characterization of the novel GABAB receptor positive allosteric modulator, 2-{1-[2-(4-chlorophenyl)-5-methylpyrazolo[1,5-a]pyrimidin-7-yl]-2-piperidinyl}ethanol (CMPPE). Neuropharmacology 2011, 61:957-966. 10.1016/j.neuropharm.2011.06.024, 21756923.
    • (2011) Neuropharmacology , vol.61 , pp. 957-966
    • Perdona, E.1    Costantini, V.J.2    Tessari, M.3    Martinelli, P.4    Carignani, C.5    Valerio, E.6
  • 57
    • 78049414628 scopus 로고    scopus 로고
    • Matching models to data: a receptor pharmacologist's guide
    • 10.1111/j.1476-5381.2010.00879.x, 3000653, 20977467
    • Hall DA, Langmead CJ. Matching models to data: a receptor pharmacologist's guide. Br J Pharmacol 2010, 161:1276-1290. 10.1111/j.1476-5381.2010.00879.x, 3000653, 20977467.
    • (2010) Br J Pharmacol , vol.161 , pp. 1276-1290
    • Hall, D.A.1    Langmead, C.J.2
  • 59
    • 58849138430 scopus 로고    scopus 로고
    • Overlapping binding site for the endogenous agonist, small-molecule agonists, and ago-allosteric modulators on the ghrelin receptor
    • 10.1124/mol.108.049189, 18923064
    • Holst B, Frimurer TM, Mokrosinski J, Halkjaer T, Cullberg KB, Underwood CR. Overlapping binding site for the endogenous agonist, small-molecule agonists, and ago-allosteric modulators on the ghrelin receptor. Mol Pharmacol 2009, 75:44-59. 10.1124/mol.108.049189, 18923064.
    • (2009) Mol Pharmacol , vol.75 , pp. 44-59
    • Holst, B.1    Frimurer, T.M.2    Mokrosinski, J.3    Halkjaer, T.4    Cullberg, K.B.5    Underwood, C.R.6
  • 60
    • 84857732011 scopus 로고    scopus 로고
    • Discovery of 2-(2-benzoxazoyl amino)-4-aryl-5-cyanopyrimidine as negative allosteric modulators (NAMs) of metabotropic glutamate receptor 5 (mGlu5): from an artificial neural network virtual screen to an in vivo tool compound
    • 10.1002/cmdc.201100510, 3517057, 22267125
    • Mueller R, Dawson ES, Meiler J, Rodriguez AL, Chauder BA, Bates BS. Discovery of 2-(2-benzoxazoyl amino)-4-aryl-5-cyanopyrimidine as negative allosteric modulators (NAMs) of metabotropic glutamate receptor 5 (mGlu5): from an artificial neural network virtual screen to an in vivo tool compound. ChemMedChem 2012, 7:406-414. 10.1002/cmdc.201100510, 3517057, 22267125.
    • (2012) ChemMedChem , vol.7 , pp. 406-414
    • Mueller, R.1    Dawson, E.S.2    Meiler, J.3    Rodriguez, A.L.4    Chauder, B.A.5    Bates, B.S.6


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