메뉴 건너뛰기




Volumn 1422, Issue 3, 1999, Pages 207-234

Modelling G-protein-coupled receptors for drug design

Author keywords

Agonist; Antagonist; Drug design; G Protein coupled receptor; Molecular modeling; Mutagenesis

Indexed keywords

ATENOLOL; BUSPIRONE; CALCITONIN RECEPTOR; CELL SURFACE RECEPTOR; CIMETIDINE; CISAPRIDE; CYCLIC AMP RECEPTOR; DOXAZOSIN; FAMOTIDINE; GOSERELIN; GUANINE NUCLEOTIDE BINDING PROTEIN; IPRATROPIUM BROMIDE; LEUPRORELIN; LIGAND; LORATADINE; LOSARTAN; LOSARTAN POTASSIUM; MEMBRANE PROTEIN; METABOTROPIC RECEPTOR; METOPROLOL; NIZATIDINE; OLANZAPINE; PHEROMONE; RANITIDINE; RHODOPSIN; RISPERIDONE; SALBUTAMOL; SALMETEROL; SALMETEROL XINAFOATE; SUMATRIPTAN; SUMATRIPTAN SUCCINATE; TERAZOSIN; UNINDEXED DRUG;

EID: 0032735188     PISSN: 03044157     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0304-4157(99)00006-4     Document Type: Review
Times cited : (229)

References (140)
  • 2
    • 0032563291 scopus 로고    scopus 로고
    • G protein-coupled receptors III. New roles for receptor kinases and arrestins in receptor signalling and desensitization
    • R.J. Lefkowitz, G protein-coupled receptors III. New roles for receptor kinases and arrestins in receptor signalling and desensitization, J. Biol. Chem. 273 (1998) 18677-18680.
    • (1998) J. Biol. Chem. , vol.273 , pp. 18677-18680
    • Lefkowitz, R.J.1
  • 3
    • 0028174033 scopus 로고
    • Fingerprinting G-protein-coupled receptors
    • T.K. Attwood, J.B. Findlay, Fingerprinting G-protein-coupled receptors, Protein Eng. 7 (1994) 195-203.
    • (1994) Protein Eng. , vol.7 , pp. 195-203
    • Attwood, T.K.1    Findlay, J.B.2
  • 4
    • 0025716272 scopus 로고
    • The structure of bacteriorhodopsin and its relevance to the visual opsins and other seven-helix G-protein coupled receptors
    • R. Henderson, G.F. Schertler, The structure of bacteriorhodopsin and its relevance to the visual opsins and other seven-helix G-protein coupled receptors, Phil. Trans. R. Soc. Lond. Ser. B Biol. Sci. 326 (1990) 379-389.
    • (1990) Phil. Trans. R. Soc. Lond. Ser. B Biol. Sci. , vol.326 , pp. 379-389
    • Henderson, R.1    Schertler, G.F.2
  • 5
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
    • R. Henderson, J.M. Baldwin, T.A. Ceska, F. Zemlin, E. Beckmann, K.H. Downing, Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy, J. Mol. Biol. 213 (1990) 899-929.
    • (1990) J. Mol. Biol. , vol.213 , pp. 899-929
    • Henderson, R.1    Baldwin, J.M.2    Ceska, T.A.3    Zemlin, F.4    Beckmann, E.5    Downing, K.H.6
  • 6
    • 0027375519 scopus 로고
    • Structural relationship of streptavidin to the calycin protein superfamily
    • D.R. Flower, Structural relationship of streptavidin to the calycin protein superfamily, FEBS Lett. 333 (1993) 99-102.
    • (1993) FEBS Lett. , vol.333 , pp. 99-102
    • Flower, D.R.1
  • 7
    • 0027506279 scopus 로고
    • Structure and sequence relationships in the lipocalins and related proteins
    • D.R. Flower, A.C. North, T.K. Attwood, Structure and sequence relationships in the lipocalins and related proteins, Protein Sci. 2 (1993) 753-761.
    • (1993) Protein Sci. , vol.2 , pp. 753-761
    • Flower, D.R.1    North, A.C.2    Attwood, T.K.3
  • 8
    • 0028338534 scopus 로고
    • GCRDb: A G-protein-coupled receptor database
    • L.F. Kolakowski Jr., GCRDb: a G-protein-coupled receptor database, Recept. Channels 2 (1995) 1-7.
    • (1995) Recept. Channels , vol.2 , pp. 1-7
    • Kolakowski L.F., Jr.1
  • 9
    • 0028909714 scopus 로고
    • Receptors and G-proteins as primary components of transmembrane signal transduction
    • T. Gudermann, B. Nurnberg, G. Schultz, Receptors and G-proteins as primary components of transmembrane signal transduction, J. Mol. Med. 73 (1995) 51-63.
    • (1995) J. Mol. Med. , vol.73 , pp. 51-63
    • Gudermann, T.1    Nurnberg, B.2    Schultz, G.3
  • 10
    • 0345376003 scopus 로고    scopus 로고
    • Data provided by 'IMS Health'
    • Data provided by 'IMS Health'
  • 11
    • 0030671337 scopus 로고    scopus 로고
    • Protein-coupled receptors: A neglected opportunity for pioneer drug discovery
    • J.M. Stadel, S. Wilson, D.J. Bergsma, G. Orphan, Protein-coupled receptors: a neglected opportunity for pioneer drug discovery, Trends Pharmacol. Sci. 18 (1997) 430-437.
    • (1997) Trends Pharmacol. Sci. , vol.18 , pp. 430-437
    • Stadel, J.M.1    Wilson, S.2    Bergsma, D.J.3    Orphan, G.4
  • 12
    • 0032577581 scopus 로고    scopus 로고
    • Chemokine receptors: Keys to AIDS pathogenesis?
    • D.R. Littman, Chemokine receptors: keys to AIDS pathogenesis?, Cell 93 (1998) 677-680.
    • (1998) Cell , vol.93 , pp. 677-680
    • Littman, D.R.1
  • 13
    • 0032482954 scopus 로고    scopus 로고
    • The area code hypothesis revisited - Olfactory receptors and other related transmembrane receptors may function as the last digits in a cell surface code for assembling embryos
    • W.J. Dreyer, The area code hypothesis revisited - olfactory receptors and other related transmembrane receptors may function as the last digits in a cell surface code for assembling embryos, Proc. Natl. Acad. Sci. USA 95 (1998) 9072-9077.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 9072-9077
    • Dreyer, W.J.1
  • 15
    • 0027933763 scopus 로고
    • Locating ligand-binding sites in 7TM receptors by protein engineering
    • T.W. Schwartz, Locating ligand-binding sites in 7TM receptors by protein engineering, Curr. Opin. Biotechnol. 5 (1994) 434-444.
    • (1994) Curr. Opin. Biotechnol. , vol.5 , pp. 434-444
    • Schwartz, T.W.1
  • 17
    • 0001699495 scopus 로고    scopus 로고
    • Structural characterisation and binding sites of G-protein coupled receptors
    • A.G. Beck-Sickinger, Structural characterisation and binding sites of G-protein coupled receptors, Drug Discovery Today 1 (1996) 502-513.
    • (1996) Drug Discovery Today , vol.1 , pp. 502-513
    • Beck-Sickinger, A.G.1
  • 18
    • 0032581639 scopus 로고    scopus 로고
    • G-protein coupled receptors - Models, mutagenesis, and drug design
    • J.A. Bikker, S. Trumppkallmeyer, C. Humblet, G-protein coupled receptors - models, mutagenesis, and drug design, J. Med. Chem. 41 (1998) 2911-2927.
    • (1998) J. Med. Chem. , vol.41 , pp. 2911-2927
    • Bikker, J.A.1    Trumppkallmeyer, S.2    Humblet, C.3
  • 20
    • 0031840579 scopus 로고    scopus 로고
    • G protein-coupled receptors in silico
    • F. Horn, G. Vriend, G protein-coupled receptors in silico, J. Mol. Med. 76 (1998) 464-468.
    • (1998) J. Mol. Med. , vol.76 , pp. 464-468
    • Horn, F.1    Vriend, G.2
  • 21
    • 0026071374 scopus 로고
    • Multiple sequence alignment of protein families showing low sequence homology: A methodological approach using database pattern-matching discriminators for G-protein-linked receptors
    • T.K. Attwood, E.E. Eliopoulos, J.B.C. Findlay, Multiple sequence alignment of protein families showing low sequence homology: a methodological approach using database pattern-matching discriminators for G-protein-linked receptors, Gene 98 (1991) 153-159.
    • (1991) Gene , vol.98 , pp. 153-159
    • Attwood, T.K.1    Eliopoulos, E.E.2    Findlay, J.B.C.3
  • 22
    • 0027480350 scopus 로고
    • Design of a discriminating fingerprint for G-protein-coupled receptors
    • T.K. Attwood, J.B.C. Findlay, Design of a discriminating fingerprint for G-protein-coupled receptors, Protein Eng. 6 (1993) 167-176.
    • (1993) Protein Eng. , vol.6 , pp. 167-176
    • Attwood, T.K.1    Findlay, J.B.C.2
  • 24
    • 0029164276 scopus 로고
    • Potential ligand-binding residues in rat olfactory receptors identified by correlated mutation analysis
    • M.S. Singer, L. Oliveira, G. Vriend, G.M. Shepherd, Potential ligand-binding residues in rat olfactory receptors identified by correlated mutation analysis, Recept. Channels 3 (1995) 89-95.
    • (1995) Recept. Channels , vol.3 , pp. 89-95
    • Singer, M.S.1    Oliveira, L.2    Vriend, G.3    Shepherd, G.M.4
  • 26
    • 0026598960 scopus 로고
    • Human growth hormone and extracellular domain of its receptor: Crystal structure of the complex
    • A.M. De Vos, M. Ultsch, A.A. Kossiakoff, Human growth hormone and extracellular domain of its receptor: crystal structure of the complex, Science 255 (1992) 306.
    • (1992) Science , vol.255 , pp. 306
    • De Vos, A.M.1    Ultsch, M.2    Kossiakoff, A.A.3
  • 27
    • 0030589099 scopus 로고    scopus 로고
    • Structures of the extracellular domain of the type I tumor necrosis factor receptor
    • J.H. Naismith, T.Q. Devine, T. Kohno, S.R. Sprang, Structures of the extracellular domain of the type I tumor necrosis factor receptor, Structure 4 (1996) 1251-1262.
    • (1996) Structure , vol.4 , pp. 1251-1262
    • Naismith, J.H.1    Devine, T.Q.2    Kohno, T.3    Sprang, S.R.4
  • 28
    • 0022348605 scopus 로고
    • Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3 angstroms resolution
    • J. Deisenhofer, O. Epp, K. Miki, R. Huber, H. Michel, Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3 angstroms resolution, Nature 318 (1985) 618.
    • (1985) Nature , vol.318 , pp. 618
    • Deisenhofer, J.1    Epp, O.2    Miki, K.3    Huber, R.4    Michel, H.5
  • 29
    • 0026737314 scopus 로고
    • Structure of porin refined at 1.8 angstroms resolution
    • M.S. Weiss, G.E. Schulz, Structure of porin refined at 1.8 angstroms resolution, J. Mol. Biol. 227 (1992) 493.
    • (1992) J. Mol. Biol. , vol.227 , pp. 493
    • Weiss, M.S.1    Schulz, G.E.2
  • 30
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
    • R. Henderson, J.M. Baldwin, T.A. Ceska, F. Zemlin, E. Beckmann, K.H. Downing, Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy, J. Mol. Biol. 213 (1990) 899.
    • (1990) J. Mol. Biol. , vol.213 , pp. 899
    • Henderson, R.1    Baldwin, J.M.2    Ceska, T.A.3    Zemlin, F.4    Beckmann, E.5    Downing, K.H.6
  • 31
    • 0030864048 scopus 로고    scopus 로고
    • X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases
    • E. Pebay-Peyroula, G. Rummel, J.P. Rosenbusch, E.M. Landau, X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases, Science 277 (1997) 1676-1681.
    • (1997) Science , vol.277 , pp. 1676-1681
    • Pebay-Peyroula, E.1    Rummel, G.2    Rosenbusch, J.P.3    Landau, E.M.4
  • 32
    • 0029142564 scopus 로고
    • Overexpression of integral membrane proteins for structural studies
    • R. Grisshammer, C.G. Tate, Overexpression of integral membrane proteins for structural studies, Q. Rev. Biophys. 28 (1995) 315-422.
    • (1995) Q. Rev. Biophys. , vol.28 , pp. 315-422
    • Grisshammer, R.1    Tate, C.G.2
  • 33
    • 0026506038 scopus 로고
    • Two-dimensional crystallization of membrane proteins
    • W. Kuhlbrandt, Two-dimensional crystallization of membrane proteins, Q. Rev. Biophys. 25 (1992) 1-49.
    • (1992) Q. Rev. Biophys. , vol.25 , pp. 1-49
    • Kuhlbrandt, W.1
  • 34
    • 0031260369 scopus 로고    scopus 로고
    • Quantitative evaluation of neurotensin receptor purification by immobilized metal affinity chromatography
    • R. Grisshammer, J. Tucker, Quantitative evaluation of neurotensin receptor purification by immobilized metal affinity chromatography, Protein Expr. Purif. 11 (1997) 53-60.
    • (1997) Protein Expr. Purif. , vol.11 , pp. 53-60
    • Grisshammer, R.1    Tucker, J.2
  • 35
    • 0032493354 scopus 로고    scopus 로고
    • Lipid nanotubes as substrates for helical crystallization of macromolecules
    • E. Wilson-Kubalek, R. Brown, H. Celia, R. Milligan, Lipid nanotubes as substrates for helical crystallization of macromolecules, Proc. Natl. Acad. Sci. USA 95 (1998) 8040-8045.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 8040-8045
    • Wilson-Kubalek, E.1    Brown, R.2    Celia, H.3    Milligan, R.4
  • 36
    • 0032560585 scopus 로고    scopus 로고
    • Submolecular resolution of single macromolecules with atomic force microscopy
    • D. Czajkowsky, Z. Shao, Submolecular resolution of single macromolecules with atomic force microscopy, FEBS Lett. 430 (1998) 51-54.
    • (1998) FEBS Lett. , vol.430 , pp. 51-54
    • Czajkowsky, D.1    Shao, Z.2
  • 37
    • 0028962270 scopus 로고
    • Low resolution structure of bovine rhodopsin determined by electron cryo-microscopy
    • V.M. Unger, G.F. Schertler, Low resolution structure of bovine rhodopsin determined by electron cryo-microscopy, Biophys. J. 68 (1995) 1776-1786.
    • (1995) Biophys. J. , vol.68 , pp. 1776-1786
    • Unger, V.M.1    Schertler, G.F.2
  • 38
    • 0029556994 scopus 로고
    • Projection structure of frog rhodopsin in two crystal forms
    • G.F. Schertler, P.A. Hargrave, Projection structure of frog rhodopsin in two crystal forms, Proc. Natl. Acad. Sci. USA 92 (1995) 11578-11582.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 11578-11582
    • Schertler, G.F.1    Hargrave, P.A.2
  • 40
  • 41
    • 0031565726 scopus 로고    scopus 로고
    • An alpha-carbon template for the transmembrane helices in the rhodopsin family of G-protein-coupled receptors
    • J.M. Baldwin, G.F. Schertler, V.M. Unger, An alpha-carbon template for the transmembrane helices in the rhodopsin family of G-protein-coupled receptors, J. Mol. Biol. 272 (1997) 144-164.
    • (1997) J. Mol. Biol. , vol.272 , pp. 144-164
    • Baldwin, J.M.1    Schertler, G.F.2    Unger, V.M.3
  • 42
    • 0028812838 scopus 로고
    • Structure of the third cytoplasmic loop of bovine rhodopsin
    • P.L. Yeagle, J.L. Alderfer, A.D. Albert, Structure of the third cytoplasmic loop of bovine rhodopsin, Biochemistry 34 (1995) 14621-14625.
    • (1995) Biochemistry , vol.34 , pp. 14621-14625
    • Yeagle, P.L.1    Alderfer, J.L.2    Albert, A.D.3
  • 43
    • 0029391341 scopus 로고
    • Structure of the carboxy-terminal domain of bovine rhodopsin
    • P.L. Yeagle, J.L. Alderfer, A.D. Albert, Structure of the carboxy-terminal domain of bovine rhodopsin, Nat. Struct. Biol. 2 (1995) 832-834.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 832-834
    • Yeagle, P.L.1    Alderfer, J.L.2    Albert, A.D.3
  • 44
    • 0030964858 scopus 로고    scopus 로고
    • The first and second cytoplasmic loops of the G-protein receptor, rhodopsin, independently form beta-turns
    • P.L. Yeagle, J.L. Alderfer, A.C. Salloum, L. Ali, A.D. Albert, The first and second cytoplasmic loops of the G-protein receptor, rhodopsin, independently form beta-turns, Biochemistry 36 (1997) 3864-3869.
    • (1997) Biochemistry , vol.36 , pp. 3864-3869
    • Yeagle, P.L.1    Alderfer, J.L.2    Salloum, A.C.3    Ali, L.4    Albert, A.D.5
  • 45
    • 0030841110 scopus 로고    scopus 로고
    • Three-dimensional structure of the cytoplasmic face of the G protein receptor rhodopsin
    • P.L. Yeagle, J.L. Alderfer, A.D. Albert, Three-dimensional structure of the cytoplasmic face of the G protein receptor rhodopsin, Biochemistry 36 (1997) 9649-9654.
    • (1997) Biochemistry , vol.36 , pp. 9649-9654
    • Yeagle, P.L.1    Alderfer, J.L.2    Albert, A.D.3
  • 46
    • 0031026207 scopus 로고    scopus 로고
    • The structure of MCP-1 in two crystal forms provides a rare example of variable quaternary interactions
    • J. Lubkowski, G. Bujacz, L. Boque, P.J. Domaille, T.M. Handel, A. Wlodawer, The structure of MCP-1 in two crystal forms provides a rare example of variable quaternary interactions, Nat. Struct. Biol. 4 (1996) 64-69.
    • (1996) Nat. Struct. Biol. , vol.4 , pp. 64-69
    • Lubkowski, J.1    Bujacz, G.2    Boque, L.3    Domaille, P.J.4    Handel, T.M.5    Wlodawer, A.6
  • 49
    • 0032474767 scopus 로고    scopus 로고
    • G-protein diseases furnish a model for the turn-on switch
    • T. Iiri, Z. Farfel, H.R. Bourne, G-protein diseases furnish a model for the turn-on switch, Nature 394 (1998) 35-38.
    • (1998) Nature , vol.394 , pp. 35-38
    • Iiri, T.1    Farfel, Z.2    Bourne, H.R.3
  • 50
    • 0025667804 scopus 로고
    • Three-dimensional modelling of G protein-linked receptors
    • J.B.C. Findlay, E.E. Eliopoulos, Three-dimensional modelling of G protein-linked receptors, Trends Pharmacol. Sci. 11 (1991) 492-499.
    • (1991) Trends Pharmacol. Sci. , vol.11 , pp. 492-499
    • Findlay, J.B.C.1    Eliopoulos, E.E.2
  • 51
    • 0025881062 scopus 로고
    • Three-dimensional models of neurotransmitter G- Binding protein-coupled receptors
    • M.F. Hibert, S. Trumpp-Kallmeyer, A. Bruinvels, J. Hoflack, Three-dimensional models of neurotransmitter G- binding protein-coupled receptors, Mol. Pharmacol. 40 (1991) 8-15.
    • (1991) Mol. Pharmacol. , vol.40 , pp. 8-15
    • Hibert, M.F.1    Trumpp-Kallmeyer, S.2    Bruinvels, A.3    Hoflack, J.4
  • 52
    • 0026457758 scopus 로고
    • A model of the adrenergic beta-2 receptor and binding sites for agonist and antagonist
    • X.Q. Lewell, A model of the adrenergic beta-2 receptor and binding sites for agonist and antagonist, Drug Des. Discov. 9 (1992) 29-48.
    • (1992) Drug Des. Discov. , vol.9 , pp. 29-48
    • Lewell, X.Q.1
  • 53
    • 0027979326 scopus 로고
    • Re-evaluation of bacteriorhodopsin as a model for G protein-coupled receptors
    • J. Hoflack, S. Trumpp-Kallmeyer, M. Hibert, Re-evaluation of bacteriorhodopsin as a model for G protein-coupled receptors, Trends Pharmacol. Sci. 15 (1994) 7-9.
    • (1994) Trends Pharmacol. Sci. , vol.15 , pp. 7-9
    • Hoflack, J.1    Trumpp-Kallmeyer, S.2    Hibert, M.3
  • 55
    • 0026517309 scopus 로고
    • On the use of the transmembrane domain of bacteriorhodopsin as a template for modelling the three-dimensional structure of guanine nucleotide-binding regulatory protein-coupled receptors
    • L. Pardo, J.A. Ballesteros, R. Osman, H. Weinstein, On the use of the transmembrane domain of bacteriorhodopsin as a template for modelling the three-dimensional structure of guanine nucleotide-binding regulatory protein-coupled receptors, Proc. Natl. Acad. Sci. USA 89 (1992) 4009-4012.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4009-4012
    • Pardo, L.1    Ballesteros, J.A.2    Osman, R.3    Weinstein, H.4
  • 56
    • 0030194704 scopus 로고    scopus 로고
    • An analysis of the conserved residues between halobacterial retinal proteins and G-protein coupled receptors: Implications for GPCR modelling
    • T.G. Metzger, M.G. Paterlini, P.S. Portoghese, D.M. Ferguson, An analysis of the conserved residues between halobacterial retinal proteins and G-protein coupled receptors: implications for GPCR modelling, J. Chem. Inf. Comput. Sci. 36 (1996) 857-861.
    • (1996) J. Chem. Inf. Comput. Sci. , vol.36 , pp. 857-861
    • Metzger, T.G.1    Paterlini, M.G.2    Portoghese, P.S.3    Ferguson, D.M.4
  • 59
    • 0030831364 scopus 로고    scopus 로고
    • A new approach to docking in the beta 2-adrenergic receptor that exploits the domain structure of G-protein-coupled receptors
    • P.R. Gouldson, C.R. Snell, C.A. Reynolds, A new approach to docking in the beta 2-adrenergic receptor that exploits the domain structure of G-protein-coupled receptors, J. Med. Chem. 40 (1997) 3871-3886.
    • (1997) J. Med. Chem. , vol.40 , pp. 3871-3886
    • Gouldson, P.R.1    Snell, C.R.2    Reynolds, C.A.3
  • 60
    • 0027506471 scopus 로고
    • The probable arrangement of the helices in G protein-coupled receptors
    • J.M. Baldwin, The probable arrangement of the helices in G protein-coupled receptors, EMBO J. 12 (1993) 1693-1703.
    • (1993) EMBO J. , vol.12 , pp. 1693-1703
    • Baldwin, J.M.1
  • 61
    • 0030998038 scopus 로고    scopus 로고
    • The transmembrane 7-alpha-bundle of rhodopsin: Distance geometry calculations with hydrogen bonding constraints
    • I.D. Pogozheva, A.L. Lomize, H.I. Mosberg, The transmembrane 7-alpha-bundle of rhodopsin: distance geometry calculations with hydrogen bonding constraints, Biophys. J. 72 (1997) 1963.
    • (1997) Biophys. J. , vol.72 , pp. 1963
    • Pogozheva, I.D.1    Lomize, A.L.2    Mosberg, H.I.3
  • 62
    • 0032575763 scopus 로고    scopus 로고
    • Combined biophysical and biochemical information confirms arrangement of transmembrane helices visible from the three-dimensional map of frog rhodopsin
    • P. Herzyk, R.E. Hubbard, Combined biophysical and biochemical information confirms arrangement of transmembrane helices visible from the three-dimensional map of frog rhodopsin, J. Mol. Biol. 281 (1998) 741-754.
    • (1998) J. Mol. Biol. , vol.281 , pp. 741-754
    • Herzyk, P.1    Hubbard, R.E.2
  • 63
    • 0032382964 scopus 로고    scopus 로고
    • General procedure for building the transmembrane domains of G-protein coupled receptors
    • J.J. Perez, M. Filizola, M.A. Caritenifarina, General procedure for building the transmembrane domains of G-protein coupled receptors, J. Math. Chem. 23 (1998) 229-238.
    • (1998) J. Math. Chem. , vol.23 , pp. 229-238
    • Perez, J.J.1    Filizola, M.2    Caritenifarina, M.A.3
  • 64
    • 0345375999 scopus 로고    scopus 로고
    • F. Campagne, J.M. Bernassau, B. Maigret
    • http://www.lctn.u-nancy.fr/viseur/viseur.html; F. Campagne, J.M. Bernassau, B. Maigret.
  • 65
    • 0032011940 scopus 로고    scopus 로고
    • Bundle - A program for building the transmembrane domains of G-protein-coupled receptors
    • M. Filizola, J.J. Perez, M. Cartenifarina, Bundle - a program for building the transmembrane domains of G-protein-coupled receptors, J. Computer-Aided Mol. Design 12 (1998) 111-118.
    • (1998) J. Computer-Aided Mol. Design , vol.12 , pp. 111-118
    • Filizola, M.1    Perez, J.J.2    Cartenifarina, M.3
  • 66
    • 0028829235 scopus 로고
    • Automated method for modelling seven-helix transmembrane receptors from experimental data
    • P. Herzyk, R.E. Hubbard, Automated method for modelling seven-helix transmembrane receptors from experimental data, Biophys. J. 69 (1995) 2419-2442.
    • (1995) Biophys. J. , vol.69 , pp. 2419-2442
    • Herzyk, P.1    Hubbard, R.E.2
  • 67
    • 0030451549 scopus 로고    scopus 로고
    • Automated modelling of the transmembrane region of G-protein coupled receptor by Swiss-model
    • M.C. Peitsch, P. Herzyk, T.N. Wells, R.E. Hubbard, Automated modelling of the transmembrane region of G-protein coupled receptor by Swiss-model, Recept. Channels 4 (1996) 161-164.
    • (1996) Recept. Channels , vol.4 , pp. 161-164
    • Peitsch, M.C.1    Herzyk, P.2    Wells, T.N.3    Hubbard, R.E.4
  • 68
    • 0029845242 scopus 로고    scopus 로고
    • A database of mutants and effects of site-directed mutagenesis experiments on G-protein coupled receptors
    • K. Kristiansen, S.G. Dahl, Ø. Edvardsen, A database of mutants and effects of site-directed mutagenesis experiments on G-protein coupled receptors, Proteins 26 (1996) 81-94.
    • (1996) Proteins , vol.26 , pp. 81-94
    • Kristiansen, K.1    Dahl, S.G.2    Edvardsen, Ø.3
  • 69
    • 0024519931 scopus 로고
    • Structural basis of beta-adrenergic receptor function
    • C.D. Strader, I.S. Sigal, R.A. Dixon, Structural basis of beta-adrenergic receptor function, FASEB J. 3 (1989) 1825-1832.
    • (1989) FASEB J. , vol.3 , pp. 1825-1832
    • Strader, C.D.1    Sigal, I.S.2    Dixon, R.A.3
  • 70
    • 0026059456 scopus 로고
    • Biophysical and genetic analysis of the ligand-binding site of the beta-adrenoceptor
    • M.R. Tota, M.R. Candelore, R.A. Dixon, C.D. Strader, Biophysical and genetic analysis of the ligand-binding site of the beta-adrenoceptor, Trends Pharmacol. Sci. 12 (1991) 4-6.
    • (1991) Trends Pharmacol. Sci. , vol.12 , pp. 4-6
    • Tota, M.R.1    Candelore, M.R.2    Dixon, R.A.3    Strader, C.D.4
  • 71
    • 0026548156 scopus 로고
    • In vitro mutagenesis and the search for structure-function relationships among G protein-coupled receptors
    • T.M. Savarese, C.M. Fraser, In vitro mutagenesis and the search for structure-function relationships among G protein-coupled receptors, Biochem. J. 283 (1992) 1-19.
    • (1992) Biochem. J. , vol.283 , pp. 1-19
    • Savarese, T.M.1    Fraser, C.M.2
  • 72
    • 0028339899 scopus 로고
    • Functional mapping of the ligand binding sites of G-protein coupled receptors
    • T.M. Fong, C.D. Strader, Functional mapping of the ligand binding sites of G-protein coupled receptors, Med. Res. Rev. 14 (1994) 387-399.
    • (1994) Med. Res. Rev. , vol.14 , pp. 387-399
    • Fong, T.M.1    Strader, C.D.2
  • 75
    • 0023740863 scopus 로고
    • Conserved aspartic acid residues 79 and 113 of the beta-adrenergic receptor have different roles in receptor function
    • C.D. Strader, I.S. Sigal, M.R. Candelore, E. Rands, W.S. Hill, R.A. Dixon, Conserved aspartic acid residues 79 and 113 of the beta-adrenergic receptor have different roles in receptor function, J. Biol. Chem. 63 (1988) 10267-10271.
    • (1988) J. Biol. Chem. , vol.63 , pp. 10267-10271
    • Strader, C.D.1    Sigal, I.S.2    Candelore, M.R.3    Rands, E.4    Hill, W.S.5    Dixon, R.A.6
  • 76
    • 0024344941 scopus 로고
    • Identification of two serine residues involved in agonist activation of the beta-adrenergic receptor
    • C.D. Strader, M.R. Candelore, W.S. Hill, I.S. Sigal, R.A. Dixon, Identification of two serine residues involved in agonist activation of the beta-adrenergic receptor, J. Biol. Chem. 264 (1989) 13572-13578.
    • (1989) J. Biol. Chem. , vol.264 , pp. 13572-13578
    • Strader, C.D.1    Candelore, M.R.2    Hill, W.S.3    Sigal, I.S.4    Dixon, R.A.5
  • 77
    • 0025036339 scopus 로고
    • Characterization of the binding domain of the beta-adrenergic receptor with the fluorescent antagonist carazolol. Evidence for a buried ligand binding site
    • M.R. Tota, C.D. Strader, Characterization of the binding domain of the beta-adrenergic receptor with the fluorescent antagonist carazolol. Evidence for a buried ligand binding site, J. Biol. Chem. 265 (1990) 16891-16897.
    • (1990) J. Biol. Chem. , vol.265 , pp. 16891-16897
    • Tota, M.R.1    Strader, C.D.2
  • 78
    • 0029838206 scopus 로고    scopus 로고
    • Involvement of Asn-293 in stereospecific agonist recognition and in activation of the beta 2-adrenergic receptor
    • K. Wieland, H.M. Zuurmond, C. Krasel, A.P. Ijzerman, M.J. Lohse, Involvement of Asn-293 in stereospecific agonist recognition and in activation of the beta 2-adrenergic receptor, Proc. Natl. Acad. Sci. USA 93 (1996) 9276-9281.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 9276-9281
    • Wieland, K.1    Zuurmond, H.M.2    Krasel, C.3    Ijzerman, A.P.4    Lohse, M.J.5
  • 79
    • 0024426708 scopus 로고
    • A single amino acid substitution in the beta-adrenergic receptor promotes partial agonist activity from antagonists
    • C.D. Strader, M.R. Candelore, W.S. Hill, R.A. Dixon, I.S. Sigal, A single amino acid substitution in the beta-adrenergic receptor promotes partial agonist activity from antagonists, J. Biol. Chem. 64 (1989) 16470-16477.
    • (1989) J. Biol. Chem. , vol.64 , pp. 16470-16477
    • Strader, C.D.1    Candelore, M.R.2    Hill, W.S.3    Dixon, R.A.4    Sigal, I.S.5
  • 80
    • 0027296745 scopus 로고
    • Amino acid substitutions at position 312 in the seventh hydrophobic segment of the beta 2-adrenergic receptor modify ligand-binding specificity
    • S. Suryanarayana, B.K. Kobilka, Amino acid substitutions at position 312 in the seventh hydrophobic segment of the beta 2-adrenergic receptor modify ligand-binding specificity, Mol. Pharmacol. 44 (1993) 111-114.
    • (1993) Mol. Pharmacol. , vol.44 , pp. 111-114
    • Suryanarayana, S.1    Kobilka, B.K.2
  • 81
    • 0031939636 scopus 로고    scopus 로고
    • The role of the seventh transmembrane region in high affinity binding of a beta 2-selective agonist TA-2005
    • H. Kikkawa, M. Isogaya, T. Nagao, H. Kurose, The role of the seventh transmembrane region in high affinity binding of a beta 2-selective agonist TA-2005, Mol. Pharmacol. 53 (1998) 128-134.
    • (1998) Mol. Pharmacol. , vol.53 , pp. 128-134
    • Kikkawa, H.1    Isogaya, M.2    Nagao, T.3    Kurose, H.4
  • 82
    • 0029841642 scopus 로고    scopus 로고
    • Sustained activation of a G protein-coupled receptor via 'anchored' agonist binding. Molecular localization of the salmeterol exosite within the 2-adrenergic receptor
    • S.A. Green, A.P. Spasoff, R.A. Coleman, M. Johnson, S.B. Liggett, Sustained activation of a G protein-coupled receptor via 'anchored' agonist binding. Molecular localization of the salmeterol exosite within the 2-adrenergic receptor, J. Biol. Chem. 271 (1996) 24029-24035.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24029-24035
    • Green, S.A.1    Spasoff, A.P.2    Coleman, R.A.3    Johnson, M.4    Liggett, S.B.5
  • 83
    • 0030247623 scopus 로고    scopus 로고
    • Exosites: Their current status, and their relevance to the duration of action of long-acting beta 2-adrenoceptor agonists
    • R.A. Coleman, M. Johnson, A.T. Niais, C.J. Vardey, Exosites: their current status, and their relevance to the duration of action of long-acting beta 2-adrenoceptor agonists, Trends Pharmacol. Sci. 17 (1996) 324-330.
    • (1996) Trends Pharmacol. Sci. , vol.17 , pp. 324-330
    • Coleman, R.A.1    Johnson, M.2    Niais, A.T.3    Vardey, C.J.4
  • 85
    • 0029916331 scopus 로고    scopus 로고
    • The ligand binding site of the angiotensin AT1 receptor
    • L. Hunyady, T. Balla, K.J. Catt, The ligand binding site of the angiotensin AT1 receptor, Trends Pharmacol. Sci. 17 (1996) 135-140.
    • (1996) Trends Pharmacol. Sci. , vol.17 , pp. 135-140
    • Hunyady, L.1    Balla, T.2    Catt, K.J.3
  • 86
    • 0031010320 scopus 로고    scopus 로고
    • A review of mutagenesis studies of angiotensin II type 1 receptor, the three-dimensional receptor model in search of the agonist and antagonist binding site and the hypothesis of a receptor activation mechanism
    • Y. Inoue, N. Nakamura, T. Inagami, A review of mutagenesis studies of angiotensin II type 1 receptor, the three-dimensional receptor model in search of the agonist and antagonist binding site and the hypothesis of a receptor activation mechanism, J. Hypertens. 15 (1997) 703-714.
    • (1997) J. Hypertens. , vol.15 , pp. 703-714
    • Inoue, Y.1    Nakamura, N.2    Inagami, T.3
  • 87
    • 0026666733 scopus 로고
    • Identification of amino acid residues of rat angiotensin II receptor for ligand binding by site directed mutagenesis
    • Y. Yamano, K. Ohyama, S. Chaki, D.F. Guo, T. Inagami, Identification of amino acid residues of rat angiotensin II receptor for ligand binding by site directed mutagenesis, Biochem. Biophys. Res. Commun. 187 (1992) 1426-1431.
    • (1992) Biochem. Biophys. Res. Commun. , vol.187 , pp. 1426-1431
    • Yamano, Y.1    Ohyama, K.2    Chaki, S.3    Guo, D.F.4    Inagami, T.5
  • 88
    • 0027988149 scopus 로고
    • Identification of peptide binding residues in the extracellular domains of the AT1 receptor
    • S.A. Hjorth, H.T. Schambye, W.J. Greenlee, T.W. Schwartz, Identification of peptide binding residues in the extracellular domains of the AT1 receptor, J. Biol. Chem. 269 (1994) 30953-30959.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30953-30959
    • Hjorth, S.A.1    Schambye, H.T.2    Greenlee, W.J.3    Schwartz, T.W.4
  • 89
    • 0028977998 scopus 로고
    • The docking of Arg2 of angiotensin II with Asp281 of AT1 receptor is essential for full agonism
    • Y.H. Feng, K. Noda, Y. Saad, X.P. Liu, A. Husain, S.S. Karnik, The docking of Arg2 of angiotensin II with Asp281 of AT1 receptor is essential for full agonism, J. Biol. Chem. 270 (1995) 12846-12850.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12846-12850
    • Feng, Y.H.1    Noda, K.2    Saad, Y.3    Liu, X.P.4    Husain, A.5    Karnik, S.S.6
  • 90
    • 0028973086 scopus 로고
    • Interaction of Phe8 of angiotensin II with Lys199 and His256 of AT1 receptor in agonist activation
    • K. Noda, Y. Saad, S.S. Karnik, Interaction of Phe8 of angiotensin II with Lys199 and His256 of AT1 receptor in agonist activation, J. Biol. Chem. 270 (1995) 28511-28514.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28511-28514
    • Noda, K.1    Saad, Y.2    Karnik, S.S.3
  • 91
    • 0028237894 scopus 로고
    • Differential structural requirements for specific binding of nonpeptide and peptide antagonists to the AT1 angiotensin receptor. Identification of amino acid residues that determine binding of the antihypertensive drug losartan
    • H. Ji, M. Leung, Y. Zhang, K.J. Catt, K. Sandberg, Differential structural requirements for specific binding of nonpeptide and peptide antagonists to the AT1 angiotensin receptor. Identification of amino acid residues that determine binding of the antihypertensive drug losartan, J. Biol. Chem. 269 (1994) 16533-16536.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16533-16536
    • Ji, H.1    Leung, M.2    Zhang, Y.3    Catt, K.J.4    Sandberg, K.5
  • 93
    • 0028926576 scopus 로고
    • Tetrazole and carboxylate groups of angiotensin receptor antagonists bind to the same subsite by different mechanisms
    • K. Noda, Y. Saad, A. Kinoshita, T.P. Boyle, R.M. Graham, A. Husain, S.S. Karnik, Tetrazole and carboxylate groups of angiotensin receptor antagonists bind to the same subsite by different mechanisms, J. Biol. Chem. 270 (1995) 2284-2289.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2284-2289
    • Noda, K.1    Saad, Y.2    Kinoshita, A.3    Boyle, T.P.4    Graham, R.M.5    Husain, A.6    Karnik, S.S.7
  • 94
    • 0028969511 scopus 로고
    • Interaction between the nonpeptide angiotensin antagonist SKF-108,566 and histidine 256 (HisVI:16) of the angiotensin type 1 receptor
    • H.T. Schambye, S.A. Hjorth, J. Weinstock, T.W. Schwartz, Interaction between the nonpeptide angiotensin antagonist SKF-108,566 and histidine 256 (HisVI:16) of the angiotensin type 1 receptor, Mol. Pharmacol. 47 (1995) 425-431.
    • (1995) Mol. Pharmacol. , vol.47 , pp. 425-431
    • Schambye, H.T.1    Hjorth, S.A.2    Weinstock, J.3    Schwartz, T.W.4
  • 95
    • 0030466265 scopus 로고    scopus 로고
    • Interaction of biphenylimidazole and imidazoleacrylic acid nonpeptide antagonists with valine 108 in TM III of the AT1 angiotensin receptor
    • V. Nirula, W. Zheng, R. Sothinathan, K. Sandberg, Interaction of biphenylimidazole and imidazoleacrylic acid nonpeptide antagonists with valine 108 in TM III of the AT1 angiotensin receptor, Br. J. Pharmacol. 119 (1996) 1505-1507.
    • (1996) Br. J. Pharmacol. , vol.119 , pp. 1505-1507
    • Nirula, V.1    Zheng, W.2    Sothinathan, R.3    Sandberg, K.4
  • 96
    • 0029021945 scopus 로고
    • Genetic transfer of a nonpeptide antagonist binding site to a previously unresponsive angiotensin receptor
    • H. Ji, W. Zheng, Y. Zhang, K.J. Catt, K. Sandberg, Genetic transfer of a nonpeptide antagonist binding site to a previously unresponsive angiotensin receptor, Proc. Natl. Acad. Sci. USA 92 (1995) 9240-9244.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9240-9244
    • Ji, H.1    Zheng, W.2    Zhang, Y.3    Catt, K.J.4    Sandberg, K.5
  • 97
    • 0030574024 scopus 로고    scopus 로고
    • Identification of nonconserved amino acids in the AT1 receptor which comprise a general binding site for biphenylimidazole antagonists
    • V. Nirula, W. Zheng, K. Krishnamurthi, K. Sandberg, Identification of nonconserved amino acids in the AT1 receptor which comprise a general binding site for biphenylimidazole antagonists, FEBS Lett. 394 (1996) 361-364.
    • (1996) FEBS Lett. , vol.394 , pp. 361-364
    • Nirula, V.1    Zheng, W.2    Krishnamurthi, K.3    Sandberg, K.4
  • 98
    • 0032512713 scopus 로고    scopus 로고
    • Shared determinants of receptor binding for subtype selective, and dual endothelin-angiotensin antagonists on the AT1 angiotensin II receptor
    • D. Dascal, V. Nirula, K. Lawus, S.E. Yoo, T.F. Walsh, K. Sandberg, Shared determinants of receptor binding for subtype selective, and dual endothelin-angiotensin antagonists on the AT1 angiotensin II receptor, FEBS Lett. 423 (1998) 15-18.
    • (1998) FEBS Lett. , vol.423 , pp. 15-18
    • Dascal, D.1    Nirula, V.2    Lawus, K.3    Yoo, S.E.4    Walsh, T.F.5    Sandberg, K.6
  • 100
    • 0028674972 scopus 로고
    • Structural model of antagonist and agonist binding to the angiotensin II, AT1 subtype, G protein coupled receptor
    • D.J. Underwood, C.D. Strader, R. Rivero, A.A. Patchett, W. Greenlee, K. Prendergast, Structural model of antagonist and agonist binding to the angiotensin II, AT1 subtype, G protein coupled receptor, Chem. Biol. 1 (1994) 211-221.
    • (1994) Chem. Biol. , vol.1 , pp. 211-221
    • Underwood, D.J.1    Strader, C.D.2    Rivero, R.3    Patchett, A.A.4    Greenlee, W.5    Prendergast, K.6
  • 101
    • 0019332167 scopus 로고
    • How different amino acid sequences determine similar protein structures: The structure and evolutionary dynamics of the globins
    • A.M. Lesk, C. Chothia, How different amino acid sequences determine similar protein structures: the structure and evolutionary dynamics of the globins, J. Mol. Biol. 136 (1980) 225-270.
    • (1980) J. Mol. Biol. , vol.136 , pp. 225-270
    • Lesk, A.M.1    Chothia, C.2
  • 102
    • 0028953765 scopus 로고
    • Measuring diversity - Experimental-design of combinatorial libraries for drug discovery
    • E.J. Martin, J.M. Blaney, M.A. Siani, D.C. Spellmeyer, A.K. Wong, W.H. Moos, Measuring diversity - experimental-design of combinatorial libraries for drug discovery, J. Med. Chem. 38 (1995) 1431-1436.
    • (1995) J. Med. Chem. , vol.38 , pp. 1431-1436
    • Martin, E.J.1    Blaney, J.M.2    Siani, M.A.3    Spellmeyer, D.C.4    Wong, A.K.5    Moos, W.H.6
  • 103
    • 0029074391 scopus 로고
    • Library of libraries: Approach to synthetic combinatorial library design and screening of 'pharmacophore' motifs
    • N.F. Sepetov, V. Krchnak, M. Stankova, S. Wade, K.S. Lam, M. Lebl, Library of libraries: approach to synthetic combinatorial library design and screening of 'pharmacophore' motifs, Proc. Natl. Acad. Sci. USA 92 (1995) 5426-5430.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 5426-5430
    • Sepetov, N.F.1    Krchnak, V.2    Stankova, M.3    Wade, S.4    Lam, K.S.5    Lebl, M.6
  • 104
    • 0031569368 scopus 로고    scopus 로고
    • Serendipity meets precision: The integration of structure-based drug design and combinatorial chemistry for efficient drug discovery
    • F.R. Salemme, J. Spurlino, R. Bone, Serendipity meets precision: the integration of structure-based drug design and combinatorial chemistry for efficient drug discovery, Structure 5 (1997) 319-324.
    • (1997) Structure , vol.5 , pp. 319-324
    • Salemme, F.R.1    Spurlino, J.2    Bone, R.3
  • 107
    • 0032514481 scopus 로고    scopus 로고
    • Peptidomimetic growth hormone secretagogues - Design considerations and therapeutic potential
    • R.P. Nargund, A.A. Patchett, M.A. Bach, M.G. Murphy, R.G. Smith, Peptidomimetic growth hormone secretagogues - design considerations and therapeutic potential, J. Med. Chem. 41 (1998) 3103-3127.
    • (1998) J. Med. Chem. , vol.41 , pp. 3103-3127
    • Nargund, R.P.1    Patchett, A.A.2    Bach, M.A.3    Murphy, M.G.4    Smith, R.G.5
  • 109
    • 0001486718 scopus 로고    scopus 로고
    • The arrangement of the transmembrane helices in the secretin receptor family of G-protein coupled receptors
    • D. Donnelly, The arrangement of the transmembrane helices in the secretin receptor family of G-protein coupled receptors, FEBS Lett. 409 (1997) 431-436.
    • (1997) FEBS Lett. , vol.409 , pp. 431-436
    • Donnelly, D.1
  • 110
    • 0029819599 scopus 로고    scopus 로고
    • Homology modelling of metabotropic glutamate receptors. (mGluRs) structural motifs affecting binding modes and pharmacological profile of mGluR1 agonists and competitive antagonists
    • G. Costantino, R. Pellicciari, Homology modelling of metabotropic glutamate receptors. (mGluRs) structural motifs affecting binding modes and pharmacological profile of mGluR1 agonists and competitive antagonists, J. Med. Chem. 39 (1996) 3998-4006.
    • (1996) J. Med. Chem. , vol.39 , pp. 3998-4006
    • Costantino, G.1    Pellicciari, R.2
  • 111
    • 0032541084 scopus 로고    scopus 로고
    • G protein coupled receptors II. Mechanism of agonist activation
    • U. Gether, B.K. Kobilka, G protein coupled receptors II. Mechanism of agonist activation, J. Biol. Chem. 273 (1998) 17979-17982.
    • (1998) J. Biol. Chem. , vol.273 , pp. 17979-17982
    • Gether, U.1    Kobilka, B.K.2
  • 112
    • 0030938936 scopus 로고    scopus 로고
    • G-protein-coupled receptors: Molecular mechanisms involved in receptor activation and selectivity of G-protein recognition
    • J. Wess, G-protein-coupled receptors: molecular mechanisms involved in receptor activation and selectivity of G-protein recognition, FASEB J. 11 (1997) 346-354.
    • (1997) FASEB J. , vol.11 , pp. 346-354
    • Wess, J.1
  • 113
    • 0029907599 scopus 로고    scopus 로고
    • Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin
    • D.L. Farrens, C. Altenbach, K. Yang, W.L. Hubbell, H.G. Khorana, Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin, Science 274 (1996) 768-770.
    • (1996) Science , vol.274 , pp. 768-770
    • Farrens, D.L.1    Altenbach, C.2    Yang, K.3    Hubbell, W.L.4    Khorana, H.G.5
  • 114
    • 0029878713 scopus 로고    scopus 로고
    • Mechanistic hypotheses for the activation of G-protein-coupled receptors
    • T.M. Fong, Mechanistic hypotheses for the activation of G-protein-coupled receptors, Cell. Signal. 8 (1996) 217-224.
    • (1996) Cell. Signal. , vol.8 , pp. 217-224
    • Fong, T.M.1
  • 115
    • 0030859541 scopus 로고    scopus 로고
    • Agonists induce conformational changes in transmembrane domains III and VI of the β2 adrenoceptor
    • U. Gether, S. Lin, P. Ghanouni, J.A. Ballesteros, H. Weinstein, B.K. Kobilka, Agonists induce conformational changes in transmembrane domains III and VI of the β2 adrenoceptor, EMBO J. 16 (1997) 6737-6747.
    • (1997) EMBO J. , vol.16 , pp. 6737-6747
    • Gether, U.1    Lin, S.2    Ghanouni, P.3    Ballesteros, J.A.4    Weinstein, H.5    Kobilka, B.K.6
  • 118
    • 0031437841 scopus 로고    scopus 로고
    • Measurement of agonist efficacy using an alpha2A-adrenoceptor-Gi1alpha fusion protein
    • A. Wise, I.C. Carr, D.A. Groarke, G. Milligan, Measurement of agonist efficacy using an alpha2A-adrenoceptor-Gi1alpha fusion protein, FEBS Lett. 419 (1997) 141-146.
    • (1997) FEBS Lett. , vol.419 , pp. 141-146
    • Wise, A.1    Carr, I.C.2    Groarke, D.A.3    Milligan, G.4
  • 119
    • 0032562288 scopus 로고    scopus 로고
    • Agonist occupation of an alpha2A-adrenoreceptor-Gi1alpha fusion protein results in activation of both receptor-linked and endogenous Gi proteins. Comparisons of their contributions to GTPase activity and signal transduction and analysis of receptor-G protein activation stoichiometry
    • A.R. Burt, M. Sautel, M.A. Wilson, S. Rees, A. Wise, G. Milligan, Agonist occupation of an alpha2A-adrenoreceptor-Gi1alpha fusion protein results in activation of both receptor-linked and endogenous Gi proteins. Comparisons of their contributions to GTPase activity and signal transduction and analysis of receptor-G protein activation stoichiometry, J. Biol. Chem. 273 (1998) 10367-10375.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10367-10375
    • Burt, A.R.1    Sautel, M.2    Wilson, M.A.3    Rees, S.4    Wise, A.5    Milligan, G.6
  • 121
    • 0028348690 scopus 로고
    • Agonist-specific coupling of a cloned Drosophila octopamine/tyramine receptor to multiple second messenger systems
    • S. Robb, T.R. Cheek, F.L. Hannan, L.M. Hall, J.M. Midgley, P.D. Evans, Agonist-specific coupling of a cloned Drosophila octopamine/tyramine receptor to multiple second messenger systems, EMBO J. 13 (1994) 1325-1330.
    • (1994) EMBO J. , vol.13 , pp. 1325-1330
    • Robb, S.1    Cheek, T.R.2    Hannan, F.L.3    Hall, L.M.4    Midgley, J.M.5    Evans, P.D.6
  • 122
    • 0030049488 scopus 로고    scopus 로고
    • Constitutive activation of a single effector pathway: Evidence for multiple activation states of a G protein-coupled receptor
    • D.M. Perez, J. Hwa, R. Gaivin, M. Mathur, F. Brown, R.M. Graham, Constitutive activation of a single effector pathway: evidence for multiple activation states of a G protein-coupled receptor, Mol. Pharmacol. 49 (1996) 112-122.
    • (1996) Mol. Pharmacol. , vol.49 , pp. 112-122
    • Perez, D.M.1    Hwa, J.2    Gaivin, R.3    Mathur, M.4    Brown, F.5    Graham, R.M.6
  • 123
    • 0030474049 scopus 로고    scopus 로고
    • What can we learn from molecular recognition in protein-ligand complexes for the design of new drugs
    • in English
    • H.J. Bohm, G. Klebe, What can we learn from molecular recognition in protein-ligand complexes for the design of new drugs., Angewandte Chemie Int. Ed. (in English) 35 (22) (1996) 2589-2614.
    • (1996) Angewandte Chemie Int. Ed. , vol.35 , Issue.22 , pp. 2589-2614
    • Bohm, H.J.1    Klebe, G.2
  • 124
    • 0027385177 scopus 로고
    • Matching chemistry and shape in molecular docking
    • B.K. Shoichet, I.D. Kuntz, Matching chemistry and shape in molecular docking, Protein Eng. 6 (1993) 223-232.
    • (1993) Protein Eng. , vol.6 , pp. 223-232
    • Shoichet, B.K.1    Kuntz, I.D.2
  • 125
    • 0029705324 scopus 로고    scopus 로고
    • Docking of flexible ligands: Applications of AutoDock
    • D.S. Goodsell, G.M. Morris, A.J. Olson, Docking of flexible ligands: applications of AutoDock, J. Mol. Recogn. 9 (1996) 1-5.
    • (1996) J. Mol. Recogn. , vol.9 , pp. 1-5
    • Goodsell, D.S.1    Morris, G.M.2    Olson, A.J.3
  • 126
    • 0030599010 scopus 로고    scopus 로고
    • Predicting receptor-ligand interactions by an incremental construction algorithm
    • M. Rarey, B. Kramer, T. Lengauer, G. Klebe, Predicting receptor-ligand interactions by an incremental construction algorithm, J. Mol. Biol. 261 (1996) 470-489.
    • (1996) J. Mol. Biol. , vol.261 , pp. 470-489
    • Rarey, M.1    Kramer, B.2    Lengauer, T.3    Klebe, G.4
  • 127
    • 0027522358 scopus 로고
    • Structure-based discovery of inhibitors of thymidylate synthase
    • B.K. Shoichet, R.M. Stroud, D.V. Santi, I.D. Kuntz, K.M. Perry, Structure-based discovery of inhibitors of thymidylate synthase, Science 259 (1993) 1445-1450.
    • (1993) Science , vol.259 , pp. 1445-1450
    • Shoichet, B.K.1    Stroud, R.M.2    Santi, D.V.3    Kuntz, I.D.4    Perry, K.M.5
  • 128
    • 0032571380 scopus 로고    scopus 로고
    • An example of a protein ligand found by database mining: Description of the docking method and its verification by a 2.3 a X-ray structure of a thrombin-ligand complex
    • P. Burkhard, P. Taylor, M.D. Walkinshaw, An example of a protein ligand found by database mining: description of the docking method and its verification by a 2.3 A X-ray structure of a thrombin-ligand complex, J. Mol. Biol. 277 (1998) 449-466.
    • (1998) J. Mol. Biol. , vol.277 , pp. 449-466
    • Burkhard, P.1    Taylor, P.2    Walkinshaw, M.D.3
  • 129
    • 0028861437 scopus 로고
    • Elusive affinities
    • J. Janin, Elusive affinities, Proteins 21 (1995) 30-39.
    • (1995) Proteins , vol.21 , pp. 30-39
    • Janin, J.1
  • 130
    • 0031178505 scopus 로고    scopus 로고
    • Constructing protein models for ligand-receptor binding thermodynamic simulations
    • J. Tokarski, A.J. Hopfinger, Constructing protein models for ligand-receptor binding thermodynamic simulations, J. Chem. Inf. Comput. Sci. 37 (1997) 779-791.
    • (1997) J. Chem. Inf. Comput. Sci. , vol.37 , pp. 779-791
    • Tokarski, J.1    Hopfinger, A.J.2
  • 131
    • 0030815956 scopus 로고    scopus 로고
    • A virtual screening approach applied to the search for trypanothione reductase inhibitors
    • D. Horvath, A virtual screening approach applied to the search for trypanothione reductase inhibitors, J. Med. Chem. 40 (1997) 2412-2423.
    • (1997) J. Med. Chem. , vol.40 , pp. 2412-2423
    • Horvath, D.1
  • 132
    • 0029000922 scopus 로고
    • Prediction of drug binding affinities by comparative binding energy analysis
    • A.R. Ortiz, M.T. Pisabarro, F. Gago, R.C. Wade, Prediction of drug binding affinities by comparative binding energy analysis, J. Med. Chem. 38 (1995) 2681-2691.
    • (1995) J. Med. Chem. , vol.38 , pp. 2681-2691
    • Ortiz, A.R.1    Pisabarro, M.T.2    Gago, F.3    Wade, R.C.4
  • 133
    • 0029995624 scopus 로고    scopus 로고
    • VALIDATE - A new method for the receptor-based prediction of binding affinities of novel ligands
    • R.D. Head, M.L. Smythe, T.I. Oprea, C.L. Waller, S.M. Green, G.R. Marshall, VALIDATE - a new method for the receptor-based prediction of binding affinities of novel ligands, J. Am. Che. Soc. 118 (1996) 3959-3969.
    • (1996) J. Am. Che. Soc. , vol.118 , pp. 3959-3969
    • Head, R.D.1    Smythe, M.L.2    Oprea, T.I.3    Waller, C.L.4    Green, S.M.5    Marshall, G.R.6
  • 134
    • 0027413349 scopus 로고
    • Pseudo-receptor modelling: A new concept for the three-dimensional construction of receptor binding sites
    • A. Vedani, P. Zbinden, J.P. Snyder, Pseudo-receptor modelling: a new concept for the three-dimensional construction of receptor binding sites, J. Receptor Res. 13 (1993) 163-177.
    • (1993) J. Receptor Res. , vol.13 , pp. 163-177
    • Vedani, A.1    Zbinden, P.2    Snyder, J.P.3
  • 135
    • 0031954203 scopus 로고    scopus 로고
    • PRGEN -pseudoreceptor modelling using receptor-mediated ligand alignment and pharmacophore equilibration
    • P. Zbinden, M. Dobler, G. Folkers, A. Vedani, PRGEN -pseudoreceptor modelling using receptor-mediated ligand alignment and pharmacophore equilibration, Quant. Struc.-Activ. Relatsh. 17 (1998) 122-130.
    • (1998) Quant. Struc.-Activ. Relatsh. , vol.17 , pp. 122-130
    • Zbinden, P.1    Dobler, M.2    Folkers, G.3    Vedani, A.4
  • 136
    • 0027994253 scopus 로고
    • On the interaction of the aromatic part of dopaminergic agonists with the receptor
    • D. Kocjan, On the interaction of the aromatic part of dopaminergic agonists with the receptor, J. Med. Chem. 37 (1994) 2851-2855.
    • (1994) J. Med. Chem. , vol.37 , pp. 2851-2855
    • Kocjan, D.1
  • 137
    • 0028801099 scopus 로고
    • Novel deltorphin heptapeptide analogs with potent delta agonist, delta antagonist, or mixed mu antagonist/delta agonist properties
    • Y. Sasaki, T. Chiba, Novel deltorphin heptapeptide analogs with potent delta agonist, delta antagonist, or mixed mu antagonist/delta agonist properties, J. Med. Chem. 38 (1995) 3995-3999.
    • (1995) J. Med. Chem. , vol.38 , pp. 3995-3999
    • Sasaki, Y.1    Chiba, T.2
  • 138
    • 0030846176 scopus 로고    scopus 로고
    • Pyrrolidine-3-carboxylic acids as endothelin antagonists. 2. Sulfonamide-based ETA/ETB mixed antagonists
    • H.S. Jae, M. Winn, D.B. Dixon, K.C. Marsh, B. Nguyen, T.J. Opgenorth, T.W. von Geldern, Pyrrolidine-3-carboxylic acids as endothelin antagonists. 2. Sulfonamide-based ETA/ETB mixed antagonists, J. Med. Chem. 40 (1997) 3217-3227.
    • (1997) J. Med. Chem. , vol.40 , pp. 3217-3227
    • Jae, H.S.1    Winn, M.2    Dixon, D.B.3    Marsh, K.C.4    Nguyen, B.5    Opgenorth, T.J.6    Von Geldern, T.W.7
  • 140
    • 0031459284 scopus 로고    scopus 로고
    • ALTER: Eclectic management of molecular structure data
    • D.R. Flower, ALTER: eclectic management of molecular structure data, J. Mol. Graphics Model. 15 (1997) 161-169.
    • (1997) J. Mol. Graphics Model. , vol.15 , pp. 161-169
    • Flower, D.R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.