메뉴 건너뛰기




Volumn 32, Issue , 2003, Pages 375-397

The crystallographic model of rhodopsin and its use in studies of other G protein-coupled receptors

Author keywords

Homology models; Phototransduction; Signal transduction; Transmembrane protein; Vision

Indexed keywords

G PROTEIN COUPLED RECEPTOR; GUANINE NUCLEOTIDE BINDING PROTEIN; RHODOPSIN;

EID: 0037494099     PISSN: 10568700     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.biophys.32.110601.142520     Document Type: Review
Times cited : (110)

References (126)
  • 1
    • 0030810419 scopus 로고    scopus 로고
    • A distance measurement between specific sites on the cytoplasmic surface of bovine rhodopsin in rod outer segment disk membranes
    • Albert AD, Watts A, Spooner P, Groebner G, Young J, Yeagle PL. 1997. A distance measurement between specific sites on the cytoplasmic surface of bovine rhodopsin in rod outer segment disk membranes. Biochim. Biophys. Acta 1328:74-82
    • (1997) Biochim. Biophys. Acta , vol.1328 , pp. 74-82
    • Albert, A.D.1    Watts, A.2    Spooner, P.3    Groebner, G.4    Young, J.5    Yeagle, P.L.6
  • 2
    • 0035951097 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: Mapping light-dependent changes in distance between residue 65 in helix TM1 and residues in the sequence 306-319 at the cytoplasmic end of helix TM7 and in helix HS
    • Altenbach C, Cai KW, Klein-Seetharaman J, Khorana HG, Hubbell WL. 2001. Structure and function in rhodopsin: mapping light-dependent changes in distance between residue 65 in helix TM1 and residues in the sequence 306-319 at the cytoplasmic end of helix TM7 and in helix HS. Biochemistry 40:15483-92
    • (2001) Biochemistry , vol.40 , pp. 15483-15492
    • Altenbach, C.1    Cai, K.W.2    Klein-Seetharaman, J.3    Khorana, H.G.4    Hubbell, W.L.5
  • 3
    • 0035951062 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: Mapping light-dependent changes in distance between residue 316 in helix 8 and residues in the sequence 60-75, covering the cytoplasmic end of helices TM1 and TM2 and their connection loop CL1
    • Altenbach C, Klein-Seetharaman J, Cai KW, Khorana HG, Hubbell WL. 2001. Structure and function in rhodopsin: mapping light-dependent changes in distance between residue 316 in helix 8 and residues in the sequence 60-75, covering the cytoplasmic end of helices TM1 and TM2 and their connection loop CL1. Biochemistry 40:15493-500
    • (2001) Biochemistry , vol.40 , pp. 15493-15500
    • Altenbach, C.1    Klein-Seetharaman, J.2    Cai, K.W.3    Khorana, H.G.4    Hubbell, W.L.5
  • 4
    • 0036217072 scopus 로고    scopus 로고
    • The lutropin/choriogonadotropin receptor, a 2002 perspective
    • Ascoli M, Fanelli F, Segaloff DL. 2002. The lutropin/choriogonadotropin receptor, a 2002 perspective. Endocr. Rev. 23:141-74
    • (2002) Endocr. Rev. , vol.23 , pp. 141-174
    • Ascoli, M.1    Fanelli, F.2    Segaloff, D.L.3
  • 5
    • 0031565726 scopus 로고    scopus 로고
    • An alpha-carbon template for the transmembrane helices in the rhodopsin family of G-protein-coupled receptors
    • Baldwin JM, Schertler GFX, Unger VM. 1997. An alpha-carbon template for the transmembrane helices in the rhodopsin family of G-protein-coupled receptors. J. Mol. Biol. 272:144-64
    • (1997) J. Mol. Biol. , vol.272 , pp. 144-164
    • Baldwin, J.M.1    Schertler, G.F.X.2    Unger, V.M.3
  • 6
    • 0034801665 scopus 로고    scopus 로고
    • G protein-coupled receptor drug discovery: Implications from the crystal structure of rhodopsin
    • Ballesteros J, Palczewski K. 2001. G protein-coupled receptor drug discovery: implications from the crystal structure of rhodopsin. Curr. Opin. Drug Discov. Dev. 4:561-74
    • (2001) Curr. Opin. Drug Discov. Dev. , vol.4 , pp. 561-574
    • Ballesteros, J.1    Palczewski, K.2
  • 7
    • 0035800850 scopus 로고    scopus 로고
    • Activation of the beta(2)-adrenergic receptor involves disruption of an ionic lock between the cytoplasmic ends of transmembrane segments 3 and 6
    • Ballesteros JA, Jensen AD, Liapakis G, Rasmussen SGF, Shi L, et al. 2001. Activation of the beta(2)-adrenergic receptor involves disruption of an ionic lock between the cytoplasmic ends of transmembrane segments 3 and 6. J. Biol. Chem. 276:29171-77
    • (2001) J. Biol. Chem. , vol.276 , pp. 29171-29177
    • Ballesteros, J.A.1    Jensen, A.D.2    Liapakis, G.3    Rasmussen, S.G.F.4    Shi, L.5
  • 8
    • 0034948696 scopus 로고    scopus 로고
    • Structural mimicry in G protein-coupled receptors: Implications of the high-resolution structure of rhodopsin for structure-function analysis of rhodopsin-like receptors
    • Ballesteros JA, Shi L, Javitch JA. 2001. Structural mimicry in G protein-coupled receptors: implications of the high-resolution structure of rhodopsin for structure-function analysis of rhodopsin-like receptors. Mol. Pharmacol. 60:1-19
    • (2001) Mol. Pharmacol. , vol.60 , pp. 1-19
    • Ballesteros, J.A.1    Shi, L.2    Javitch, J.A.3
  • 9
    • 77957055780 scopus 로고
    • Integrated methods for the construction of three-dimensional models and computational probing of structure-function relations in G protein coupled receptors
    • Ballesteros JA, Weinstein H. 1995. Integrated methods for the construction of three-dimensional models and computational probing of structure-function relations in G protein coupled receptors. Methods Neurosci. 25:366-428
    • (1995) Methods Neurosci. , vol.25 , pp. 366-428
    • Ballesteros, J.A.1    Weinstein, H.2
  • 10
    • 0035899176 scopus 로고    scopus 로고
    • Fluorosulfonyl-and bis-(beta-chloroethyl)amino-phenylamino functionalized pyrazolo 4,3-e1, 2,4-triazolo 1,5-c pyrimidine derivatives: Irreversible antagonists at the human A(3) adenosine receptor and molecular modeling studies
    • Baraldi PG, Cacciari B, Moro S, Romagnoli R, Ji XD, et al. 2001. Fluorosulfonyl-and bis-(beta-chloroethyl)amino-phenylamino functionalized pyrazolo 4,3-e1, 2,4-triazolo 1,5-c pyrimidine derivatives: irreversible antagonists at the human A(3) adenosine receptor and molecular modeling studies. J. Med. Chem. 44:2735-42
    • (2001) J. Med. Chem. , vol.44 , pp. 2735-2742
    • Baraldi, P.G.1    Cacciari, B.2    Moro, S.3    Romagnoli, R.4    Ji, X.D.5
  • 11
    • 0037075142 scopus 로고    scopus 로고
    • Synthesis, biological activity, and molecular modeling investigation of new pyrazolo 4,3-e-1,2,4-triazolo 1,5-c pyrimidine derivatives as human A(3) adenosine receptor antagonists
    • Baraldi PG, Cacciari B, Moro S, Spalluto G, Pastorin G, et al. 2002. Synthesis, biological activity, and molecular modeling investigation of new pyrazolo 4,3-e-1,2,4-triazolo 1,5-c pyrimidine derivatives as human A(3) adenosine receptor antagonists. J. Med. Chem. 45:770-80
    • (2002) J. Med. Chem. , vol.45 , pp. 770-780
    • Baraldi, P.G.1    Cacciari, B.2    Moro, S.3    Spalluto, G.4    Pastorin, G.5
  • 17
    • 0344972891 scopus 로고    scopus 로고
    • Absolute sense of twist of the C12-C13 bond of the retinal chromophore in rhodopsin - Semiempirical and nonempirical calculations of chiroptical data
    • Buss V, Kolster K, Terstegen F, Vahrenhorst R. 1998. Absolute sense of twist of the C12-C13 bond of the retinal chromophore in rhodopsin - semiempirical and nonempirical calculations of chiroptical data. Angew. Chem. Int. Ed. 37:1893-95
    • (1998) Angew. Chem. Int. Ed. , vol.37 , pp. 1893-1895
    • Buss, V.1    Kolster, K.2    Terstegen, F.3    Vahrenhorst, R.4
  • 18
    • 0035940464 scopus 로고    scopus 로고
    • Probing the dark state tertiary structure in the cytoplasmic domain of rhodopsin: Proximities between amino acids deduced from spontaneous disulfide bond formation between cysteine pairs engineered in cytoplasmic loops 1, 3, and 4
    • Cai KW, Klein-Seetharaman J, Altenbach C, Hubbell WL, Khorana HG. 2001. Probing the dark state tertiary structure in the cytoplasmic domain of rhodopsin: proximities between amino acids deduced from spontaneous disulfide bond formation between cysteine pairs engineered in cytoplasmic loops 1, 3, and 4. Biochemistry 40:12479-85
    • (2001) Biochemistry , vol.40 , pp. 12479-12485
    • Cai, K.W.1    Klein-Seetharaman, J.2    Altenbach, C.3    Hubbell, W.L.4    Khorana, H.G.5
  • 20
    • 0033982348 scopus 로고    scopus 로고
    • Solution structure of the sixth transmembrane helix of the G-protein-coupled receptor, rhodopsin
    • Chopra A, Yeagle PL, Alderfer JA, Albert AD. 2000. Solution structure of the sixth transmembrane helix of the G-protein-coupled receptor, rhodopsin. Biochim. Biophys. Acta 1463:1-5
    • (2000) Biochim. Biophys. Acta , vol.1463 , pp. 1-5
    • Chopra, A.1    Yeagle, P.L.2    Alderfer, J.A.3    Albert, A.D.4
  • 21
    • 0037133525 scopus 로고    scopus 로고
    • NMR structure of the second intracellular loop of the alpha 2A adrenergic receptor: Evidence for a novel cytoplasmic helix
    • Chung DA, Zuiderweg ERP, Fowler CB, Soyer OS, Mosberg HI, Neubig RR. 2002. NMR structure of the second intracellular loop of the alpha 2A adrenergic receptor: evidence for a novel cytoplasmic helix. Biochemistry 41:3596-604
    • (2002) Biochemistry , vol.41 , pp. 3596-3604
    • Chung, D.A.1    Zuiderweg, E.R.P.2    Fowler, C.B.3    Soyer, O.S.4    Mosberg, H.I.5    Neubig, R.R.6
  • 22
    • 0035037874 scopus 로고    scopus 로고
    • Determination of amino acid residues that are accessible from the ligand binding crevice in the seventh transmembrane-spanning region of the human A(1) adenosine receptor
    • Dawson ES, Wells JN. 2001. Determination of amino acid residues that are accessible from the ligand binding crevice in the seventh transmembrane-spanning region of the human A(1) adenosine receptor. Mol. Pharmacol. 59:1187-95
    • (2001) Mol. Pharmacol. , vol.59 , pp. 1187-1195
    • Dawson, E.S.1    Wells, J.N.2
  • 24
    • 0034901067 scopus 로고    scopus 로고
    • Characterization of the type A cholecystokinin receptor hormone-binding domain: Use of contrasting and complementary methodologies
    • Ding XQ, Miller LJ. 2001. Characterization of the type A cholecystokinin receptor hormone-binding domain: use of contrasting and complementary methodologies. Peptides 22:1223-28
    • (2001) Peptides , vol.22 , pp. 1223-1228
    • Ding, X.Q.1    Miller, L.J.2
  • 25
    • 0036233457 scopus 로고    scopus 로고
    • Refinement of the conformation of a critical region of charge-charge interaction between cholecystokinin and its receptor
    • Ding XQ, Pinon DI, Furse KE, Lybrand TP, Miller LJ. 2002. Refinement of the conformation of a critical region of charge-charge interaction between cholecystokinin and its receptor. Mol. Pharmacol. 61:1041-52
    • (2002) Mol. Pharmacol. , vol.61 , pp. 1041-1052
    • Ding, X.Q.1    Pinon, D.I.2    Furse, K.E.3    Lybrand, T.P.4    Miller, L.J.5
  • 26
    • 0033592726 scopus 로고    scopus 로고
    • High-resolution X-ray structure of an early intermediate in the bacteriorhodopsin photocycle
    • Edman K, Nollert P, Royant A, Belrhali H, Pebay-Peyroula E, et al. 1999. High-resolution X-ray structure of an early intermediate in the bacteriorhodopsin photocycle. Nature 401:822-26
    • (1999) Nature , vol.401 , pp. 822-826
    • Edman, K.1    Nollert, P.2    Royant, A.3    Belrhali, H.4    Pebay-Peyroula, E.5
  • 27
    • 0034792566 scopus 로고    scopus 로고
    • Magic angle spinning nuclear magnetic resonance of isotopically labeled rhodopsin
    • Eilers M, Ying WW, Reeves PJ, Khorana HG, Smith SO. 2002. Magic angle spinning nuclear magnetic resonance of isotopically labeled rhodopsin. Methods Enzymol. 343:212-22
    • (2002) Methods Enzymol. , vol.343 , pp. 212-222
    • Eilers, M.1    Ying, W.W.2    Reeves, P.J.3    Khorana, H.G.4    Smith, S.O.5
  • 28
    • 0035800798 scopus 로고    scopus 로고
    • Single amino acid substitutions and deletions that alter the G protein coupling properties of the V2 vasopressin receptor identified in yeast by receptor random mutagenesis
    • Erlenbach I, Kostenis E, Schmidt C, Serradeil-Le Gal C, Raufaste D, et al. 2001. Single amino acid substitutions and deletions that alter the G protein coupling properties of the V2 vasopressin receptor identified in yeast by receptor random mutagenesis. J. Biol. Chem. 276:29382-92
    • (2001) J. Biol. Chem. , vol.276 , pp. 29382-29392
    • Erlenbach, I.1    Kostenis, E.2    Schmidt, C.3    Serradeil-Le Gal, C.4    Raufaste, D.5
  • 29
    • 18544378433 scopus 로고    scopus 로고
    • The biologically crucial C terminus of cholecystokinin and the non-peptide agonist SR-146,131 share a common binding site in the human CCK1 receptor - Evidence for a crucial role of Met-121 in the activation process
    • Escrieut C, Gigoux V, Archer E, Verrier S, Maigret B, et al. 2002. The biologically crucial C terminus of cholecystokinin and the non-peptide agonist SR-146,131 share a common binding site in the human CCK1 receptor - evidence for a crucial role of Met-121 in the activation process. J. Biol. Chem. 277:7546-55
    • (2002) J. Biol. Chem. , vol.277 , pp. 7546-7555
    • Escrieut, C.1    Gigoux, V.2    Archer, E.3    Verrier, S.4    Maigret, B.5
  • 31
    • 0034864258 scopus 로고    scopus 로고
    • Lutropin receptor function: Insights from natural, engineered, and computer-simulated mutations
    • Fanelli F, Themmen APN, Puett D. 2001. Lutropin receptor function: insights from natural, engineered, and computer-simulated mutations. IUBMB Life 51:149-55
    • (2001) IUBMB Life , vol.51 , pp. 149-155
    • Fanelli, F.1    Themmen, A.P.N.2    Puett, D.3
  • 34
    • 0035957911 scopus 로고    scopus 로고
    • Molecular interactions of cyclam and bicyclam non-peptide antagonists with the CXCR4 chemokine receptor
    • Gerlach LO, Skerlj RT, Bridger GJ, Schwartz TW. 2001. Molecular interactions of cyclam and bicyclam non-peptide antagonists with the CXCR4 chemokine receptor. J. Biol. Chem. 276:14153-60
    • (2001) J. Biol. Chem. , vol.276 , pp. 14153-14160
    • Gerlach, L.O.1    Skerlj, R.T.2    Bridger, G.J.3    Schwartz, T.W.4
  • 35
    • 0035117505 scopus 로고    scopus 로고
    • Minireview: Insights into G protein-coupled receptor function using molecular models
    • Gershengorn MC, Osman R. 2001. Minireview: insights into G protein-coupled receptor function using molecular models. Endocrinology 142:2-10
    • (2001) Endocrinology , vol.142 , pp. 2-10
    • Gershengorn, M.C.1    Osman, R.2
  • 36
    • 0032541084 scopus 로고    scopus 로고
    • G protein-coupled receptors. II. Mechanism of agonist activation
    • Gether U, Kobilka BK. 1998. G protein-coupled receptors. II. Mechanism of agonist activation. J. Biol. Chem. 273:17979-82
    • (1998) J. Biol. Chem. , vol.273 , pp. 17979-17982
    • Gether, U.1    Kobilka, B.K.2
  • 37
    • 0037046144 scopus 로고    scopus 로고
    • Intermolecular interactions between cholecystokinin-8 and the third extracellular loop of the cholecystokinin-2 receptor
    • Giragossian C, Mierke DF. 2002. Intermolecular interactions between cholecystokinin-8 and the third extracellular loop of the cholecystokinin-2 receptor. Biochemistry 41:4560-66
    • (2002) Biochemistry , vol.41 , pp. 4560-4566
    • Giragossian, C.1    Mierke, D.F.2
  • 39
    • 0035918313 scopus 로고    scopus 로고
    • The TXP motif in the second transmembrane helix of CCR5 - A structural determinant of chemokine-induced activation
    • Govaerts C, Blanpain C, Deupi X, Ballet S, Ballesteros JA, et al. 2001. The TXP motif in the second transmembrane helix of CCR5 - a structural determinant of chemokine-induced activation. J. Biol. Chem. 276:13217-25
    • (2001) J. Biol. Chem. , vol.276 , pp. 13217-13225
    • Govaerts, C.1    Blanpain, C.2    Deupi, X.3    Ballet, S.4    Ballesteros, J.A.5
  • 40
    • 0035933839 scopus 로고    scopus 로고
    • A conserved Asn in transmembrane helix 7 is an on/off switch in the activation of the thyrotropin receptor
    • Govaerts C, Lefort A, Costagliola S, Wodak SJ, Ballesteros JA, et al. 2001. A conserved Asn in transmembrane helix 7 is an on/off switch in the activation of the thyrotropin receptor. J. Biol. Chem. 276:22991-99
    • (2001) J. Biol. Chem. , vol.276 , pp. 22991-22999
    • Govaerts, C.1    Lefort, A.2    Costagliola, S.3    Wodak, S.J.4    Ballesteros, J.A.5
  • 41
    • 0036239236 scopus 로고    scopus 로고
    • Mutagenesis and modelling of the alpha(1b)-adrenergic receptor highlight the role of the helix 3/helix 6 interface in receptor activation
    • Greasley PJ, Fanelli F, Rossier O, Abuin L, Cotecchia S. 2002. Mutagenesis and modelling of the alpha(1b)-adrenergic receptor highlight the role of the helix 3/helix 6 interface in receptor activation. Mol. Pharmacol. 61:1025-32
    • (2002) Mol. Pharmacol. , vol.61 , pp. 1025-1032
    • Greasley, P.J.1    Fanelli, F.2    Rossier, O.3    Abuin, L.4    Cotecchia, S.5
  • 42
    • 0035824582 scopus 로고    scopus 로고
    • Mutational and computational analysis of the alpha(1b)-adrenergic receptor. Involvement of basic and hydrophobic residues in receptor activation and G protein coupling
    • Greasley PJ, Fanelli F, Scheer A, Abuin L, Nenniger-Tosato M, et al. 2001. Mutational and computational analysis of the alpha(1b)-adrenergic receptor. Involvement of basic and hydrophobic residues in receptor activation and G protein coupling. J. Biol. Chem. 276:46485-94
    • (2001) J. Biol. Chem. , vol.276 , pp. 46485-46494
    • Greasley, P.J.1    Fanelli, F.2    Scheer, A.3    Abuin, L.4    Nenniger-Tosato, M.5
  • 43
    • 0035942220 scopus 로고    scopus 로고
    • How activated receptors couple to G proteins
    • Hamm HE. 2001. How activated receptors couple to G proteins. Proc. Natl. Acad. Sci. USA 98:4819-21
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 4819-4821
    • Hamm, H.E.1
  • 44
    • 0026522293 scopus 로고
    • Rhodopsin and phototransduction - A model system for G-protein-linked receptors
    • Hargrave PA, McDowell JH. 1992. Rhodopsin and phototransduction - a model system for G-protein-linked receptors. FASEB J. 6:2323-31
    • (1992) FASEB J. , vol.6 , pp. 2323-2331
    • Hargrave, P.A.1    McDowell, J.H.2
  • 45
    • 0035918601 scopus 로고    scopus 로고
    • Structure activity studies of the melanocortin-4 receptor by in vitro mutagenesis: Identification of agouti-related protein (AGRP), melanocortin agonist and synthetic peptide antagonist interaction determinants
    • Haskell-Luevano C, Cone RD, Monck EK, Wan YP. 2001. Structure activity studies of the melanocortin-4 receptor by in vitro mutagenesis: identification of agouti-related protein (AGRP), melanocortin agonist and synthetic peptide antagonist interaction determinants. Biochemistry 40:6164-79
    • (2001) Biochemistry , vol.40 , pp. 6164-6179
    • Haskell-Luevano, C.1    Cone, R.D.2    Monck, E.K.3    Wan, Y.P.4
  • 47
    • 0032575763 scopus 로고    scopus 로고
    • Combined biophysical and biochemical information confirms arrangement of transmembrane helices visible from the three-dimensional map of frog rhodopsin
    • Herzyk P, Hubbard RE. 1998. Combined biophysical and biochemical information confirms arrangement of transmembrane helices visible from the three-dimensional map of frog rhodopsin. J. Mol. Biol. 281:741-54
    • (1998) J. Mol. Biol. , vol.281 , pp. 741-754
    • Herzyk, P.1    Hubbard, R.E.2
  • 48
    • 0035847094 scopus 로고    scopus 로고
    • Charged residues at the intracellular boundary of transmembrane helices 2 and 3 independently affect constitutive activity of Kaposi's sarcoma-associated herpesvirus G protein-coupled receptor
    • Ho HH, Ganeshalingam N, Rosenhouse-Dantsker A, Osman R, Gershengorn MC. 2001. Charged residues at the intracellular boundary of transmembrane helices 2 and 3 independently affect constitutive activity of Kaposi's sarcoma-associated herpesvirus G protein-coupled receptor. J. Biol. Chem. 276:1376-82
    • (2001) J. Biol. Chem. , vol.276 , pp. 1376-1382
    • Ho, H.H.1    Ganeshalingam, N.2    Rosenhouse-Dantsker, A.3    Osman, R.4    Gershengorn, M.C.5
  • 49
    • 0035170508 scopus 로고    scopus 로고
    • Collecting and harvesting biological data: The GPCRDB and NucleaRDB information systems
    • Horn F, Vriend G, Cohen FE. 2001. Collecting and harvesting biological data: the GPCRDB and NucleaRDB information systems. Nucleic Acids Res. 29:346-49
    • (2001) Nucleic Acids Res. , vol.29 , pp. 346-349
    • Horn, F.1    Vriend, G.2    Cohen, F.E.3
  • 50
    • 0037192126 scopus 로고    scopus 로고
    • Impact of aromatic residues within transmembrane helix 6 of the human gonadotropin-releasing hormone receptor upon agonist and antagonist binding
    • Hovelmann S, Hoffmann SH, Kuhne R, ter Laak T, Reilander H, Beckers T. 2002. Impact of aromatic residues within transmembrane helix 6 of the human gonadotropin-releasing hormone receptor upon agonist and antagonist binding. Biochemistry 41:1129-36
    • (2002) Biochemistry , vol.41 , pp. 1129-1136
    • Hovelmann, S.1    Hoffmann, S.H.2    Kuhne, R.3    Ter Laak, T.4    Reilander, H.5    Beckers, T.6
  • 51
    • 0035856560 scopus 로고    scopus 로고
    • Functional role of a conserved motif in TM6 of the rat mu opioid receptor: Constitutively active and inactive receptors result from substitutions of Thr6.34(279) with Lys and Asp
    • Huang P, Li J, Chen CG, Visiers I, Weinstein H, Liu-Chen LY. 2001. Functional role of a conserved motif in TM6 of the rat mu opioid receptor: Constitutively active and inactive receptors result from substitutions of Thr6.34(279) with Lys and Asp. Biochemistry 40:13501-9
    • (2001) Biochemistry , vol.40 , pp. 13501-13509
    • Huang, P.1    Li, J.2    Chen, C.G.3    Visiers, I.4    Weinstein, H.5    Liu-Chen, L.Y.6
  • 52
    • 0035935737 scopus 로고    scopus 로고
    • Neoceptor concept based on molecular complementarity in GPCRs: A mutant adenosine A(3) receptor with selectively enhanced affinity for amine-modified nucleosides
    • Jacobson KA, Gao ZG, Chen AS, Barak D, Kim SA, et al. 2001. Neoceptor concept based on molecular complementarity in GPCRs: a mutant adenosine A(3) receptor with selectively enhanced affinity for amine-modified nucleosides. J. Med. Chem. 44:4125-36
    • (2001) J. Med. Chem. , vol.44 , pp. 4125-4136
    • Jacobson, K.A.1    Gao, Z.G.2    Chen, A.S.3    Barak, D.4    Kim, S.A.5
  • 53
    • 0034792329 scopus 로고    scopus 로고
    • Use of the substituted cysteine accessibility method to study the structure and function of G protein-coupled receptors
    • Javitch JA, Shi L, Liapakis G. 2002. Use of the substituted cysteine accessibility method to study the structure and function of G protein-coupled receptors. Methods Enzymol. 343:137-56
    • (2002) Methods Enzymol , vol.343 , pp. 137-156
    • Javitch, J.A.1    Shi, L.2    Liapakis, G.3
  • 54
    • 0032504237 scopus 로고    scopus 로고
    • G Protein-coupled receptors. I. Diversity of receptor-ligand interactions
    • Ji T-H, Grossmann M, Ji I. 1998. G Protein-coupled receptors. I. Diversity of receptor-ligand interactions. J. Biol. Chem. 273:17299-302
    • (1998) J. Biol. Chem. , vol.273 , pp. 17299-17302
    • Ji, T.-H.1    Grossmann, M.2    Ji, I.3
  • 56
    • 0035855916 scopus 로고    scopus 로고
    • Acyclic and cyclopropyl analogues of adenosine bisphosphate antagonists of the P2Y(1) receptor: Structure-activity relationships and receptor docking
    • Kim HS, Barak D, Harden TK, Boyer JL, Jacobson KA. 2001. Acyclic and cyclopropyl analogues of adenosine bisphosphate antagonists of the P2Y(1) receptor: structure-activity relationships and receptor docking. J. Med. Chem. 44:3092-108
    • (2001) J. Med. Chem. , vol.44 , pp. 3092-3108
    • Kim, H.S.1    Barak, D.2    Harden, T.K.3    Boyer, J.L.4    Jacobson, K.A.5
  • 57
    • 0035940506 scopus 로고    scopus 로고
    • Probing the dark state tertiary structure in the cytoplasmic domain of rhodopsin: Proximities between amino acids deduced from spontaneous disulfide bond formation between Cys316 and engineered cysteines in cytoplasmic loop 1
    • Klein-Seetharaman J, Hwa J, Cai KW, Altenbach C, Hubbell WL, Khorana HG. 2001. Probing the dark state tertiary structure in the cytoplasmic domain of rhodopsin: proximities between amino acids deduced from spontaneous disulfide bond formation between Cys316 and engineered cysteines in cytoplasmic loop 1. Biochemistry 40:12472-78
    • (2001) Biochemistry , vol.40 , pp. 12472-12478
    • Klein-Seetharaman, J.1    Hwa, J.2    Cai, K.W.3    Altenbach, C.4    Hubbell, W.L.5    Khorana, H.G.6
  • 58
    • 0035902976 scopus 로고    scopus 로고
    • Functional roles of conserved transmembrane prolines in the human VPAC-(1) receptor
    • Knudsen SM, Tams JW, Fahrenkrug J. 2001. Functional roles of conserved transmembrane prolines in the human VPAC-(1) receptor. FEBS Lett. 503:126-30
    • (2001) FEBS Lett. , vol.503 , pp. 126-130
    • Knudsen, S.M.1    Tams, J.W.2    Fahrenkrug, J.3
  • 60
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi R, Billeter M, Wüthrich K. 1996. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14:51-55
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 61
    • 0032563291 scopus 로고    scopus 로고
    • G protein-coupled receptors. III. New roles for receptor kinases and beta-arrestins in receptor signaling and desensitization
    • Lefkowitz RJ. 1998. G protein-coupled receptors. III. New roles for receptor kinases and beta-arrestins in receptor signaling and desensitization. J. Biol. Chem. 273:18677-80
    • (1998) J. Biol. Chem. , vol.273 , pp. 18677-18680
    • Lefkowitz, R.J.1
  • 62
    • 0035834092 scopus 로고    scopus 로고
    • Constitutive activation of the mu opioid receptor by mutation of D3.49(164), but not D3.32(147): D3.49(164) is critical for stabilization of the inactive form of the receptor and for its expression
    • Li J, Huang P, Chen CG, de Riel JK, Weinstein H, Liu-Chen LY. 2001. Constitutive activation of the mu opioid receptor by mutation of D3.49(164), but not D3.32(147): D3.49(164) is critical for stabilization of the inactive form of the receptor and for its expression. Biochemistry 40:12039-50
    • (2001) Biochemistry , vol.40 , pp. 12039-12050
    • Li, J.1    Huang, P.2    Chen, C.G.3    De Riel, J.K.4    Weinstein, H.5    Liu-Chen, L.Y.6
  • 63
    • 84961974889 scopus 로고    scopus 로고
    • Study of the bioactive conformation of novel 5-HT4 receptor ligands: Influence of an intramolecular hydrogen bond
    • Lopez-Rodriguez ML, Benhamu B, Viso A, Murcia M, Pardo L. 2001. Study of the bioactive conformation of novel 5-HT4 receptor ligands: influence of an intramolecular hydrogen bond. Tetrahedron 57:6745-49
    • (2001) Tetrahedron , vol.57 , pp. 6745-6749
    • Lopez-Rodriguez, M.L.1    Benhamu, B.2    Viso, A.3    Murcia, M.4    Pardo, L.5
  • 65
    • 0032546920 scopus 로고    scopus 로고
    • Proton transfer pathways in bacteriorhodopsin at 2.3 Å resolution
    • Luecke H, Richter HT, Lanyi JK. 1998. Proton transfer pathways in bacteriorhodopsin at 2.3 Å resolution. Science 280:1934-37
    • (1998) Science , vol.280 , pp. 1934-1937
    • Luecke, H.1    Richter, H.T.2    Lanyi, J.K.3
  • 67
    • 0025890946 scopus 로고
    • Influence of proline residues on protein conformation
    • Macarthur MW, Thornton JM. 1991. Influence of proline residues on protein conformation. J. Mol. Biol. 218:397-412
    • (1991) J. Mol. Biol. , vol.218 , pp. 397-412
    • Macarthur, M.W.1    Thornton, J.M.2
  • 68
    • 0035798651 scopus 로고    scopus 로고
    • Control of conformational equilibria in the human B-2 bradykinin receptor - Modeling of non-peptidic ligand action and comparison to the rhodopsin structure
    • Marie J, Richard E, Pruneau D, Paquet JL, Siatka C, et al. 2001. Control of conformational equilibria in the human B-2 bradykinin receptor - modeling of non-peptidic ligand action and comparison to the rhodopsin structure. J. Biol. Chem. 276:41100-11
    • (2001) J. Biol. Chem. , vol.276 , pp. 41100-41111
    • Marie, J.1    Richard, E.2    Pruneau, D.3    Paquet, J.L.4    Siatka, C.5
  • 69
    • 0035689343 scopus 로고    scopus 로고
    • Peptide interactions with G-protein coupled receptors
    • Marshall GR. 2001. Peptide interactions with G-protein coupled receptors. Biopolymers 60:246-77
    • (2001) Biopolymers , vol.60 , pp. 246-277
    • Marshall, G.R.1
  • 71
    • 0035498937 scopus 로고    scopus 로고
    • Receptor activation: What does the rhodopsin structure tell us?
    • Meng EC, Bourne HR. 2001. Receptor activation: What does the rhodopsin structure tell us? Trends Pharmacol. Sci. 22:587-93
    • (2001) Trends Pharmacol. Sci. , vol.22 , pp. 587-593
    • Meng, E.C.1    Bourne, H.R.2
  • 72
    • 0034784920 scopus 로고    scopus 로고
    • Rhodopsin: Structural basis of molecular physiology
    • Menon S, Han M, Sakmar TP. 2001. Rhodopsin: structural basis of molecular physiology. Physiol. Rev. 81:1659-88
    • (2001) Physiol. Rev. , vol.81 , pp. 1659-1688
    • Menon, S.1    Han, M.2    Sakmar, T.P.3
  • 73
    • 0034671926 scopus 로고    scopus 로고
    • Characterization of the binding site on the formyl peptide receptor using three receptor mutants and analogs of Met-Leu-Phe and Met-Met-Trp-Leu-Leu
    • Mills JS, Miettinen HM, Cummings D, Jesaitis AJ. 2000. Characterization of the binding site on the formyl peptide receptor using three receptor mutants and analogs of Met-Leu-Phe and Met-Met-Trp-Leu-Leu. J. Biol. Chem. 275:39012-17
    • (2000) J. Biol. Chem. , vol.275 , pp. 39012-39017
    • Mills, J.S.1    Miettinen, H.M.2    Cummings, D.3    Jesaitis, A.J.4
  • 74
    • 0037133356 scopus 로고    scopus 로고
    • Molecular characterization of a ligand-tethered parathyroid hormone receptor
    • Monticelli L, Mammi S, Mierke DF. 2002. Molecular characterization of a ligand-tethered parathyroid hormone receptor. Biophys. Chem. 95:165-72
    • (2002) Biophys. Chem. , vol.95 , pp. 165-172
    • Monticelli, L.1    Mammi, S.2    Mierke, D.F.3
  • 75
    • 0034918454 scopus 로고    scopus 로고
    • Modeling and mutational analysis of a putative sodium-binding pocket on the dopamine D-2 receptor
    • Neve KA, Cumbay MG, Thompson KR, Yang R, Buck DC, et al. 2001. Modeling and mutational analysis of a putative sodium-binding pocket on the dopamine D-2 receptor. Mol. Pharmacol. 60:373-81
    • (2001) Mol. Pharmacol. , vol.60 , pp. 373-381
    • Neve, K.A.1    Cumbay, M.G.2    Thompson, K.R.3    Yang, R.4    Buck, D.C.5
  • 76
    • 0035237770 scopus 로고    scopus 로고
    • Novel approach to computer modeling of seven-helical transmembrane proteins: Current progress in the test case of bacteriorhodopsin
    • Nikiforovich GV, Galaktionov S, Balodis J, Marshall GR. 2001. Novel approach to computer modeling of seven-helical transmembrane proteins: current progress in the test case of bacteriorhodopsin. Acta Biochim. Pol. 48:53-64
    • (2001) Acta Biochim. Pol. , vol.48 , pp. 53-64
    • Nikiforovich, G.V.1    Galaktionov, S.2    Balodis, J.3    Marshall, G.R.4
  • 77
    • 0034805794 scopus 로고    scopus 로고
    • 3D model for TM region of the AT-1 receptor in complex with angiotensin II independently validated by site-directed mutagenssis data
    • Nikiforovich GV, Marshall GR. 2001. 3D model for TM region of the AT-1 receptor in complex with angiotensin II independently validated by site-directed mutagenssis data. Biochem. Biophys. Res. Commun. 286:1204-11
    • (2001) Biochem. Biophys. Res. Commun. , vol.286 , pp. 1204-1211
    • Nikiforovich, G.V.1    Marshall, G.R.2
  • 78
    • 0035336676 scopus 로고    scopus 로고
    • Activation of rhodopsin: New insights from structural and biochemical studies
    • Okada T, Ernst OP, Palczewski K, Hofmann KP. 2001. Activation of rhodopsin: new insights from structural and biochemical studies. Trends Biochem. Sci. 26:318-24
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 318-324
    • Okada, T.1    Ernst, O.P.2    Palczewski, K.3    Hofmann, K.P.4
  • 80
    • 0343081370 scopus 로고    scopus 로고
    • X-ray diffraction analysis of three-dimensional crystals of bovine rhodopsin obtained from mixed micelles
    • Okada T, Le Trong I, Fox BA, Behnke CA, Stenkamp RE, Palczewski K. 2000. X-ray diffraction analysis of three-dimensional crystals of bovine rhodopsin obtained from mixed micelles. J. Struct. Biol. 130:73-80
    • (2000) J. Struct. Biol. , vol.130 , pp. 73-80
    • Okada, T.1    Le Trong, I.2    Fox, B.A.3    Behnke, C.A.4    Stenkamp, R.E.5    Palczewski, K.6
  • 81
    • 0035423908 scopus 로고    scopus 로고
    • Crystal structure of rhodopsin: Implications for vision and beyond
    • Okada T, Palczewski K. 2001. Crystal structure of rhodopsin: implications for vision and beyond. Curr. Opin. Struct. Biol. 11:420-26
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 420-426
    • Okada, T.1    Palczewski, K.2
  • 82
    • 0032059717 scopus 로고    scopus 로고
    • Highly selective separation of rhodopsin from bovine rod outer segment membranes using combination of divalent cation and alkyl(thio)glucoside
    • Okada T, Takeda K, Kouyama T. 1998. Highly selective separation of rhodopsin from bovine rod outer segment membranes using combination of divalent cation and alkyl(thio)glucoside. Photochem. Photobiol. 67:495-99
    • (1998) Photochem. Photobiol. , vol.67 , pp. 495-499
    • Okada, T.1    Takeda, K.2    Kouyama, T.3
  • 83
    • 0036214523 scopus 로고    scopus 로고
    • Variant amino acids in the extracellular loops of murine and human vasopressin V2 receptors account for differences in cell surface expression and ligand affinity
    • Oksche A, Leder G, Valet S, Platzer M, Hasse K, et al. 2002. Variant amino acids in the extracellular loops of murine and human vasopressin V2 receptors account for differences in cell surface expression and ligand affinity. Mol. Endocrinol. 16:799-813
    • (2002) Mol. Endocrinol. , vol.16 , pp. 799-813
    • Oksche, A.1    Leder, G.2    Valet, S.3    Platzer, M.4    Hasse, K.5
  • 84
    • 0035928480 scopus 로고    scopus 로고
    • Length analyses of mammalian G-protein-coupled receptors
    • Otaki JM, Firestein S. 2001. Length analyses of mammalian G-protein-coupled receptors. J. Theor. Biol. 211:77-100
    • (2001) J. Theor. Biol. , vol.211 , pp. 77-100
    • Otaki, J.M.1    Firestein, S.2
  • 87
    • 0030864048 scopus 로고    scopus 로고
    • X-ray structure of bacteriorhodopsin at 2.5 Å from microcrystals grown in lipidic cubic phases
    • Pebay-Peyroula E, Rummel G, Rosenbusch JP, Landau EM. 1997. X-ray structure of bacteriorhodopsin at 2.5 Å from microcrystals grown in lipidic cubic phases. Science 277:1676-81
    • (1997) Science , vol.277 , pp. 1676-1681
    • Pebay-Peyroula, E.1    Rummel, G.2    Rosenbusch, J.P.3    Landau, E.M.4
  • 88
    • 0037023669 scopus 로고    scopus 로고
    • Structural insight into the role of the second intracellular loop of the bradykinin 2 receptor in signaling and internalization
    • Piserchio A, Prado GN, Zhang R, Yu J, Taylor L, et al. 2002. Structural insight into the role of the second intracellular loop of the bradykinin 2 receptor in signaling and internalization. Biopolymers 63:239-46
    • (2002) Biopolymers , vol.63 , pp. 239-246
    • Piserchio, A.1    Prado, G.N.2    Zhang, R.3    Yu, J.4    Taylor, L.5
  • 89
    • 0030998038 scopus 로고    scopus 로고
    • The transmembrane 7-alpha-bundle of rhodopsin: Distance geometry calculations with hydrogen bonding constraints
    • Pogozheva ID, Lomize AL, Mosberg HI. 1997. The transmembrane 7-alpha-bundle of rhodopsin: distance geometry calculations with hydrogen bonding constraints. Biophys. J. 72:1963-85
    • (1997) Biophys. J. , vol.72 , pp. 1963-1985
    • Pogozheva, I.D.1    Lomize, A.L.2    Mosberg, H.I.3
  • 91
    • 0033063884 scopus 로고    scopus 로고
    • The role of a conserved proline residue in mediating conformational changes associated with voltage gating of Cx32 gap junctions
    • Ri Y, Ballesteros JA, Abrams CK, Oh S, Verselis VK, et al. 1999. The role of a conserved proline residue in mediating conformational changes associated with voltage gating of Cx32 gap junctions. Biophys. J. 76:2887-98
    • (1999) Biophys. J. , vol.76 , pp. 2887-2898
    • Ri, Y.1    Ballesteros, J.A.2    Abrams, C.K.3    Oh, S.4    Verselis, V.K.5
  • 92
    • 0035895421 scopus 로고    scopus 로고
    • Non-alpha-helical elements modulate polytopic membrane protein architecture
    • Riek RP, Rigoutsos I, Novotny J, Graham RM. 2001. Non-alpha-helical elements modulate polytopic membrane protein architecture. J. Mol. Biol. 306:349-62
    • (2001) J. Mol. Biol. , vol.306 , pp. 349-362
    • Riek, R.P.1    Rigoutsos, I.2    Novotny, J.3    Graham, R.M.4
  • 93
    • 0035783023 scopus 로고    scopus 로고
    • Stability of membrane proteins: Relevance for the selection of appropriate methods for high-resolution structure determinations
    • Rosenbusch JP. 2001. Stability of membrane proteins: relevance for the selection of appropriate methods for high-resolution structure determinations. J. Struct. Biol. 136:144-57
    • (2001) J. Struct. Biol. , vol.136 , pp. 144-157
    • Rosenbusch, J.P.1
  • 94
    • 0036532207 scopus 로고    scopus 로고
    • Structure of rhodopsin and the superfamily of seven-helical receptors: The same and not the same
    • Sakmar TP. 2002. Structure of rhodopsin and the superfamily of seven-helical receptors: the same and not the same. Curr. Opin. Cell Biol. 14:189-95
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 189-195
    • Sakmar, T.P.1
  • 98
    • 0034532346 scopus 로고    scopus 로고
    • Requirement of specific intrahelical interactions for stabilizing the inactive conformation of glycoprotein hormone receptors
    • Schulz A, Bruns K, Henklein P, Krause G, Schubert M, et al. 2000. Requirement of specific intrahelical interactions for stabilizing the inactive conformation of glycoprotein hormone receptors. J. Biol. Chem. 275:37860-69
    • (2000) J. Biol. Chem. , vol.275 , pp. 37860-37869
    • Schulz, A.1    Bruns, K.2    Henklein, P.3    Krause, G.4    Schubert, M.5
  • 100
    • 0037192858 scopus 로고    scopus 로고
    • Evidence for a model of agonist-induced activation of 5-hydroxytryptamine 2A serotonin receptors that involves the disruption of a strong ionic interaction between helices 3 and 6
    • Shapiro DA, Kristiansen K, Weiner DM, Kroeze WK, Roth BL. 2002. Evidence for a model of agonist-induced activation of 5-hydroxytryptamine 2A serotonin receptors that involves the disruption of a strong ionic interaction between helices 3 and 6. J. Biol. Chem. 277:11441-49
    • (2002) J. Biol. Chem. , vol.277 , pp. 11441-11449
    • Shapiro, D.A.1    Kristiansen, K.2    Weiner, D.M.3    Kroeze, W.K.4    Roth, B.L.5
  • 101
    • 0035899988 scopus 로고    scopus 로고
    • The first transmembrane segment of the dopamine D2 receptor: Accessibility in the binding-site crevice and position in the transmembrane bundle
    • Shi L, Simpson MM, Ballesteros JA, Jayitch JA. 2001. The first transmembrane segment of the dopamine D2 receptor: accessibility in the binding-site crevice and position in the transmembrane bundle. Biochemistry 40:12339-48
    • (2001) Biochemistry , vol.40 , pp. 12339-12348
    • Shi, L.1    Simpson, M.M.2    Ballesteros, J.A.3    Jayitch, J.A.4
  • 102
    • 0032412196 scopus 로고    scopus 로고
    • Visual pigment: G-protein-coupled receptor for light signals
    • Shichida Y, Imai H. 1998. Visual pigment: G-protein-coupled receptor for light signals. Cell. Mol. Life Sci. 54:1299-315
    • (1998) Cell. Mol. Life Sci. , vol.54 , pp. 1299-1315
    • Shichida, Y.1    Imai, H.2
  • 103
    • 0034982278 scopus 로고    scopus 로고
    • Pleiotropic effects of substitutions of a highly conserved leucine in transmembrane helix III of the human lutropin/choriogonadotropin receptor with respect to constitutive activation and hormone responsiveness
    • Shinozaki H, Fanelli F, Liu XB, Jaquette J, Nakamura K, Segaloff DL. 2001. Pleiotropic effects of substitutions of a highly conserved leucine in transmembrane helix III of the human lutropin/choriogonadotropin receptor with respect to constitutive activation and hormone responsiveness. Mol. Endocrinol. 15:972-84
    • (2001) Mol. Endocrinol. , vol.15 , pp. 972-984
    • Shinozaki, H.1    Fanelli, F.2    Liu, X.B.3    Jaquette, J.4    Nakamura, K.5    Segaloff, D.L.6
  • 104
    • 0035836452 scopus 로고    scopus 로고
    • Conformation and orientation of the retinyl chromophore in rhodopsin: A critical evaluation of recent NMR data on the basis of theoretical calculations results in a minimum energy structure consistent with all experimental data
    • Singh D, Hudson BS, Middleton C, Birge RR. 2000. Conformation and orientation of the retinyl chromophore in rhodopsin: A critical evaluation of recent NMR data on the basis of theoretical calculations results in a minimum energy structure consistent with all experimental data. Biochemistry 40:4201-4
    • (2000) Biochemistry , vol.40 , pp. 4201-4204
    • Singh, D.1    Hudson, B.S.2    Middleton, C.3    Birge, R.R.4
  • 105
    • 0035957579 scopus 로고    scopus 로고
    • Constitutively active muscarinic receptors
    • Spalding TA, Burstein ES. 2001. Constitutively active muscarinic receptors. Life Sci. 68:2511-16
    • (2001) Life Sci. , vol.68 , pp. 2511-2516
    • Spalding, T.A.1    Burstein, E.S.2
  • 106
    • 0037129946 scopus 로고    scopus 로고
    • Relative orientation between the β-ionone ring and the polyene chain for the chromophore of rhodopsin in native membranes
    • Spooner PJR, Sharples JM, Verhoeven MA, Lugtenburg J, Glaubitz C, Watts A. 2002. Relative orientation between the β-ionone ring and the polyene chain for the chromophore of rhodopsin in native membranes. Biochemistry 41:7549-55
    • (2002) Biochemistry , vol.41 , pp. 7549-7555
    • Spooner, P.J.R.1    Sharples, J.M.2    Verhoeven, M.A.3    Lugtenburg, J.4    Glaubitz, C.5    Watts, A.6
  • 109
    • 0036235905 scopus 로고    scopus 로고
    • The critical role of transmembrane prolines in human prostacyclin receptor activation
    • Stitham J, Martin KA, Hwa J. 2002. The critical role of transmembrane prolines in human prostacyclin receptor activation. Mol. Pharmacol. 61:1202-10
    • (2002) Mol. Pharmacol. , vol.61 , pp. 1202-1210
    • Stitham, J.1    Martin, K.A.2    Hwa, J.3
  • 110
    • 0034734253 scopus 로고    scopus 로고
    • Crystallographic analysis of protein conformational changes in the bacteriorhodopsin photocycle
    • Subramaniam S, Henderson R. 2000. Crystallographic analysis of protein conformational changes in the bacteriorhodopsin photocycle. Biochim. Biophys. Acta Bioenerg. 1460:157-65
    • (2000) Biochim. Biophys. Acta Bioenerg. , vol.1460 , pp. 157-165
    • Subramaniam, S.1    Henderson, R.2
  • 111
    • 0030810079 scopus 로고    scopus 로고
    • Absolute sense of twist of the C12-C13 bond of the retinal chromophore in bovine rhodopsin based on exciton-coupled CD spectra of 11,12-dihydroretinal analogues
    • Tan Q, Lou JH, Borhan B, Karnaukhova E, Berova N, Nakanishi K. 1997. Absolute sense of twist of the C12-C13 bond of the retinal chromophore in bovine rhodopsin based on exciton-coupled CD spectra of 11,12-dihydroretinal analogues. Angew. Chem. Int. Ed. 36:2089-93
    • (1997) Angew. Chem. Int. Ed. , vol.36 , pp. 2089-2093
    • Tan, Q.1    Lou, J.H.2    Borhan, B.3    Karnaukhova, E.4    Berova, N.5    Nakanishi, K.6
  • 112
    • 0035800032 scopus 로고    scopus 로고
    • Advances in determination of a high-resolution three-dimensional structure of rhodopsin, a model of G-protein-coupled receptors (GPCRs)
    • Teller DC, Okada T, Behnke CA, Palczewski K, Stenkamp RE. 2001. Advances in determination of a high-resolution three-dimensional structure of rhodopsin, a model of G-protein-coupled receptors (GPCRs). Biochemistry 40:7761-72
    • (2001) Biochemistry , vol.40 , pp. 7761-7772
    • Teller, D.C.1    Okada, T.2    Behnke, C.A.3    Palczewski, K.4    Stenkamp, R.E.5
  • 113
    • 0035965271 scopus 로고    scopus 로고
    • Molecular basis for selectivity of high affinity peptide antagonists for the gastrin-releasing peptide receptor
    • Tokita K, Katsuno T, Hocart SJ, Coy DH, Llinares M, et al. 2001. Molecular basis for selectivity of high affinity peptide antagonists for the gastrin-releasing peptide receptor. J. Biol. Chem. 276:36652-63
    • (2001) J. Biol. Chem. , vol.276 , pp. 36652-36663
    • Tokita, K.1    Katsuno, T.2    Hocart, S.J.3    Coy, D.H.4    Llinares, M.5
  • 116
    • 0034800005 scopus 로고    scopus 로고
    • Strategies for modeling the interactions of transmembrane helices of G protein-coupled receptors by geometric complementarity using the GRAMM computer algorithm
    • Vakser IA, Jiang SL. 2002. Strategies for modeling the interactions of transmembrane helices of G protein-coupled receptors by geometric complementarity using the GRAMM computer algorithm. Methods Enzymol. 343:313-28
    • (2002) Methods Enzymol. , vol.343 , pp. 313-328
    • Vakser, I.A.1    Jiang, S.L.2
  • 117
    • 0032504180 scopus 로고    scopus 로고
    • G protein-coupled receptors minireview series
    • Vaughan M. 1998. G protein-coupled receptors minireview series. J. Biol. Chem. 273:17297
    • (1998) J. Biol. Chem. , vol.273 , pp. 17297
    • Vaughan, M.1
  • 118
    • 0034787251 scopus 로고    scopus 로고
    • Three-dimensional representations of G protein-coupled receptor structures and mechanisms
    • Visiers I, Ballesteros JA, Weinstein H. 2002. Three-dimensional representations of G protein-coupled receptor structures and mechanisms. Methods Enzymol. 343:329-71
    • (2002) Methods Enzymol. , vol.343 , pp. 329-371
    • Visiers, I.1    Ballesteros, J.A.2    Weinstein, H.3
  • 119
    • 0033768889 scopus 로고    scopus 로고
    • Prokink: A protocol for numerical evaluation of helix distortions by proline
    • Visiers I, Braunheim BB, Weinstein H. 2000. Prokink: a protocol for numerical evaluation of helix distortions by proline. Protein Eng. 13:603-6
    • (2000) Protein Eng. , vol.13 , pp. 603-606
    • Visiers, I.1    Braunheim, B.B.2    Weinstein, H.3
  • 120
    • 0037127315 scopus 로고    scopus 로고
    • Conformational changes that occur during M-3 muscarinic acetylcholine receptor activation probed by the use of an in situ disulfide cross-linking strategy
    • Ward SDC, Hamdan FF, Bloodworth LM, Wess J. 2002. Conformational changes that occur during M-3 muscarinic acetylcholine receptor activation probed by the use of an in situ disulfide cross-linking strategy. J. Biol. Chem. 277:2247-57
    • (2002) J. Biol. Chem. , vol.277 , pp. 2247-2257
    • Ward, S.D.C.1    Hamdan, F.F.2    Bloodworth, L.M.3    Wess, J.4
  • 122
    • 0035816665 scopus 로고    scopus 로고
    • Phe-308 and Phe-312 in transmembrane domain 7 are major sites of alpha(1)-adrenergic receptor antagonist binding - Imidazoline agonists bind like antagonists
    • Waugh DJJ, Gaivin RJ, Zuscik MJ, Gonzalez-Cabrera P, Ross SA, et al. 2001. Phe-308 and Phe-312 in transmembrane domain 7 are major sites of alpha(1)-adrenergic receptor antagonist binding - imidazoline agonists bind like antagonists. J. Biol. Chem. 276:25366-71
    • (2001) J. Biol. Chem. , vol.276 , pp. 25366-25371
    • Waugh, D.J.J.1    Gaivin, R.J.2    Zuscik, M.J.3    Gonzalez-Cabrera, P.4    Ross, S.A.5
  • 123
    • 0025602520 scopus 로고
    • The influence of proline residues on alpha-helical structure
    • Woolfson DN, Williams DH. 1990. The influence of proline residues on alpha-helical structure. FEBS Lett. 277:185-88
    • (1990) FEBS Lett. , vol.277 , pp. 185-188
    • Woolfson, D.N.1    Williams, D.H.2
  • 124
    • 0035838374 scopus 로고    scopus 로고
    • Comparison of the amino acid residues in the sixth transmembrane domains accessible in the binding-site crevices of mu, delta, and kappa opioid receptors
    • Xu W, Li J, Chen CG, Huang P, Weinstein H, et al. 2001. Comparison of the amino acid residues in the sixth transmembrane domains accessible in the binding-site crevices of mu, delta, and kappa opioid receptors. Biochemistry 40:8018-29
    • (2001) Biochemistry , vol.40 , pp. 8018-8029
    • Xu, W.1    Li, J.2    Chen, C.G.3    Huang, P.4    Weinstein, H.5
  • 125
    • 0034610311 scopus 로고    scopus 로고
    • Molecular determinants of ligand binding to the human melanocortin-4 receptor
    • Yang Y, Fong TM, Dickinson CJ, Mao C, Li JY, et al. 2000. Molecular determinants of ligand binding to the human melanocortin-4 receptor. Biochemistry 39:14900-11
    • (2000) Biochemistry , vol.39 , pp. 14900-14911
    • Yang, Y.1    Fong, T.M.2    Dickinson, C.J.3    Mao, C.4    Li, J.Y.5
  • 126
    • 0035797877 scopus 로고    scopus 로고
    • Studies on the structure of the G-protein-coupled receptor rhodopsin including the putative G-protein binding site in unactivated and activated forms
    • Yeagle PL, Choi G, Albert AD. 2001. Studies on the structure of the G-protein-coupled receptor rhodopsin including the putative G-protein binding site in unactivated and activated forms. Biochemistry 40:11932-37
    • (2001) Biochemistry , vol.40 , pp. 11932-11937
    • Yeagle, P.L.1    Choi, G.2    Albert, A.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.