{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,17]],"date-time":"2026-08-17T20:32:54Z","timestamp":1786998774438,"version":"3.56.0"},"reference-count":79,"publisher":"Elsevier BV","issue":"3","license":[{"start":{"date-parts":[[2002,3,1]],"date-time":"2002-03-01T00:00:00Z","timestamp":1014940800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Trends in Pharmacological Sciences"],"published-print":{"date-parts":[[2002,3]]},"DOI":"10.1016\/s0165-6147(00)01973-8","type":"journal-article","created":{"date-parts":[[2002,7,25]],"date-time":"2002-07-25T07:32:04Z","timestamp":1027582324000},"page":"140-146","source":"Crossref","is-referenced-by-count":135,"title":["Seven-transmembrane receptors: crystals clarify"],"prefix":"10.1016","volume":"23","author":[{"given":"Zhi-Liang","family":"Lu","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jose W","family":"Saldanha","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Edward C","family":"Hulme","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/S0165-6147(00)01973-8_BIB1","doi-asserted-by":"crossref","first-page":"1304","DOI":"10.1126\/science.1058040","article-title":"The sequence of the human genome","volume":"291","author":"Venter","year":"2001","journal-title":"Science"},{"key":"10.1016\/S0165-6147(00)01973-8_BIB2","doi-asserted-by":"crossref","first-page":"860","DOI":"10.1038\/35057062","article-title":"Initial sequencing and analysis of the human genome","volume":"409","year":"2001","journal-title":"Nature"},{"key":"10.1016\/S0165-6147(00)01973-8_BIB3","doi-asserted-by":"crossref","first-page":"7761","DOI":"10.1021\/bi0155091","article-title":"Advances in determination of a high-resolution three-dimensional structure of rhodopsin, a model of G-protein-coupled receptors (GPCRs)","volume":"40","author":"Teller","year":"2001","journal-title":"Biochemistry"},{"key":"10.1016\/S0165-6147(00)01973-8_BIB4","doi-asserted-by":"crossref","first-page":"739","DOI":"10.1126\/science.289.5480.739","article-title":"Crystal structure of rhodopsin: a G protein-coupled receptor","volume":"289","author":"Palczewski","year":"2000","journal-title":"Science"},{"key":"10.1016\/S0165-6147(00)01973-8_BIB5","doi-asserted-by":"crossref","first-page":"366","DOI":"10.1016\/S1043-9471(05)80049-7","article-title":"Integrated methods for the construction of three dimensional models and computational probing of structure\u2013function relations in G-protein-coupled receptors","volume":"25","author":"Ballesteros","year":"1995","journal-title":"Methods Neurosci."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB6","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1089\/dna.1992.11.1","article-title":"Sequence alignment of the G-protein coupled receptor superfamily","volume":"11","author":"Probst","year":"1992","journal-title":"DNA Cell Biol."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB7","doi-asserted-by":"crossref","first-page":"8812","DOI":"10.1021\/bi00027a033","article-title":"Mapping light-dependent structural changes in the cytoplasmic loop connecting helices C and D in rhodopsin: a site-directed spin labeling study","volume":"34","author":"Farahbakhsh","year":"1995","journal-title":"Biochemistry"},{"key":"10.1016\/S0165-6147(00)01973-8_BIB8","doi-asserted-by":"crossref","first-page":"12470","DOI":"10.1021\/bi960849l","article-title":"Structural features and light-dependent changes in the cytoplasmic interhelical E\u2013F loop region of rhodopsin: a site-directed spin-labelling study","volume":"35","author":"Altenbach","year":"1996","journal-title":"Biochemistry"},{"key":"10.1016\/S0165-6147(00)01973-8_BIB9","doi-asserted-by":"crossref","first-page":"7938","DOI":"10.1021\/bi990013t","volume":"38","author":"Klein-Seetharaman","year":"2000","journal-title":"Biochemistry"},{"key":"10.1016\/S0165-6147(00)01973-8_BIB10","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1006\/jmbi.1997.1240","article-title":"An \u03b1-carbon template for the transmembrane helices in the rhodopsin family of G-protein-coupled receptors","volume":"272","author":"Baldwin","year":"1997","journal-title":"J. Mol. Biol."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB11","doi-asserted-by":"crossref","first-page":"4991","DOI":"10.1073\/pnas.87.13.4991","article-title":"Role of the intradiscal domain in rhodopsin assembly and function","volume":"87","author":"Doi","year":"1990","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB12","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1124\/mol.60.1.1","article-title":"Structural mimicry in G protein-coupled receptors: implications of the high-resolution structure of rhodopsin for structure\u2013function analysis of rhodopsin-like receptors","volume":"60","author":"Ballesteros","year":"2001","journal-title":"Mol. Pharmacol."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB13","doi-asserted-by":"crossref","first-page":"234","DOI":"10.1124\/mol.51.2.234","article-title":"The Role of the aspartate\u2013arginine\u2013tyrosine triad in the m1 muscarinic receptor: mutations of aspartate 122 and tyrosine 124 decrease receptor expression but do not abolish signaling","volume":"51","author":"Lu","year":"1997","journal-title":"Mol. Pharmacol."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB14","doi-asserted-by":"crossref","first-page":"318","DOI":"10.1016\/S0968-0004(01)01799-6","article-title":"Activation of rhodopsin: new insights from structural and biochemical studies","volume":"26","author":"Okada","year":"2001","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB15","doi-asserted-by":"crossref","first-page":"5682","DOI":"10.1074\/jbc.275.8.5682","article-title":"A network of conserved intramolecular contacts defines the off-state of the transmembrane switch mechanism in a seven-transmembrane receptor","volume":"275","author":"Lu","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB16","doi-asserted-by":"crossref","first-page":"7405","DOI":"10.1074\/jbc.270.13.7405","article-title":"Activating and inactivating mutations in N- and C-terminal i3 loop junctions of muscarinic acetylcholine Hm1 receptors","volume":"270","author":"Hogger","year":"1995","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB17","doi-asserted-by":"crossref","first-page":"34098","DOI":"10.1074\/jbc.M104217200","article-title":"Transmembrane domains 4 and 7 of the M1 muscarinic actylcholine receptor are critical for ligand binding and the receptor activation switch","volume":"276","author":"Lu","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB18","doi-asserted-by":"crossref","first-page":"10445","DOI":"10.1074\/jbc.273.17.10445","article-title":"Functional microdomains in G-protein-coupled receptors","volume":"273","author":"Ballesteros","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB19","doi-asserted-by":"crossref","first-page":"28880","DOI":"10.1074\/jbc.274.41.28880","article-title":"The functional microdomain in transmembrane helices 2 and 7 regulates expression, activation, and coupling pathways of the gonadotropin-releasing hormone receptor","volume":"274","author":"Flanagan","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB20","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1210\/edrv.21.1.0390","article-title":"Uncovering molecular mechanisms involved in activation of G protein-coupled receptors","volume":"21","author":"Gether","year":"2001","journal-title":"Endocr. Rev."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB21","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1615\/CritRevNeurobiol.v10.i1.40","article-title":"Molecular biology of muscarinic acetylcholine receptors","volume":"10","author":"Wess","year":"1996","journal-title":"Crit. Rev. Neurobiol."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB22","doi-asserted-by":"crossref","first-page":"7309","DOI":"10.1074\/jbc.274.11.7309","article-title":"The functional topography of transmembrane domain 3 of the M1 muscarinic acetylcholine receptor, revealed by scanning mutagenesis","volume":"274","author":"Lu","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB23","doi-asserted-by":"crossref","first-page":"1031","DOI":"10.1124\/mol.56.5.1031","article-title":"Alanine-scanning mutagenesis of transmembrane domain 6 of the M1 muscarinic acetylcholine receptor suggests that Tyr381 plays key roles in receptor function","volume":"56","author":"Ward","year":"1999","journal-title":"Mol. Pharmacol."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB24","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1124\/mol.58.1.175","article-title":"Scanning mutagenesis identifies amino acid side chains in transmembrane domain 5 of the M1 muscarinic receptor that participate in binding the acetyl methyl group of acetylcholine","volume":"58","author":"Allman","year":"2000","journal-title":"Mol. Pharmacol."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB25","doi-asserted-by":"crossref","first-page":"194","DOI":"10.1124\/mol.58.1.194","article-title":"Allosteric interactions of staurosporine and other indolocarbazoles with N-[methyl-3H]-scopolamine and acetylcholine at muscarinic receptor subtypes: identification of a second allosteric site","volume":"58","author":"Lazareno","year":"2000","journal-title":"Mol. Pharmacol."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB26","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1038\/35077011","article-title":"Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors","volume":"411","author":"Brejc","year":"2001","journal-title":"Nature"},{"key":"10.1016\/S0165-6147(00)01973-8_BIB27","doi-asserted-by":"crossref","first-page":"308","DOI":"10.1016\/0165-6147(93)90049-P","article-title":"Molecular basis of muscarinic acetylcholine receptor function","volume":"14","author":"Wess","year":"1993","journal-title":"Trends Pharmacol. Sci."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB28","first-page":"8","article-title":"Three-dimensional models of neurotransmitter G-binding protein-coupled receptors","volume":"40","author":"Hibert","year":"1991","journal-title":"Mol. Pharmacol."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB29","doi-asserted-by":"crossref","first-page":"17299","DOI":"10.1074\/jbc.273.28.17299","article-title":"G protein-coupled receptors. I. diversity of receptor-ligand interactions","volume":"273","author":"Ji","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB30","doi-asserted-by":"crossref","first-page":"370","DOI":"10.1124\/mol.53.3.370","article-title":"Chloroethylclonidine binds irreversibnly to exposed cysteines in the fifth membrane-spanning domain of the human \u03b12A-adrenergic receptor","volume":"53","author":"Marjamaki","year":"1998","journal-title":"Mol. Pharmacol."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB31","doi-asserted-by":"crossref","first-page":"16320","DOI":"10.1074\/jbc.274.23.16320","article-title":"Phe310 in transmembrane VI of the \u03b11B-adrenergic receptor is a key switch residue involved in activation and catecholamine ring aromatic bonding","volume":"274","author":"Chen","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB32","doi-asserted-by":"crossref","first-page":"35393","DOI":"10.1074\/jbc.M005602200","article-title":"Genetic mapping of the human C5a receptor: identification of transmembrane amino acids critical for receptor function","volume":"275","author":"Geva","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB33","doi-asserted-by":"crossref","first-page":"3394","DOI":"10.1074\/jbc.M007748200","article-title":"An activation switch in the ligand binding pocket of the C5a receptor","volume":"276","author":"Gerber","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB34","doi-asserted-by":"crossref","first-page":"4029","DOI":"10.1073\/pnas.91.9.4029","article-title":"Structure and function in rhodopsin: replacement by alanine of cysteine residues 110 and 187, components of a conserved disulfide bond in rhodopsin, affects the light-activated metarhodopsin II state","volume":"91","author":"Davidson","year":"1994","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB35","doi-asserted-by":"crossref","first-page":"13702","DOI":"10.1016\/S0021-9258(18)77406-1","article-title":"Muscarinic acetylcholine receptors: peptide sequencing identifies residues involved in antagonist binding and disulfide bond formation","volume":"265","author":"Kurtenbach","year":"1990","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB36","doi-asserted-by":"crossref","first-page":"11439","DOI":"10.1016\/S0021-9258(19)49929-8","article-title":"Site-directed mutagenesis of the rat m1 muscarinic acetylcholine receptor: role of conserved cysteines in receptor function","volume":"267","author":"Savarese","year":"1992","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB37","doi-asserted-by":"crossref","first-page":"2404","DOI":"10.1046\/j.1471-4159.1999.0722404.x","article-title":"Conserved extracellular cysteine pair in the M3 muscarinic acetylcholine receptor is necessary for proper receptor cell surface localization, but not for G protein coupling","volume":"72","author":"Zeng","year":"1999","journal-title":"J. Neurochem."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB38","first-page":"88","article-title":"Probing of the location of the allosteric site on m1 muscarinic receptors by site-directed mutagenesis","volume":"47","author":"Matsui","year":"1995","journal-title":"Mol. Pharmacol."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB39","doi-asserted-by":"crossref","first-page":"18836","DOI":"10.1074\/jbc.M000112200","article-title":"Evidence for a tandem two-site model of ligand binding to muscarinic acetylcholine receptors","volume":"275","author":"Jakubik","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB40","doi-asserted-by":"crossref","first-page":"875","DOI":"10.1124\/mol.59.4.875","article-title":"Activation of guanosine 5\u2032-[-35S]thio-triphosphate binding through M1 muscarinic receptors in transfected chinese hamster ovary cell membranes:1. mathematical analysis of catalytic G protein activation","volume":"59","author":"Waelbroeck","year":"2001","journal-title":"Mol. Pharmacol."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB41","doi-asserted-by":"crossref","first-page":"886","DOI":"10.1124\/mol.59.4.886","article-title":"Activation of guanosine 5\u2032-[35S]thio-triphosphate binding through M1 muscarinic receptors in transfected chinese hamster ovary cell membranes: 2. testing the \u2018two-states\u2019 model of receptor activation","volume":"59","author":"Waelbroeck","year":"2001","journal-title":"Mol. Pharmacol."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB42","doi-asserted-by":"crossref","first-page":"348","DOI":"10.1124\/mol.56.2.348","article-title":"Effects of guanine, inosine and xanthine nucleotides on \u03b22-adrenergic receptor\/Gs interaction: evidence for multiple receptor conformations","volume":"56","author":"Seifert","year":"1999","journal-title":"Mol. Pharmacol."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB43","doi-asserted-by":"crossref","first-page":"24433","DOI":"10.1074\/jbc.C100162200","article-title":"Functionally different agonists induce distinct conformations in the G protein coupling domain of the \u03b22 adrenergic receptor","volume":"276","author":"Ghanouni","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB44","doi-asserted-by":"crossref","first-page":"2209","DOI":"10.1126\/science.288.5474.2209","article-title":"Movement of retinal along the visual transduction path","volume":"288","author":"Borhan","year":"2000","journal-title":"Science"},{"key":"10.1016\/S0165-6147(00)01973-8_BIB45","doi-asserted-by":"crossref","first-page":"12322","DOI":"10.1073\/pnas.96.22.12322","article-title":"Conversion of agonist site to metal-ion chelator site in the \u03b22-adrenergic receptor","volume":"96","author":"Elling","year":"1999","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB46","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1124\/mol.58.2.263","article-title":"Partial agonism through a zinc-ion switch constructed between transmembrane domains III and VII in the tachykinin NK(1) receptor","volume":"58","author":"Holst","year":"2000","journal-title":"Mol. Pharmacol."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB47","doi-asserted-by":"crossref","first-page":"8253","DOI":"10.1021\/bi980147r","article-title":"Constitutive activation of opsin by mutation of methionine 257 on transmembrane helix 6","volume":"37","author":"Han","year":"1998","journal-title":"Biochemistry"},{"key":"10.1016\/S0165-6147(00)01973-8_BIB48","doi-asserted-by":"crossref","first-page":"21563","DOI":"10.1074\/jbc.273.34.21563","article-title":"Identification of a ligand-dependent switch within a muscarinic receptor","volume":"273","author":"Spalding","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB49","doi-asserted-by":"crossref","first-page":"1272","DOI":"10.1210\/mend.14.8.0503","article-title":"Constitutive activation of G protein-coupled receptors as a result of selective substitution of a conserved leucine residue in transmembrane helix III","volume":"14","author":"Tao","year":"2000","journal-title":"Mol. Endocrinol."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB50","doi-asserted-by":"crossref","first-page":"601","DOI":"10.1016\/S0006-3495(98)77551-4","article-title":"A proposed structure for transmembrane segment 7 of G protein-coupled receptor incorporating an Asn-Pro\/Asp-Pro motif","volume":"75","author":"Konvicka","year":"1998","journal-title":"Biophys. J."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB51","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1016\/S0014-2999(99)00297-6","article-title":"The conformational switch in 7-transmembrane receptors: the muscarinic receptor paradigm","volume":"375","author":"Hulme","year":"1999","journal-title":"Eur. J. Pharmacol."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB52","doi-asserted-by":"crossref","first-page":"14273","DOI":"10.1073\/pnas.94.26.14273","article-title":"Structure and function in rhodopsin: rhodopsin mutants with a neutral amino acid at E134 have a partially activated conformation in the dark state","volume":"94","author":"Kim","year":"1997","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB53","doi-asserted-by":"crossref","first-page":"808","DOI":"10.1073\/pnas.94.3.808","article-title":"The activation process of the \u03b11B-adrenergic receptor: potential role of protonation and hydrophobicity of a highly conserved aspartate","volume":"94","author":"Scheer","year":"1997","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB54","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1124\/mol.56.1.175","article-title":"Mutation of a highly conserved aspartic acid in the \u03b22 adrenergic receptor: constitutive activation, structural instability, and conformational rearrangement of transmembrane segment 6","volume":"56","author":"Rasmussen","year":"1999","journal-title":"Mol. Pharmacol."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB55","first-page":"890","article-title":"The effect of mutations in the DRY motif on the constitutive activity and structural instability of the histamine H2 receptor","volume":"57","author":"Alewjinse","year":"2000","journal-title":"Mol. Pharmacol."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB56","doi-asserted-by":"crossref","first-page":"1683","DOI":"10.1074\/jbc.274.3.1683","article-title":"Conformational changes in rhodopsin: movement of helix F detected by site-specific chemical labeling and fluorescence spectroscopy","volume":"274","author":"Dunham","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB57","doi-asserted-by":"crossref","first-page":"9279","DOI":"10.1074\/jbc.M004871200","article-title":"Agonist-induced conformational changes at the cytoplasmic side of TM6 in the \u03b22 adrenergic receptor mapped by site-selective fluorescent labeling","volume":"276","author":"Jensen","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB58","doi-asserted-by":"crossref","first-page":"17033","DOI":"10.1074\/jbc.274.24.17033","article-title":"Similar structures and shared switch mechanisms of the \u03b22-adrenoceptor and the parathyroid hormone receptor: Zn(II) bridges between helices III and VI block activation","volume":"274","author":"Sheikh","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB59","doi-asserted-by":"crossref","first-page":"587","DOI":"10.1016\/S0165-6147(00)01825-3","article-title":"Receptor activation: what does the rhodopsin structure tell us?","volume":"22","author":"Meng","year":"2001","journal-title":"Trends Pharmacol. Sci."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB60","doi-asserted-by":"crossref","first-page":"7931","DOI":"10.1021\/bi9900121","article-title":"Structural features and light-dependent changes in the sequence 306\u2013322 extending from helix VII to the palmitoylation sites in rhodopsin: a site-directed spin-labeling study","volume":"38","author":"Altenbach","year":"1999","journal-title":"Biochemistry"},{"key":"10.1016\/S0165-6147(00)01973-8_BIB61","doi-asserted-by":"crossref","first-page":"12854","DOI":"10.1073\/pnas.95.22.12854","article-title":"Light-induced exposure of the cytoplasmic end of transmembrane helix seven in rhodopsin","volume":"95","author":"Abdulaev","year":"1998","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB62","doi-asserted-by":"crossref","first-page":"12028","DOI":"10.1021\/bi990948+","article-title":"State-dependent disulfide cross-linking in rhodopsin","volume":"38","author":"Yu","year":"1999","journal-title":"Biochemistry"},{"key":"10.1016\/S0165-6147(00)01973-8_BIB63","first-page":"140","article-title":"Alanine scanning mutagenesis of conserved arginine\/lysine-arginine\/lysine-x-x-arginine\/lysine G protein-activating motifs on m1 muscarinic acetylcholine receptors","volume":"50","author":"Lee","year":"1996","journal-title":"Mol. Pharmacol."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB64","doi-asserted-by":"crossref","first-page":"3809","DOI":"10.1002\/j.1460-2075.1993.tb06059.x","article-title":"Charged amino acids required for signal transduction by the m3 muscarinic acetylcholine receptor","volume":"12","author":"Kunkel","year":"1993","journal-title":"EMBO J."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB65","doi-asserted-by":"crossref","first-page":"1487","DOI":"10.1021\/bi962554d","article-title":"Molecular basis of receptor\/G protein coupling selectivity studied by co-expression of wild type and mutant m2 muscarinic receptors with mutant G\u03b1q subunits","volume":"36","author":"Kostenis","year":"1997","journal-title":"Biochemistry"},{"key":"10.1016\/S0165-6147(00)01973-8_BIB66","doi-asserted-by":"crossref","first-page":"274","DOI":"10.1038\/363274a0","article-title":"Substitution of three amino acids switches receptor specificity of Gq\u03b1 to that of Gi\u03b1","volume":"363","author":"Conklin","year":"1993","journal-title":"Nature"},{"key":"10.1016\/S0165-6147(00)01973-8_BIB67","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1016\/S0955-0674(97)80054-3","article-title":"How receptors talk to trimeric G proteins","volume":"9","author":"Bourne","year":"1997","journal-title":"Curr. Opin. Cell Biol."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB68","doi-asserted-by":"crossref","first-page":"23675","DOI":"10.1074\/jbc.272.38.23675","article-title":"Genetic analysis of receptor\/G\u03b1q coupling selectivity","volume":"272","author":"Kostenis","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB69","doi-asserted-by":"crossref","first-page":"7865","DOI":"10.1074\/jbc.274.12.7865","article-title":"Roles of the transducin \u03b1-subunit \u03b14\u2013helix\/\u03b14\u2013\u03b26 loop in the receptor and effector interactions","volume":"274","author":"Natochin","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB70","doi-asserted-by":"crossref","first-page":"4877","DOI":"10.1073\/pnas.051632898","article-title":"Mapping of contact sites in complex formation between transducin and light-activated rhodopsin by covalent crosslinking: use of a photoactivatable agent","volume":"98","author":"Cai","year":"2001","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB71","doi-asserted-by":"crossref","first-page":"4883","DOI":"10.1073\/pnas.051632998","article-title":"Mapping of contact sites in complex formation between transducin and light-activated rhodopsin by covalent crosslinking: use of a chemically preactivated reagent","volume":"98","author":"Itoh","year":"2001","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB72","doi-asserted-by":"crossref","first-page":"17032","DOI":"10.1016\/S0021-9258(18)41888-1","article-title":"Rhodopsin\/transducin interactions: 1. characterization of the binding of the transducin-\u03b2\u03b3 subunit complex to rhodopsin using fluorescence spectroscopy","volume":"267","author":"Phillips","year":"1992","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB73","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1038\/379311a0","article-title":"The 2.0 \u00c5 crystal structure of a heterotrimeric G protein","volume":"379","author":"Lambright","year":"1996","journal-title":"Nature"},{"key":"10.1016\/S0165-6147(00)01973-8_BIB74","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1016\/S0165-6147(99)01404-2","article-title":"Insights into ligand pharmacology using receptor\u2013G-protein fusion proteins","volume":"21","author":"Milligan","year":"2000","journal-title":"Trends Phamacol. Sci."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB75","doi-asserted-by":"crossref","first-page":"19107","DOI":"10.1074\/jbc.272.31.19107","article-title":"The N-terminal extension of G\u03b1q is critical for constraining the selectivity of receptor coupling","volume":"272","author":"Kostenis","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB76","doi-asserted-by":"crossref","first-page":"1937","DOI":"10.1074\/jbc.275.3.1937","article-title":"Mutation of the fourth cytoplasmic loop of rhodopsin affects binding of transducin and peptides derived from the carboxyl terminal sequences of transducin \u03b1 and \u03b3 subunits","volume":"275","author":"Ernst","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB77","doi-asserted-by":"crossref","first-page":"1930","DOI":"10.1074\/jbc.275.3.1930","article-title":"The amino terminus of the fourth cytoplasmic loop of rhodopsin modulates rhodopsin-transducin interaction","volume":"275","author":"Marin","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB78","doi-asserted-by":"crossref","first-page":"3336","DOI":"10.1074\/jbc.271.7.3336","article-title":"Receptor and membrane interaction sites on G\u03b2: a receptor-derived peptide binds to the carboxyl terminus","volume":"271","author":"Taylor","year":"1996","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0165-6147(00)01973-8_BIB79","doi-asserted-by":"crossref","first-page":"9026","DOI":"10.1074\/jbc.275.12.9026","article-title":"Identification of G\u03b2\u03b3 binding sites in the third intracellular loop of the M3-muscarinic receptor and their role in receptor regulation","volume":"275","author":"Wu","year":"2000","journal-title":"J. Biol. Chem."}],"container-title":["Trends in Pharmacological Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0165614700019738?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0165614700019738?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2021,5,4]],"date-time":"2021-05-04T23:36:26Z","timestamp":1620171386000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0165614700019738"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2002,3]]},"references-count":79,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2002,3]]}},"alternative-id":["S0165614700019738"],"URL":"https:\/\/doi.org\/10.1016\/s0165-6147(00)01973-8","relation":{},"ISSN":["0165-6147"],"issn-type":[{"value":"0165-6147","type":"print"}],"subject":[],"published":{"date-parts":[[2002,3]]}}}