{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,13]],"date-time":"2026-02-13T13:45:17Z","timestamp":1770990317764,"version":"3.50.1"},"reference-count":66,"publisher":"Elsevier BV","issue":"2","license":[{"start":{"date-parts":[[1997,4,1]],"date-time":"1997-04-01T00:00:00Z","timestamp":859852800000},"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":["Current Opinion in Cell Biology"],"published-print":{"date-parts":[[1997,4]]},"DOI":"10.1016\/s0955-0674(97)80054-3","type":"journal-article","created":{"date-parts":[[2002,7,25]],"date-time":"2002-07-25T10:32:55Z","timestamp":1027593175000},"page":"134-142","source":"Crossref","is-referenced-by-count":468,"title":["How receptors talk to trimeric G proteins"],"prefix":"10.1016","volume":"9","author":[{"given":"Henry R","family":"Bourne","sequence":"first","affiliation":[]}],"member":"78","reference":[{"key":"10.1016\/S0955-0674(97)80054-3_BIB1","doi-asserted-by":"crossref","first-page":"164","DOI":"10.1038\/371164a0","article-title":"Rapid GDP release from Gs\u03b1 in patients with gain and loss of endocrine function","volume":"371","author":"Iiri","year":"1994","journal-title":"Nature"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB2_1","doi-asserted-by":"crossref","first-page":"1047","DOI":"10.1016\/0092-8674(95)90220-1","article-title":"The structure of the G protein heterotrimer Gl\u03b11\u03b21\u03b32","volume":"83","author":"Wall","year":"1995","journal-title":"Cell"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB3_1","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\/S0955-0674(97)80054-3_BIB4_1","doi-asserted-by":"crossref","first-page":"7507","DOI":"10.1073\/pnas.93.15.7507","article-title":"Evolutionarily conserved G\u03b1\u03b2\u03b3 binding surfaces support a model of the G protein\u2014receptor complex","volume":"93","author":"Lichtarge","year":"1996","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB5","doi-asserted-by":"crossref","first-page":"631","DOI":"10.1016\/0092-8674(93)90245-L","article-title":"Structural elements of G\u03b1 subunits that interact with G\u03b2\u03b3, receptors, and effectors","volume":"73","author":"Conklin","year":"1993","journal-title":"Cell"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB6","doi-asserted-by":"crossref","first-page":"4460","DOI":"10.1002\/j.1460-2075.1995.tb00125.x","article-title":"Transducin-\u03b1 C-terminal mutations present activation by rhodopsin: a new assay using recombinant proteins expressed in cultured cells","volume":"14","author":"Garcia","year":"1995","journal-title":"EMBO J"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB7","doi-asserted-by":"crossref","first-page":"745","DOI":"10.1096\/fasebj.9.9.7601339","article-title":"The family of G-protein-coupled receptors","volume":"9","author":"Strader","year":"1995","journal-title":"FASEB J"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB8","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\/S0955-0674(97)80054-3_BIB9","doi-asserted-by":"crossref","first-page":"770","DOI":"10.1038\/362770a0","article-title":"Projection structure of rhodopsin","volume":"362","author":"Schertler","year":"1993","journal-title":"Nature"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB10_1","doi-asserted-by":"crossref","first-page":"11578","DOI":"10.1073\/pnas.92.25.11578","article-title":"Projection structure of frog rhodopsin in two crystal forms","volume":"92","author":"Schertler","year":"1995","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB11","doi-asserted-by":"crossref","first-page":"1693","DOI":"10.1002\/j.1460-2075.1993.tb05814.x","article-title":"The probable arrangement of the helices in G protein-coupled receptors","volume":"12","author":"Baldwin","year":"1993","journal-title":"EMBO J"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB12","doi-asserted-by":"crossref","first-page":"7564","DOI":"10.1016\/S0021-9258(18)83271-9","article-title":"Palmitoylation of the human \u03b22-adrenergic receptor","volume":"264","author":"O'Dowd","year":"1989","journal-title":"J Biol Chem"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB13","first-page":"12","article-title":"Structure determination of the fourth cytoplasmic loop and carboxyl terminal domain of bovine rhodopsin","volume":"2","author":"Yeagle","year":"1996","journal-title":"Mol Vision"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB14","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1016\/0955-0674(94)90135-X","article-title":"Expanding horizons for receptors coupled to G proteins: diversity and disease","volume":"6","author":"Coughlin","year":"1994","journal-title":"Curr Opin Cell Biol"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB15","doi-asserted-by":"crossref","first-page":"6188","DOI":"10.1128\/MCB.15.11.6188","article-title":"Functional coupling of a mammalian somatostatin receptor to the yeast pheromone response pathway","volume":"15","author":"Price","year":"1995","journal-title":"Mol Cell Biol"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB16_1","doi-asserted-by":"crossref","first-page":"825","DOI":"10.1016\/0896-6273(95)90226-0","article-title":"Mapping the binding-site crevice of the dopamine D2 receptor by the substituted-cysteine accessibility method","volume":"14","author":"Javitch","year":"1995","journal-title":"Neuron"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB17_1","doi-asserted-by":"crossref","first-page":"11278","DOI":"10.1021\/bi960928x","article-title":"Residues in the seventh membrane-spanning segment of the dopamine D2 receptor accessible in the binding-site crevice","volume":"35","author":"Fu","year":"1996","journal-title":"Biochemistry"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB18","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/0896-6273(92)90034-B","article-title":"Constitutively active mutants of rhodopsin","volume":"9","author":"Robinson","year":"1992","journal-title":"Neuron"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB19","doi-asserted-by":"crossref","first-page":"6524","DOI":"10.1016\/S0021-9258(17)37403-3","article-title":"Active site-directed inactivation of constitutively active mutants of rhodopsin","volume":"269","author":"Govardhan","year":"1994","journal-title":"J Biol Chem"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB20","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1016\/0301-4622(95)00030-2","article-title":"Photoactivated state of rhodopsin and how it can form","volume":"56","author":"Fahmy","year":"1995","journal-title":"Biophys Chem"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB21","doi-asserted-by":"crossref","first-page":"1416","DOI":"10.1126\/science.8248781","article-title":"Photoactivated conformational changes in rhodopsin: a time-resolved spin label study","volume":"262","author":"Farahbakhsh","year":"1993","journal-title":"Science"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB22_1","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\/S0955-0674(97)80054-3_BIB23_1","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 labeling study","volume":"35","author":"Altenbach","year":"1996","journal-title":"Biochemistry"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB24_1","doi-asserted-by":"crossref","first-page":"768","DOI":"10.1126\/science.274.5288.768","article-title":"A light-activated conformational switch in rhodopsin","volume":"274","author":"Farrens","year":"1996","journal-title":"Science"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB25","doi-asserted-by":"crossref","first-page":"566","DOI":"10.1016\/S0959-440X(94)90219-4","article-title":"Investigation of structure and dynamics in membrane proteins using site-directed spin labeling","volume":"4","author":"Hubbell","year":"1994","journal-title":"Curr Opin Struct Biol"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB26","doi-asserted-by":"crossref","first-page":"11149","DOI":"10.1021\/bi960858u","article-title":"Specific tryptophan UV-absorbance changes are probes of the transition of rhodopsin to its active state","volume":"35","author":"Lin","year":"1996","journal-title":"Biochemistry"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB27","doi-asserted-by":"crossref","first-page":"347","DOI":"10.1038\/383347a0","article-title":"Rhodopsin activation blocked by metal-ion-binding sites linking transmembrane helices C and F","volume":"383","author":"Sheikh","year":"1996","journal-title":"Nature"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB28_1","doi-asserted-by":"crossref","first-page":"10580","DOI":"10.1074\/jbc.270.18.10580","article-title":"Characterization of rhodopsin mutants that bind transducin but fail to induce GTP nucleotide uptake. Classification of mutant pigments by fluorescence, nucleotide release, and flash-induced light-scattering assays","volume":"270","author":"Ernst","year":"1995","journal-title":"J Biol Chem"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB29","doi-asserted-by":"crossref","first-page":"25406","DOI":"10.1074\/jbc.271.41.25406","article-title":"Modulation of GDP release from transducin by the conserved Glu134\u2014Arg135 sequence in rhodopsin","volume":"271","author":"Acharya","year":"1996","journal-title":"J Biol Chem"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB30","doi-asserted-by":"crossref","first-page":"23879","DOI":"10.1016\/S0021-9258(19)51020-1","article-title":"A conserved carboxylic acid group mediates light-dependent proton uptake and signaling by rhodopsin","volume":"269","author":"Arnis","year":"1994","journal-title":"J Biol Chem"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB31","doi-asserted-by":"crossref","first-page":"14767","DOI":"10.1016\/S0021-9258(18)42106-0","article-title":"Structure and function in rhodopsin. Studies of the interaction between the rhodopsin cytoplasmic domain and transducin","volume":"267","author":"Franke","year":"1992","journal-title":"J Biol Chem"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB32","doi-asserted-by":"crossref","first-page":"7229","DOI":"10.1021\/bi00079a020","article-title":"Regulation of the rhodopsin\u2014transducin interaction by a highly conserved carboxylic acid group","volume":"32","author":"Fahmy","year":"1993","journal-title":"Biochemistry"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB33","doi-asserted-by":"crossref","first-page":"1430","DOI":"10.1016\/S0021-9258(18)45962-5","article-title":"Constitutive activation of the \u03b11B-adrenergic receptor by all amino acid substitutions at a single site. Evidence for a region which constrains receptor activation","volume":"267","author":"Kjelsberg","year":"1992","journal-title":"J Biol Chem"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB34","doi-asserted-by":"crossref","first-page":"16483","DOI":"10.1016\/S0021-9258(19)85445-5","article-title":"Constitutively active mutants of the \u03b12-adrenergic receptor","volume":"268","author":"Ren","year":"1993","journal-title":"J Biol Chem"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB35","doi-asserted-by":"crossref","first-page":"9921","DOI":"10.1073\/pnas.90.21.9921","article-title":"Mutations that alter the third cytoplasmic loop of the a-factor receptor lead to a constitutive and hypersensitive phenotype","volume":"90","author":"Boone","year":"1993","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB36","doi-asserted-by":"crossref","first-page":"22470","DOI":"10.1074\/jbc.271.37.22470","article-title":"Transmembrane regions V and VI of the human luteinizing hormone receptor are required for constitutive activation by a mutation in the third intracellular loop","volume":"271","author":"Kudo","year":"1996","journal-title":"J Biol Chem"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB37","doi-asserted-by":"crossref","first-page":"424","DOI":"10.1038\/358424a0","article-title":"Different \u03b2-subunits determine G-protein interaction with transmembrane receptors","volume":"358","author":"Kleuss","year":"1992","journal-title":"Nature"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB38","doi-asserted-by":"crossref","first-page":"832","DOI":"10.1126\/science.8094261","article-title":"Selectivity in signal transduction determined by \u03b3 subunits of heterotrimeric G proteins","volume":"259","author":"Kleuss","year":"1993","journal-title":"Science"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB39","doi-asserted-by":"crossref","first-page":"832","DOI":"10.1126\/science.3136547","article-title":"Site of G protein binding to rhodopsin mapped with synthetic peptides from the \u03b1 subunit","volume":"241","author":"Hamm","year":"1988","journal-title":"Science"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB40","doi-asserted-by":"crossref","first-page":"276","DOI":"10.1038\/363276a0","article-title":"NMR structure of a receptor-bound G-protein peptide","volume":"363","author":"Dratz","year":"1993","journal-title":"Nature"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB41","doi-asserted-by":"crossref","first-page":"274","DOI":"10.1038\/363274a0","article-title":"Substitution of three amino acids switches receptor specificity of Gi\u03b1 to that of Gi\u03b1","volume":"363","author":"Conklin","year":"1993","journal-title":"Nature"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB42","doi-asserted-by":"crossref","first-page":"429","DOI":"10.1146\/annurev.pa.36.040196.002241","article-title":"Diversity and selectivity of receptor\u2014G protein interaction","volume":"36","author":"Gudermann","year":"1996","journal-title":"Annu Rev Pharmacol Toxicol"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB43","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1146\/annurev.bi.63.070194.000533","article-title":"Structure and function of G protein-coupled receptors","volume":"63","author":"Strader","year":"1994","journal-title":"Annu Rev Biochem"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB44","doi-asserted-by":"crossref","first-page":"166","DOI":"10.1038\/365166a0","article-title":"Alternative splicing of C-terminal tail of prostaglandin E receptor subtype EP3 determines G-protein specificity","volume":"365","author":"Namba","year":"1993","journal-title":"Nature"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB45","doi-asserted-by":"crossref","first-page":"18968","DOI":"10.1016\/S0021-9258(17)32261-5","article-title":"Chimeric muscarinic cholinergic:beta-adrenergic receptors that are functionally promiscuous among G proteins","volume":"269","author":"Wong","year":"1994","journal-title":"J Biol Chem"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB46","doi-asserted-by":"crossref","first-page":"19283","DOI":"10.1074\/jbc.271.32.19283","article-title":"The luteinizing hormone\/chorionic gonadotropin receptor has distinct transmembrane conductors for cAMP and inositol phosphate signals","volume":"271","author":"Gilchrist","year":"1996","journal-title":"J Biol Chem"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB47","first-page":"112","article-title":"Constitutive activation of a single effector pathway: evidence for multiple activation states of a G protein-coupled receptor","volume":"49","author":"Perez","year":"1996","journal-title":"Mol Pharmacol"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB48_1","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1126\/science.275.5298.381","article-title":"Receptor and \u03b2\u03b3 binding sites in the \u03b1 subunit of the retinal G protein transducin","volume":"275","author":"Onrust","year":"1997","journal-title":"Science"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB49_1","doi-asserted-by":"crossref","first-page":"11642","DOI":"10.1073\/pnas.92.25.11642","article-title":"Identification of a receptor\/G-protein contact site critical for signaling specificity and G-protein activation","volume":"92","author":"Liu","year":"1995","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB50","doi-asserted-by":"crossref","first-page":"19532","DOI":"10.1074\/jbc.270.33.19532","article-title":"Mutational analysis of the relative orientation of transmembrane helices I and VII in G protein-coupled receptors","volume":"270","author":"Liu","year":"1995","journal-title":"J Biol Chem"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB51","first-page":"165","article-title":"A reciprocal mutation supports helix 2 and helix 7 proximity in the gonadotropin-releasing hormone receptor","volume":"45","author":"Zhou","year":"1994","journal-title":"Mol Pharmacol"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB52","doi-asserted-by":"crossref","first-page":"14963","DOI":"10.1021\/bi00046a002","article-title":"A general method for mapping tertiary contacts between amino acid residues in membrane-embedded proteins","volume":"34","author":"Yu","year":"1995","journal-title":"Biochemistry"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB53","doi-asserted-by":"crossref","first-page":"14040","DOI":"10.1021\/bi962113u","article-title":"Structure and function in rhodopsin. Cysteines 65 and 316 are in proximity in a rhodopsin mutant as indicated by disulfide formation and interactions between attached spin labels","volume":"35","author":"Yang","year":"1996","journal-title":"Biochemistry"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB54","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1038\/374074a0","article-title":"Conversion of antagonist-binding site to metal-ion site in the tachykinin NK-1 receptor","volume":"374","author":"Elling","year":"1995","journal-title":"Nature"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB55","doi-asserted-by":"crossref","first-page":"6213","DOI":"10.1002\/j.1460-2075.1996.tb01011.x","article-title":"Connectivity and orientation of the seven helical bundle in the tachykinin NK-1 receptor probed by zinc site engineering","volume":"15","author":"Elling","year":"1996","journal-title":"EMBO J"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB56","doi-asserted-by":"crossref","first-page":"2387","DOI":"10.1074\/jbc.271.5.2387","article-title":"Arrangement of transmembrane domains in adrenergic receptors. Similarity to bacteriorhodopsin","volume":"271","author":"Mizobe","year":"1996","journal-title":"J Biol Chem"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB57","doi-asserted-by":"crossref","first-page":"7980","DOI":"10.1073\/pnas.91.17.7980","article-title":"Insertion mutagenesis as a tool to predict the secondary structure of a muscarinic receptor domain determining specificity of G-protein coupling","volume":"91","author":"Bluml","year":"1994","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB58","doi-asserted-by":"crossref","first-page":"3058","DOI":"10.1074\/jbc.271.6.3058","article-title":"Structure of a G-protein-coupling domain of a muscarinic receptor predicted by random saturation mutagenesis","volume":"271","author":"Hill-Eubanks","year":"1996","journal-title":"J Biol Chem"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB59","doi-asserted-by":"crossref","first-page":"12464","DOI":"10.1021\/bi960848t","article-title":"Structure and function in rhodopsin. Single cysteine substitution mutants in the cytoplasmic interhelical E\u2013F loop region show position-specific effects in transducin activation","volume":"35","author":"Yang","year":"1996","journal-title":"Biochemistry"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB60","doi-asserted-by":"crossref","first-page":"14621","DOI":"10.1021\/bi00045a002","article-title":"Structure of the third cytoplasmic loop of bovine rhodopsin","volume":"34","author":"Yeagle","year":"1995","journal-title":"Biochemistry"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB61","doi-asserted-by":"crossref","first-page":"8998","DOI":"10.1021\/ja960454p","article-title":"Peptide mimetic of the third cytoplasmic loop of the PTH\/PTHrP receptor","volume":"118","author":"Mierke","year":"1996","journal-title":"J Am Chem Soc"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB62","doi-asserted-by":"crossref","first-page":"3141","DOI":"10.1074\/jbc.270.7.3141","article-title":"Structure\u2014function of muscarinic receptor coupling to G proteins. Random saturation mutagenesis identifies a critical determinant of receptor affinity for G proteins","volume":"270","author":"Burstein","year":"1995","journal-title":"J Biol Chem"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB63","doi-asserted-by":"crossref","first-page":"27618","DOI":"10.1016\/S0021-9258(18)47029-9","article-title":"Binding of an alpha 2 adrenergic receptor third intracellular loop peptide to G beta and the amino terminus of G alpha","volume":"269","author":"Taylor","year":"1994","journal-title":"J Biol Chem"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB64","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\/S0955-0674(97)80054-3_BIB65","doi-asserted-by":"crossref","first-page":"17032","DOI":"10.1016\/S0021-9258(18)41888-1","article-title":"Rhodopsin\/transducin interactions. I. Characterization of the binding of the transducin-beta gamma subunit complex to rhodopsin using fluorescence spectroscopy","volume":"267","author":"Phillips","year":"1992","journal-title":"J Biol Chem"},{"key":"10.1016\/S0955-0674(97)80054-3_BIB66","doi-asserted-by":"crossref","first-page":"351","DOI":"10.1042\/bj2990351","article-title":"A C-terminal peptide of bovine rhodopsin binds to the transducin alpha-subunit and facilitates its activation","volume":"299","author":"Phillips","year":"1994","journal-title":"Biochem J"}],"container-title":["Current Opinion in Cell Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0955067497800543?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0955067497800543?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2021,5,4]],"date-time":"2021-05-04T12:41:10Z","timestamp":1620132070000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0955067497800543"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1997,4]]},"references-count":66,"journal-issue":{"issue":"2","published-print":{"date-parts":[[1997,4]]}},"alternative-id":["S0955067497800543"],"URL":"https:\/\/doi.org\/10.1016\/s0955-0674(97)80054-3","relation":{},"ISSN":["0955-0674"],"issn-type":[{"value":"0955-0674","type":"print"}],"subject":[],"published":{"date-parts":[[1997,4]]}}}