Identification of two distinct inactive conformations of the beta2-adrenergic receptor reconciles structural and biochemical observations

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Identification of two distinct inactive conformations of the beta2-adrenergic receptor reconciles structural and biochemical observations is …
instance of (P31):
scholarly articleQ13442814

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P819ADS bibcode2009PNAS..106.4689D
P356DOI10.1073/PNAS.0811065106
P3181OpenCitations bibliographic resource ID4277833
P932PMC publication ID2650503
P698PubMed publication ID19258456
P5875ResearchGate publication ID24174747

P50authorRon Ofer DrorQ59678272
P2093author name stringStefano Piana
David E Shaw
David W Borhani
Morten Ø Jensen
Daniel H Arlow
P2860cites workThe 2.6 angstrom crystal structure of a human A2A adenosine receptor bound to an antagonistQ24654563
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A Specific Cholesterol Binding Site Is Established by the 2.8 Å Structure of the Human β2-Adrenergic ReceptorQ27650801
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GPCR engineering yields high-resolution structural insights into beta2-adrenergic receptor functionQ28254935
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Distinct signaling profiles of beta1 and beta2 adrenergic receptor ligands toward adenylyl cyclase and mitogen-activated protein kinase reveals the pluridimensionality of efficacyQ40298849
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P433issue12
P407language of work or nameEnglishQ1860
P921main subjectbiochemistryQ7094
P304page(s)4689-94
P577publication date2009-03-24
P1433published inProceedings of the National Academy of Sciences of the United States of AmericaQ1146531
P1476titleIdentification of two distinct inactive conformations of the beta2-adrenergic receptor reconciles structural and biochemical observations
P478volume106