21364764

Source:http://linkedlifedata.com/resource/pubmed/id/21364764

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0035499, umls-concept:C0035820, umls-concept:C0597225, umls-concept:C1519623
pubmed:issue	2
pubmed:dateCreated	2011-3-2
pubmed:abstractText	Rhodopsin, the prototypic member of G protein-coupled receptors (GPCRs), undergoes isomerization of 11-cis-retinal to all-trans-retinal upon photoactivation. Although the basic mechanism by which rhodopsin is activated is well understood, the roles of whole transmembrane (TM) helix-III during rhodopsin photoactivation in detail are not completely clear.
pubmed:grant	http://linkedlifedata.com/resource/pubmed/grant/EY11716, http://linkedlifedata.com/resource/pubmed/grant/GM28289
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pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/101285081
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Cysteine, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Mutant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Rhodopsin
pubmed:status	MEDLINE
pubmed:issn	1932-6203
pubmed:author	pubmed-author:KhoranaH GobindHG, pubmed-author:KimJong-MyoungJM, pubmed-author:OuWen-binWB, pubmed-author:YiTingfangT
pubmed:issnType	Electronic
pubmed:volume	6
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	e17398
pubmed:meshHeading	pubmed-meshheading:21364764-Amino Acid Sequence, pubmed-meshheading:21364764-Animals, pubmed-meshheading:21364764-COS Cells, pubmed-meshheading:21364764-Catalysis, pubmed-meshheading:21364764-Cercopithecus aethiops, pubmed-meshheading:21364764-Cysteine, pubmed-meshheading:21364764-Light, pubmed-meshheading:21364764-Membrane Proteins, pubmed-meshheading:21364764-Models, Biological, pubmed-meshheading:21364764-Molecular Sequence Data, pubmed-meshheading:21364764-Mutagenesis, Site-Directed, pubmed-meshheading:21364764-Mutant Proteins, pubmed-meshheading:21364764-Photochemical Processes, pubmed-meshheading:21364764-Protein Interaction Domains and Motifs, pubmed-meshheading:21364764-Protein Structure, Secondary, pubmed-meshheading:21364764-Rhodopsin
pubmed:year	2011
pubmed:articleTitle	The roles of transmembrane domain helix-III during rhodopsin photoactivation.
pubmed:affiliation	Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts, United States of America. ouwb75@gmail.com
pubmed:publicationType	Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, N.I.H., Extramural