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rdf:type |
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lifeskim:mentions |
umls-concept:C0086418,
umls-concept:C0181586,
umls-concept:C0205314,
umls-concept:C0243192,
umls-concept:C0390418,
umls-concept:C0558295,
umls-concept:C0600115,
umls-concept:C0679622,
umls-concept:C1527178,
umls-concept:C1705938,
umls-concept:C1707689,
umls-concept:C1710548
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pubmed:issue |
26
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pubmed:dateCreated |
2005-12-21
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pubmed:abstractText |
Combining molecular dynamics (MD) in a hydrated phospholipid (DOPC) bilayer, a Monte Carlo search, and synthesis of locked nucleotide analogues, we discovered that the Southern conformation of the ribose is preferred for ligand recognition by the P2Y(6) receptor. 2'-Deoxy-(S)-methanocarbaUDP was found to be a full agonist of the receptor and displayed a 10-fold higher potency than that for the corresponding flexible 2'-deoxyUDP. MD results also suggested a conformational change of the second extracellular loop consequent to agonist binding.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/16366591-10090736,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16366591-10329657,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16366591-10841798,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16366591-11754592,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16366591-11959804,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16366591-15465340,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16366591-15481977,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16366591-15768031,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16366591-15774473,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16366591-16121038,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16366591-8628736,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16366591-8809162,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16366591-9281613
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0022-2623
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
29
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pubmed:volume |
48
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
8108-11
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:16366591-Humans,
pubmed-meshheading:16366591-Ligands,
pubmed-meshheading:16366591-Models, Molecular,
pubmed-meshheading:16366591-Molecular Conformation,
pubmed-meshheading:16366591-Purinergic P2 Receptor Agonists,
pubmed-meshheading:16366591-Receptors, Purinergic P2,
pubmed-meshheading:16366591-Tumor Cells, Cultured,
pubmed-meshheading:16366591-Uridine Diphosphate
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pubmed:year |
2005
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pubmed:articleTitle |
Human P2Y(6) receptor: molecular modeling leads to the rational design of a novel agonist based on a unique conformational preference.
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pubmed:affiliation |
NIDDK, National Institutes of Health, DHHS, Bethesda, Maryland 20892. USA. stefanoc@mail.nih.gov
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Intramural
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