Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:10648402rdf:typepubmed:Citationlld:pubmed
pubmed-article:10648402lifeskim:mentionsumls-concept:C0005821lld:lifeskim
pubmed-article:10648402lifeskim:mentionsumls-concept:C0596901lld:lifeskim
pubmed-article:10648402lifeskim:mentionsumls-concept:C0042971lld:lifeskim
pubmed-article:10648402lifeskim:mentionsumls-concept:C0017968lld:lifeskim
pubmed-article:10648402lifeskim:mentionsumls-concept:C1517773lld:lifeskim
pubmed-article:10648402lifeskim:mentionsumls-concept:C1167622lld:lifeskim
pubmed-article:10648402lifeskim:mentionsumls-concept:C0439855lld:lifeskim
pubmed-article:10648402lifeskim:mentionsumls-concept:C0441463lld:lifeskim
pubmed-article:10648402lifeskim:mentionsumls-concept:C1514873lld:lifeskim
pubmed-article:10648402pubmed:issue3lld:pubmed
pubmed-article:10648402pubmed:dateCreated2000-2-24lld:pubmed
pubmed-article:10648402pubmed:abstractTextThe platelet glycoprotein (GP) Ib-IX-V complex mediates adhesion to von Willebrand factor (vWf) in (patho)physiologic thrombus formation. The vWf-binding site on GP Ib-IX-V is within the N-terminal 282 residues of GP Ibalpha, which consist of an N-terminal flanking sequence (His-1-Ile-35), 7 leucine-rich repeats (Leu-36-Ala-200), a C-terminal flank (Phe-201-Gly-268), and a sulfated tyrosine sequence (Asp-269-Glu-282). We have used mammalian cell expression of canine-human chimeras of GP Ibalpha, corresponding to precise structural boundaries, to demonstrate the first specific requirement for individual leucine-rich repeats for binding of vWf either induced by a modulator, ristocetin, or under hydrodynamic flow. Implicit in this approach was that the GP Ibalpha chimeras retained a functional conformation, a supposition confirmed by analyzing restoration of function to reversed human-canine chimeras and demonstrating that all chimeras bound vWf activated by botrocetin, a modulator that is indiscriminate between species. Leucine-rich repeats 2, 3, and 4 of GP Ibalpha were identified as being critical for vWf adhesion to GP Ib-IX-V.lld:pubmed
pubmed-article:10648402pubmed:granthttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10648402pubmed:keywordhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10648402pubmed:languageenglld:pubmed
pubmed-article:10648402pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10648402pubmed:citationSubsetAIMlld:pubmed
pubmed-article:10648402pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10648402pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10648402pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10648402pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10648402pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10648402pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10648402pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10648402pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10648402pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10648402pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10648402pubmed:statusMEDLINElld:pubmed
pubmed-article:10648402pubmed:monthFeblld:pubmed
pubmed-article:10648402pubmed:issn0006-4971lld:pubmed
pubmed-article:10648402pubmed:authorpubmed-author:McIntireL VLVlld:pubmed
pubmed-article:10648402pubmed:authorpubmed-author:KennyDDlld:pubmed
pubmed-article:10648402pubmed:authorpubmed-author:BerndtM CMClld:pubmed
pubmed-article:10648402pubmed:authorpubmed-author:ShenYYlld:pubmed
pubmed-article:10648402pubmed:authorpubmed-author:LópezJ AJAlld:pubmed
pubmed-article:10648402pubmed:authorpubmed-author:DongJ FJFlld:pubmed
pubmed-article:10648402pubmed:authorpubmed-author:AndrewsR KRKlld:pubmed
pubmed-article:10648402pubmed:authorpubmed-author:RomoG MGMlld:pubmed
pubmed-article:10648402pubmed:authorpubmed-author:SchadeAAlld:pubmed
pubmed-article:10648402pubmed:authorpubmed-author:WhisstockJ...lld:pubmed
pubmed-article:10648402pubmed:issnTypePrintlld:pubmed
pubmed-article:10648402pubmed:day1lld:pubmed
pubmed-article:10648402pubmed:volume95lld:pubmed
pubmed-article:10648402pubmed:ownerNLMlld:pubmed
pubmed-article:10648402pubmed:authorsCompleteYlld:pubmed
pubmed-article:10648402pubmed:pagination903-10lld:pubmed
pubmed-article:10648402pubmed:dateRevised2007-11-14lld:pubmed
pubmed-article:10648402pubmed:meshHeadingpubmed-meshheading:10648402...lld:pubmed
pubmed-article:10648402pubmed:meshHeadingpubmed-meshheading:10648402...lld:pubmed
pubmed-article:10648402pubmed:meshHeadingpubmed-meshheading:10648402...lld:pubmed
pubmed-article:10648402pubmed:meshHeadingpubmed-meshheading:10648402...lld:pubmed
pubmed-article:10648402pubmed:meshHeadingpubmed-meshheading:10648402...lld:pubmed
pubmed-article:10648402pubmed:meshHeadingpubmed-meshheading:10648402...lld:pubmed
pubmed-article:10648402pubmed:meshHeadingpubmed-meshheading:10648402...lld:pubmed
pubmed-article:10648402pubmed:meshHeadingpubmed-meshheading:10648402...lld:pubmed
pubmed-article:10648402pubmed:meshHeadingpubmed-meshheading:10648402...lld:pubmed
pubmed-article:10648402pubmed:meshHeadingpubmed-meshheading:10648402...lld:pubmed
pubmed-article:10648402pubmed:meshHeadingpubmed-meshheading:10648402...lld:pubmed
pubmed-article:10648402pubmed:meshHeadingpubmed-meshheading:10648402...lld:pubmed
pubmed-article:10648402pubmed:meshHeadingpubmed-meshheading:10648402...lld:pubmed
pubmed-article:10648402pubmed:meshHeadingpubmed-meshheading:10648402...lld:pubmed
pubmed-article:10648402pubmed:meshHeadingpubmed-meshheading:10648402...lld:pubmed
pubmed-article:10648402pubmed:meshHeadingpubmed-meshheading:10648402...lld:pubmed
pubmed-article:10648402pubmed:meshHeadingpubmed-meshheading:10648402...lld:pubmed
pubmed-article:10648402pubmed:meshHeadingpubmed-meshheading:10648402...lld:pubmed
pubmed-article:10648402pubmed:meshHeadingpubmed-meshheading:10648402...lld:pubmed
pubmed-article:10648402pubmed:meshHeadingpubmed-meshheading:10648402...lld:pubmed
pubmed-article:10648402pubmed:meshHeadingpubmed-meshheading:10648402...lld:pubmed
pubmed-article:10648402pubmed:meshHeadingpubmed-meshheading:10648402...lld:pubmed
pubmed-article:10648402pubmed:year2000lld:pubmed
pubmed-article:10648402pubmed:articleTitleRequirement of leucine-rich repeats of glycoprotein (GP) Ibalpha for shear-dependent and static binding of von Willebrand factor to the platelet membrane GP Ib-IX-V complex.lld:pubmed
pubmed-article:10648402pubmed:affiliationHazel and Pip Appel Vascular Biology Laboratory, Baker Medical Research Institute, Melbourne, Australia.lld:pubmed
pubmed-article:10648402pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:10648402pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
pubmed-article:10648402pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:10648402lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:10648402lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:10648402lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:10648402lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:10648402lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:10648402lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:10648402lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:10648402lld:pubmed