Linked Life Data

18047571

Source:http://linkedlifedata.com/resource/pubmed/id/18047571

Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:18047571rdf:typepubmed:Citationlld:pubmed
pubmed-article:18047571lifeskim:mentionsumls-concept:C1167395lld:lifeskim
pubmed-article:18047571lifeskim:mentionsumls-concept:C0205145lld:lifeskim
pubmed-article:18047571lifeskim:mentionsumls-concept:C0597357lld:lifeskim
pubmed-article:18047571lifeskim:mentionsumls-concept:C1704675lld:lifeskim
pubmed-article:18047571lifeskim:mentionsumls-concept:C0032150lld:lifeskim
pubmed-article:18047571lifeskim:mentionsumls-concept:C1514562lld:lifeskim
pubmed-article:18047571lifeskim:mentionsumls-concept:C1883221lld:lifeskim
pubmed-article:18047571lifeskim:mentionsumls-concept:C1145667lld:lifeskim
pubmed-article:18047571lifeskim:mentionsumls-concept:C1883204lld:lifeskim
pubmed-article:18047571lifeskim:mentionsumls-concept:C1283195lld:lifeskim
pubmed-article:18047571lifeskim:mentionsumls-concept:C0205214lld:lifeskim
pubmed-article:18047571lifeskim:mentionsumls-concept:C1880371lld:lifeskim
pubmed-article:18047571lifeskim:mentionsumls-concept:C1880389lld:lifeskim
pubmed-article:18047571pubmed:issue1lld:pubmed
pubmed-article:18047571pubmed:dateCreated2007-12-14lld:pubmed
pubmed-article:18047571pubmed:abstractTextThe Duffy binding-like (DBL) domain is a key adhesive module in Plasmodium falciparum, present in both erythrocyte invasion ligands (EBLs) and the large and diverse P. falciparum erythrocyte membrane protein 1 (PfEMP1) family of cytoadherence receptors. DBL domains bind a variety of different host receptors, including intercellular adhesion molecule 1 (ICAM-1), a receptor interaction that may have a role in infected erythrocyte binding to cerebral blood vessels and cerebral malaria. In this study, we expressed the nearly full complement of DBLbeta-C2 domains from the IT4/25/5 (IT4) parasite isolate and showed that ICAM-1-binding domains (DBLbeta-C2(ICAM-1)) were confined to group B and group C PfEMP1 proteins and were not present in group A, suggesting that ICAM-1 selection pressure differs between PfEMP1 groups. To further dissect the molecular determinants of binding, we modelled a DBLbeta-C2(ICAM-1) domain on a solved DBL structure and created alanine substitution mutants in two DBLbeta-C2(ICAM-1) domains. This analysis indicates that the DBLbeta-C2::ICAM-1 interaction maps to the equivalent glycan binding region of EBLs, and suggests a general model for how DBL domains evolve under dual selection for host receptor binding and immune evasion.lld:pubmed
pubmed-article:18047571pubmed:granthttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18047571pubmed:granthttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18047571pubmed:languageenglld:pubmed
pubmed-article:18047571pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18047571pubmed:citationSubsetIMlld:pubmed
pubmed-article:18047571pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18047571pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18047571pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18047571pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18047571pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18047571pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18047571pubmed:statusMEDLINElld:pubmed
pubmed-article:18047571pubmed:monthJanlld:pubmed
pubmed-article:18047571pubmed:issn0950-382Xlld:pubmed
pubmed-article:18047571pubmed:authorpubmed-author:SchiefWilliam...lld:pubmed
pubmed-article:18047571pubmed:authorpubmed-author:KraemerSusan...lld:pubmed
pubmed-article:18047571pubmed:authorpubmed-author:SmithJoseph...lld:pubmed
pubmed-article:18047571pubmed:authorpubmed-author:SpringerAmy...lld:pubmed
pubmed-article:18047571pubmed:authorpubmed-author:HowellDasein...lld:pubmed
pubmed-article:18047571pubmed:authorpubmed-author:PhippardDavid...lld:pubmed
pubmed-article:18047571pubmed:authorpubmed-author:LevinEmily...lld:pubmed
pubmed-article:18047571pubmed:issnTypePrintlld:pubmed
pubmed-article:18047571pubmed:volume67lld:pubmed
pubmed-article:18047571pubmed:ownerNLMlld:pubmed
pubmed-article:18047571pubmed:authorsCompleteYlld:pubmed
pubmed-article:18047571pubmed:pagination78-87lld:pubmed
pubmed-article:18047571pubmed:meshHeadingpubmed-meshheading:18047571...lld:pubmed
pubmed-article:18047571pubmed:meshHeadingpubmed-meshheading:18047571...lld:pubmed
pubmed-article:18047571pubmed:meshHeadingpubmed-meshheading:18047571...lld:pubmed
pubmed-article:18047571pubmed:meshHeadingpubmed-meshheading:18047571...lld:pubmed
pubmed-article:18047571pubmed:meshHeadingpubmed-meshheading:18047571...lld:pubmed
pubmed-article:18047571pubmed:meshHeadingpubmed-meshheading:18047571...lld:pubmed
pubmed-article:18047571pubmed:meshHeadingpubmed-meshheading:18047571...lld:pubmed
pubmed-article:18047571pubmed:meshHeadingpubmed-meshheading:18047571...lld:pubmed
pubmed-article:18047571pubmed:meshHeadingpubmed-meshheading:18047571...lld:pubmed
pubmed-article:18047571pubmed:meshHeadingpubmed-meshheading:18047571...lld:pubmed
pubmed-article:18047571pubmed:meshHeadingpubmed-meshheading:18047571...lld:pubmed
pubmed-article:18047571pubmed:meshHeadingpubmed-meshheading:18047571...lld:pubmed
pubmed-article:18047571pubmed:meshHeadingpubmed-meshheading:18047571...lld:pubmed
pubmed-article:18047571pubmed:meshHeadingpubmed-meshheading:18047571...lld:pubmed
pubmed-article:18047571pubmed:meshHeadingpubmed-meshheading:18047571...lld:pubmed
pubmed-article:18047571pubmed:meshHeadingpubmed-meshheading:18047571...lld:pubmed
pubmed-article:18047571pubmed:meshHeadingpubmed-meshheading:18047571...lld:pubmed
pubmed-article:18047571pubmed:meshHeadingpubmed-meshheading:18047571...lld:pubmed
pubmed-article:18047571pubmed:meshHeadingpubmed-meshheading:18047571...lld:pubmed
pubmed-article:18047571pubmed:meshHeadingpubmed-meshheading:18047571...lld:pubmed
pubmed-article:18047571pubmed:year2008lld:pubmed
pubmed-article:18047571pubmed:articleTitleMapping a common interaction site used by Plasmodium falciparum Duffy binding-like domains to bind diverse host receptors.lld:pubmed
pubmed-article:18047571pubmed:affiliationSeattle Biomedical Research Institute, 307 Westlake Ave N, Ste 500, Seattle, WA 98109-5219, USA.lld:pubmed
pubmed-article:18047571pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:18047571pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
pubmed-article:18047571pubmed:publicationTypeResearch Support, N.I.H., Extramurallld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:18047571lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:18047571lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:18047571lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:18047571lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:18047571lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:18047571lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:18047571lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:18047571lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:18047571lld:pubmed