Linked Life Data

10799524

Source:http://linkedlifedata.com/resource/pubmed/id/10799524

Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:10799524rdf:typepubmed:Citationlld:pubmed
pubmed-article:10799524lifeskim:mentionsumls-concept:C1412520lld:lifeskim
pubmed-article:10799524lifeskim:mentionsumls-concept:C1412811lld:lifeskim
pubmed-article:10799524lifeskim:mentionsumls-concept:C1514562lld:lifeskim
pubmed-article:10799524lifeskim:mentionsumls-concept:C1883221lld:lifeskim
pubmed-article:10799524lifeskim:mentionsumls-concept:C0596260lld:lifeskim
pubmed-article:10799524lifeskim:mentionsumls-concept:C0679622lld:lifeskim
pubmed-article:10799524lifeskim:mentionsumls-concept:C1883204lld:lifeskim
pubmed-article:10799524lifeskim:mentionsumls-concept:C0205314lld:lifeskim
pubmed-article:10799524lifeskim:mentionsumls-concept:C0332120lld:lifeskim
pubmed-article:10799524lifeskim:mentionsumls-concept:C1880389lld:lifeskim
pubmed-article:10799524pubmed:issue19lld:pubmed
pubmed-article:10799524pubmed:dateCreated2000-6-8lld:pubmed
pubmed-article:10799524pubmed:abstractTextWe recently identified BNIP-2, a previously cloned Bcl-2- and E1B-associated protein, as a putative substrate of the FGF receptor tyrosine kinase and showed that it possesses GTPase-activating activity toward Cdc42 despite the lack of homology to previously described catalytic domains of GTPase-activating proteins (GAPs). BNIP-2 contains many arginine residues at the carboxyl terminus, which includes the region of homology to the noncatalytic domain of Cdc42GAP, termed BNIP-2 and Cdc42GAP homology (BCH) domain. Using BNIP-2 glutathione S-transferase recombinants, it was found that its BCH bound Cdc42, and contributed the GAP activity. This domain was predicted to fold into alpha-helical bundles similar to the topology of the catalytic GAP domain of Cdc42GAP. Alignment of exposed arginine residues in this domain helped to identify Arg-235 and Arg-238 as good candidates for catalysis. Arg-238 matched well to the arginine "finger" required for enhanced GTP hydrolysis in homodimerized Cdc42. Site-directed mutagenesis confirmed that an R235K or R238K mutation severely impaired the BNIP-2 GAP activity without affecting its binding to Cdc42. From deletion studies, a region adjacent to the arginine patch ((288)EYV(290) on BNIP-2) and the Switch I and Rho family-specific "Insert" region on Cdc42 are involved in the binding. The results indicate that the BCH domain of BNIP-2 represents a novel GAP domain that employs an arginine patch motif similar to that of the Cdc42-homodimer.lld:pubmed
pubmed-article:10799524pubmed:languageenglld:pubmed
pubmed-article:10799524pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10799524pubmed:citationSubsetIMlld:pubmed
pubmed-article:10799524pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10799524pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10799524pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10799524pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10799524pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10799524pubmed:statusMEDLINElld:pubmed
pubmed-article:10799524pubmed:monthMaylld:pubmed
pubmed-article:10799524pubmed:issn0021-9258lld:pubmed
pubmed-article:10799524pubmed:authorpubmed-author:GuyG RGRlld:pubmed
pubmed-article:10799524pubmed:authorpubmed-author:LowB CBClld:pubmed
pubmed-article:10799524pubmed:authorpubmed-author:SnowS SSSlld:pubmed
pubmed-article:10799524pubmed:issnTypePrintlld:pubmed
pubmed-article:10799524pubmed:day12lld:pubmed
pubmed-article:10799524pubmed:volume275lld:pubmed
pubmed-article:10799524pubmed:ownerNLMlld:pubmed
pubmed-article:10799524pubmed:authorsCompleteYlld:pubmed
pubmed-article:10799524pubmed:pagination14415-22lld:pubmed
pubmed-article:10799524pubmed:dateRevised2006-11-15lld:pubmed
pubmed-article:10799524pubmed:meshHeadingpubmed-meshheading:10799524...lld:pubmed
pubmed-article:10799524pubmed:meshHeadingpubmed-meshheading:10799524...lld:pubmed
pubmed-article:10799524pubmed:meshHeadingpubmed-meshheading:10799524...lld:pubmed
pubmed-article:10799524pubmed:meshHeadingpubmed-meshheading:10799524...lld:pubmed
pubmed-article:10799524pubmed:meshHeadingpubmed-meshheading:10799524...lld:pubmed
pubmed-article:10799524pubmed:meshHeadingpubmed-meshheading:10799524...lld:pubmed
pubmed-article:10799524pubmed:meshHeadingpubmed-meshheading:10799524...lld:pubmed
pubmed-article:10799524pubmed:meshHeadingpubmed-meshheading:10799524...lld:pubmed
pubmed-article:10799524pubmed:meshHeadingpubmed-meshheading:10799524...lld:pubmed
pubmed-article:10799524pubmed:meshHeadingpubmed-meshheading:10799524...lld:pubmed
pubmed-article:10799524pubmed:meshHeadingpubmed-meshheading:10799524...lld:pubmed
pubmed-article:10799524pubmed:meshHeadingpubmed-meshheading:10799524...lld:pubmed
pubmed-article:10799524pubmed:year2000lld:pubmed
pubmed-article:10799524pubmed:articleTitleEvidence for a novel Cdc42GAP domain at the carboxyl terminus of BNIP-2.lld:pubmed
pubmed-article:10799524pubmed:affiliationSignal Transduction Laboratory, Institute of Molecular and Cell Biology, 30 Medical Dr., Singapore 117609, Republic of Singapore.lld:pubmed
pubmed-article:10799524pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:10799524pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
entrez-gene:998entrezgene:pubmedpubmed-article:10799524lld:entrezgene
entrez-gene:392entrezgene:pubmedpubmed-article:10799524lld:entrezgene
entrez-gene:663entrezgene:pubmedpubmed-article:10799524lld:entrezgene
http://linkedlifedata.com/r...entrezgene:pubmedpubmed-article:10799524lld:entrezgene
http://linkedlifedata.com/r...entrezgene:pubmedpubmed-article:10799524lld:entrezgene
http://linkedlifedata.com/r...entrezgene:pubmedpubmed-article:10799524lld:entrezgene
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:10799524lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:10799524lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:10799524lld:pubmed