pubmed-article:1939135 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:1939135 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
pubmed-article:1939135 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
pubmed-article:1939135 | lifeskim:mentions | umls-concept:C1705433 | lld:lifeskim |
pubmed-article:1939135 | lifeskim:mentions | umls-concept:C0005821 | lld:lifeskim |
pubmed-article:1939135 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:1939135 | lifeskim:mentions | umls-concept:C0061928 | lld:lifeskim |
pubmed-article:1939135 | lifeskim:mentions | umls-concept:C1366537 | lld:lifeskim |
pubmed-article:1939135 | pubmed:issue | 31 | lld:pubmed |
pubmed-article:1939135 | pubmed:dateCreated | 1991-12-13 | lld:pubmed |
pubmed-article:1939135 | pubmed:abstractText | The CDC42Hs protein appears to be an isoform of the ras-related GTP-binding protein G25K and is an apparent human homolog of the Saccharomyces cerevisiae cell-division-cycle protein, CDC42Sc. In this study, we report the identification of a GTPase-activating protein (GAP) for CDC42Hs from human platelets (designated from here on as CDC42Hs-GAP). The CDC42Hs-GAP activity was solubilized from platelet membranes, recovered through successive chromatography steps (the final step being Mono-Q chromatography), and purified approximately 3500-fold. The CDC42Hs-GAP activity appeared to correspond to a polypeptide with an apparent Mr of approximately 25,000. The GTPase activities of the purified human platelet CDC42Hs, the Escherichia coli-recombinant CDC42Hs, and the Spodoptera frugiperda-recombinant GTP-binding proteins are all stimulated by the CDC42Hs-GAP to identical extents, which indicates that the recombinant CDC42Hs proteins are as effective as the native human platelet protein in coupling to the GAP. However, a mutant form of the E. coli-recombinant CDC42Hs which contains a valine residue at position 12 (CDC42HsVal-12) has a significantly reduced intrinsic GTPase activity (relative to the wild type CDC42HsGly-12) which is not stimulated by the CDC42Hs-GAP. The CDC42Hs-GAP also does not stimulate the GTPase activities of the ras or rap GTP-binding proteins; however, it is capable of a weak stimulation of the GTPase activity of mammalian rho. Based on the apparent similarities in the molecular size of the CDC42Hs- and rho-GAPs (i.e. 25-30 kDa), and the cross-reactivity of rho with the CDC42Hs-GAP, it seems likely that the CDC42Hs- and rho-GAPs will constitute a specific subclass of the ras-related GAP superfamily. | lld:pubmed |
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pubmed-article:1939135 | pubmed:language | eng | lld:pubmed |
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pubmed-article:1939135 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:1939135 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:1939135 | pubmed:month | Nov | lld:pubmed |
pubmed-article:1939135 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:1939135 | pubmed:author | pubmed-author:HallAA | lld:pubmed |
pubmed-article:1939135 | pubmed:author | pubmed-author:EvansTT | lld:pubmed |
pubmed-article:1939135 | pubmed:author | pubmed-author:HartM JMJ | lld:pubmed |
pubmed-article:1939135 | pubmed:author | pubmed-author:ShinjoKK | lld:pubmed |
pubmed-article:1939135 | pubmed:author | pubmed-author:CerioneR ARA | lld:pubmed |
pubmed-article:1939135 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:1939135 | pubmed:day | 5 | lld:pubmed |
pubmed-article:1939135 | pubmed:volume | 266 | lld:pubmed |
pubmed-article:1939135 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:1939135 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:1939135 | pubmed:pagination | 20840-8 | lld:pubmed |
pubmed-article:1939135 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:1939135 | pubmed:meshHeading | pubmed-meshheading:1939135-... | lld:pubmed |
pubmed-article:1939135 | pubmed:year | 1991 | lld:pubmed |
pubmed-article:1939135 | pubmed:articleTitle | Identification of the human platelet GTPase activating protein for the CDC42Hs protein. | lld:pubmed |
pubmed-article:1939135 | pubmed:affiliation | Department of Biochemistry, Cellular and Molecular Biology, Cornell University, Ithaca, New York 14853. | lld:pubmed |
pubmed-article:1939135 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:1939135 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:1939135 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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