| pubmed-article:8700863 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8700863 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:8700863 | lifeskim:mentions | umls-concept:C0101671 | lld:lifeskim |
| pubmed-article:8700863 | lifeskim:mentions | umls-concept:C1418833 | lld:lifeskim |
| pubmed-article:8700863 | lifeskim:mentions | umls-concept:C1540057 | lld:lifeskim |
| pubmed-article:8700863 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:8700863 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:8700863 | lifeskim:mentions | umls-concept:C0332256 | lld:lifeskim |
| pubmed-article:8700863 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:8700863 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:8700863 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:8700863 | pubmed:dateCreated | 1996-9-5 | lld:pubmed |
| pubmed-article:8700863 | pubmed:abstractText | The alpha subunits of the heterotrimeric guanine nucleotide-binding proteins (G proteins) hydrolyze GTP at a rate significantly higher than do most members of the Ras family of approximatelly 20-kDa GTP-binding proteins, which depend on a GTPase-activating protein (GAP) for acceleration of GTP hydrolysis. It has been demonstrated that an inserted domain in the G-protein alpha subunit, not present in the much smaller Ras-like proteins, is responsible for this difference [Markby, D. W., Onrust, R. & Bourne, H. R. (1993) Science 262, 1895-1900]. We report here that ARD1, a 64-kDa protein with an 18-kDa carboxyl-terminal ADP-ribosylation factor (ARF) domain, exhibited significant GTPase activity, whereas the ARF domain, expressed as a recombinant protein in Escherichia coli, did not. Addition of the 46-kDa amino-terminal extension (similarly synthesized in E. coli) to the GTP-binding ARF-domain of ARD1 enhanced GTPase activity and inhibited GDP dissociation. The kinetic properties of mixtures of the ARF and non-ARF domains were similar to those of an intact recombinant ARD1. Physical association of the two proteins was demonstrated directly by gel filtration and by using the immobilized non-ARF domain. Thus, like the alpha subunits of heterotrimeric G proteins, ARD1 appears to consist of two domains that interact to regulate the biological activity of the protein. | lld:pubmed |
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| pubmed-article:8700863 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8700863 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8700863 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8700863 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8700863 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:8700863 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:8700863 | pubmed:author | pubmed-author:VaughanMM | lld:pubmed |
| pubmed-article:8700863 | pubmed:author | pubmed-author:MossJJ | lld:pubmed |
| pubmed-article:8700863 | pubmed:author | pubmed-author:VitaliJJ | lld:pubmed |
| pubmed-article:8700863 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8700863 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:8700863 | pubmed:volume | 93 | lld:pubmed |
| pubmed-article:8700863 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8700863 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8700863 | pubmed:pagination | 1941-4 | lld:pubmed |
| pubmed-article:8700863 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:8700863 | pubmed:meshHeading | pubmed-meshheading:8700863-... | lld:pubmed |
| pubmed-article:8700863 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8700863 | pubmed:articleTitle | ARD1, a 64-kDa bifunctional protein containing an 18-kDa GTP-binding ADP-ribosylation factor domain and a 46-kDa GTPase-activating domain. | lld:pubmed |
| pubmed-article:8700863 | pubmed:affiliation | Pulmonary-Critical Care Medicine Branch, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA. | lld:pubmed |
| pubmed-article:8700863 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8700863 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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