pubmed-article:1957170 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:1957170 | lifeskim:mentions | umls-concept:C1705280 | lld:lifeskim |
pubmed-article:1957170 | lifeskim:mentions | umls-concept:C2827404 | lld:lifeskim |
pubmed-article:1957170 | lifeskim:mentions | umls-concept:C0022660 | lld:lifeskim |
pubmed-article:1957170 | lifeskim:mentions | umls-concept:C0230764 | lld:lifeskim |
pubmed-article:1957170 | lifeskim:mentions | umls-concept:C0086376 | lld:lifeskim |
pubmed-article:1957170 | lifeskim:mentions | umls-concept:C0525037 | lld:lifeskim |
pubmed-article:1957170 | lifeskim:mentions | umls-concept:C0081757 | lld:lifeskim |
pubmed-article:1957170 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
pubmed-article:1957170 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:1957170 | pubmed:issue | 5035 | lld:pubmed |
pubmed-article:1957170 | pubmed:dateCreated | 1991-12-27 | lld:pubmed |
pubmed-article:1957170 | pubmed:abstractText | The binding of cytosolic coat proteins to organelles may regulate membrane structure and traffic. Evidence is presented that a small guanosine triphosphate (GTP)-binding protein, the adenosine diphosphate ribosylation factor (ARF), reversibly associates with the Golgi apparatus in an energy, GTP, and fungal metabolite brefeldin A (BFA)-sensitive manner similar to, but distinguishable from, the 110-kilodalton cytosolic coat protein beta-COP. Addition of beta gamma subunits of G proteins inhibited the association of both ARF and beta-COP with Golgi membranes that occurred upon incubation with guanosine 5'-O-(3-thiotriphosphate) (GTP-gamma-S). Thus, heterotrimeric G proteins may function to regulate the assembly of coat proteins onto the Golgi membrane. | lld:pubmed |
pubmed-article:1957170 | pubmed:language | eng | lld:pubmed |
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pubmed-article:1957170 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:1957170 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:1957170 | pubmed:month | Nov | lld:pubmed |
pubmed-article:1957170 | pubmed:issn | 0036-8075 | lld:pubmed |
pubmed-article:1957170 | pubmed:author | pubmed-author:KlausnerR DRD | lld:pubmed |
pubmed-article:1957170 | pubmed:author | pubmed-author:LORDJ PJP | lld:pubmed |
pubmed-article:1957170 | pubmed:author | pubmed-author:DonaldsonJ... | lld:pubmed |
pubmed-article:1957170 | pubmed:author | pubmed-author:Lippincott-Sc... | lld:pubmed |
pubmed-article:1957170 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:1957170 | pubmed:day | 22 | lld:pubmed |
pubmed-article:1957170 | pubmed:volume | 254 | lld:pubmed |
pubmed-article:1957170 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:1957170 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:1957170 | pubmed:pagination | 1197-9 | lld:pubmed |
pubmed-article:1957170 | pubmed:dateRevised | 2007-3-19 | lld:pubmed |
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pubmed-article:1957170 | pubmed:meshHeading | pubmed-meshheading:1957170-... | lld:pubmed |
pubmed-article:1957170 | pubmed:year | 1991 | lld:pubmed |
pubmed-article:1957170 | pubmed:articleTitle | Binding of ARF and beta-COP to Golgi membranes: possible regulation by a trimeric G protein. | lld:pubmed |
pubmed-article:1957170 | pubmed:affiliation | Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892. | lld:pubmed |
pubmed-article:1957170 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:1957170 | pubmed:publicationType | In Vitro | lld:pubmed |
pubmed-article:1957170 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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