pubmed-article:9824302 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9824302 | lifeskim:mentions | umls-concept:C1564357 | lld:lifeskim |
pubmed-article:9824302 | lifeskim:mentions | umls-concept:C1421437 | lld:lifeskim |
pubmed-article:9824302 | lifeskim:mentions | umls-concept:C1414357 | lld:lifeskim |
pubmed-article:9824302 | lifeskim:mentions | umls-concept:C1423827 | lld:lifeskim |
pubmed-article:9824302 | lifeskim:mentions | umls-concept:C1148926 | lld:lifeskim |
pubmed-article:9824302 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:9824302 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:9824302 | pubmed:dateCreated | 1998-12-10 | lld:pubmed |
pubmed-article:9824302 | pubmed:abstractText | The highly conserved ATPase p97, a member of the AAA-ATPases, is found in a complex with its co-factor p47 in rat liver cytosol. Previously it had been shown that p97-mediated reassembly of Golgi cisternae from mitotic Golgi fragments requires p47 which mediates the binding of p97 to a Golgi t-SNARE (soluble N-ethylmaleimide-sensitive factor attachment factor receptor), syntaxin 5. Here we show that it also suppresses the ATPase activity of p97 by up to 85% in a dose-dependent and saturable manner suggesting that it has other roles in the membrane fusion cycle. | lld:pubmed |
pubmed-article:9824302 | pubmed:language | eng | lld:pubmed |
pubmed-article:9824302 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9824302 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:9824302 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9824302 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:9824302 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9824302 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9824302 | pubmed:month | Oct | lld:pubmed |
pubmed-article:9824302 | pubmed:issn | 0014-5793 | lld:pubmed |
pubmed-article:9824302 | pubmed:author | pubmed-author:KondoHH | lld:pubmed |
pubmed-article:9824302 | pubmed:author | pubmed-author:WarrenGG | lld:pubmed |
pubmed-article:9824302 | pubmed:author | pubmed-author:MeyerH HHH | lld:pubmed |
pubmed-article:9824302 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9824302 | pubmed:day | 23 | lld:pubmed |
pubmed-article:9824302 | pubmed:volume | 437 | lld:pubmed |
pubmed-article:9824302 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9824302 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9824302 | pubmed:pagination | 255-7 | lld:pubmed |
pubmed-article:9824302 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
pubmed-article:9824302 | pubmed:meshHeading | pubmed-meshheading:9824302-... | lld:pubmed |
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pubmed-article:9824302 | pubmed:meshHeading | pubmed-meshheading:9824302-... | lld:pubmed |
pubmed-article:9824302 | pubmed:meshHeading | pubmed-meshheading:9824302-... | lld:pubmed |
pubmed-article:9824302 | pubmed:meshHeading | pubmed-meshheading:9824302-... | lld:pubmed |
pubmed-article:9824302 | pubmed:meshHeading | pubmed-meshheading:9824302-... | lld:pubmed |
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pubmed-article:9824302 | pubmed:meshHeading | pubmed-meshheading:9824302-... | lld:pubmed |
pubmed-article:9824302 | pubmed:meshHeading | pubmed-meshheading:9824302-... | lld:pubmed |
pubmed-article:9824302 | pubmed:meshHeading | pubmed-meshheading:9824302-... | lld:pubmed |
pubmed-article:9824302 | pubmed:year | 1998 | lld:pubmed |
pubmed-article:9824302 | pubmed:articleTitle | The p47 co-factor regulates the ATPase activity of the membrane fusion protein, p97. | lld:pubmed |
pubmed-article:9824302 | pubmed:affiliation | Cell Biology Laboratory, Imperial Cancer Research Fund, London, UK. | lld:pubmed |
pubmed-article:9824302 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:9824302 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
entrez-gene:83809 | entrezgene:pubmed | pubmed-article:9824302 | lld:entrezgene |
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