| pubmed-article:7673216 | rdf:type | pubmed:Citation | lld:pubmed |
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| pubmed-article:7673216 | lifeskim:mentions | umls-concept:C0018437 | lld:lifeskim |
| pubmed-article:7673216 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:7673216 | lifeskim:mentions | umls-concept:C1879748 | lld:lifeskim |
| pubmed-article:7673216 | lifeskim:mentions | umls-concept:C1706853 | lld:lifeskim |
| pubmed-article:7673216 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:7673216 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
| pubmed-article:7673216 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:7673216 | lifeskim:mentions | umls-concept:C1556066 | lld:lifeskim |
| pubmed-article:7673216 | lifeskim:mentions | umls-concept:C1619636 | lld:lifeskim |
| pubmed-article:7673216 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
| pubmed-article:7673216 | pubmed:issue | 38 | lld:pubmed |
| pubmed-article:7673216 | pubmed:dateCreated | 1995-10-17 | lld:pubmed |
| pubmed-article:7673216 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7673216 | pubmed:abstractText | The Saccharomyces cerevisiae vacuolar H(+)-ATPase (V-ATPase) is a multi-subunit complex that can be structurally and functionally divided into peripheral (V1) and integral membrane (V0) sectors. The vma22-1 mutation was isolated in a screen for mutants defective in V-ATPase function vma22 delta cells contain no V-ATPase activity due to a failure to assemble the enzyme complex; V1 subunits accumulate in the cytosol, and the V0 100-kDa subunit is rapidly degraded. Turnover of the 100-kDa integral membrane protein was found to occur in the endoplasmic reticulum (ER) of vma22 delta cells. The product of the VMA22 gene, Vma22p, is a 21-kDa hydrophilic protein that is not a subunit of the V-ATPase but rather is associated with ER membranes. The association of Vma22p with ER membranes was perturbed by mutations in VMA12, a gene that encodes an ER membrane protein (Vma12p) that is also required for V-ATPase assembly. These results indicate that Vma22p, along with Vma21p and Vma12p, form a set of ER proteins required for V-ATPase assembly. | lld:pubmed |
| pubmed-article:7673216 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7673216 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7673216 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7673216 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7673216 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:7673216 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7673216 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7673216 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:7673216 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:7673216 | pubmed:author | pubmed-author:HillK JKJ | lld:pubmed |
| pubmed-article:7673216 | pubmed:author | pubmed-author:StevensT HTH | lld:pubmed |
| pubmed-article:7673216 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7673216 | pubmed:day | 22 | lld:pubmed |
| pubmed-article:7673216 | pubmed:volume | 270 | lld:pubmed |
| pubmed-article:7673216 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7673216 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7673216 | pubmed:pagination | 22329-36 | lld:pubmed |
| pubmed-article:7673216 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:7673216 | pubmed:meshHeading | pubmed-meshheading:7673216-... | lld:pubmed |
| pubmed-article:7673216 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7673216 | pubmed:articleTitle | Vma22p is a novel endoplasmic reticulum-associated protein required for assembly of the yeast vacuolar H(+)-ATPase complex. | lld:pubmed |
| pubmed-article:7673216 | pubmed:affiliation | Institute of Molecular Biology, University of Oregon, Eugene 97403-1229, USA. | lld:pubmed |
| pubmed-article:7673216 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7673216 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:7673216 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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