| pubmed-article:3099391 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3099391 | lifeskim:mentions | umls-concept:C0023779 | lld:lifeskim |
| pubmed-article:3099391 | lifeskim:mentions | umls-concept:C0010852 | lld:lifeskim |
| pubmed-article:3099391 | lifeskim:mentions | umls-concept:C0085175 | lld:lifeskim |
| pubmed-article:3099391 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:3099391 | lifeskim:mentions | umls-concept:C1145667 | lld:lifeskim |
| pubmed-article:3099391 | lifeskim:mentions | umls-concept:C2825311 | lld:lifeskim |
| pubmed-article:3099391 | lifeskim:mentions | umls-concept:C2349209 | lld:lifeskim |
| pubmed-article:3099391 | lifeskim:mentions | umls-concept:C1549781 | lld:lifeskim |
| pubmed-article:3099391 | pubmed:issue | 4787 | lld:pubmed |
| pubmed-article:3099391 | pubmed:dateCreated | 1987-2-19 | lld:pubmed |
| pubmed-article:3099391 | pubmed:abstractText | Vinculin, which is associated with the cytoskeleton of many cells, has been suggested as a possible linker between microfilament bundles and the plasma membrane. Here it will be shown that fatty acid is covalently attached to vinculin in vivo. Furthermore, in chicken embryo fibroblasts infected with a temperature-sensitive mutant of Rous sarcoma virus, tsNY68, the acylation of vinculin at the permissive temperature was less than one-third that at the nonpermissive temperature. Thus, the covalent binding of lipid to vinculin is a transformation-sensitive event. The covalent modification of vinculin by lipids could be directly or indirectly involved in its reversible association with membranes. This modification may also provide a mechanism to alter the organization of vinculin within cells and thereby play a regulatory role in anchoring or stabilizing microfilament bundles at plasma membranes. | lld:pubmed |
| pubmed-article:3099391 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3099391 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3099391 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:3099391 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3099391 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:3099391 | pubmed:issn | 0036-8075 | lld:pubmed |
| pubmed-article:3099391 | pubmed:author | pubmed-author:BurtJJ | lld:pubmed |
| pubmed-article:3099391 | pubmed:author | pubmed-author:BurgerM MMM | lld:pubmed |
| pubmed-article:3099391 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3099391 | pubmed:day | 23 | lld:pubmed |
| pubmed-article:3099391 | pubmed:volume | 235 | lld:pubmed |
| pubmed-article:3099391 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3099391 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3099391 | pubmed:pagination | 476-9 | lld:pubmed |
| pubmed-article:3099391 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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| pubmed-article:3099391 | pubmed:meshHeading | pubmed-meshheading:3099391-... | lld:pubmed |
| pubmed-article:3099391 | pubmed:year | 1987 | lld:pubmed |
| pubmed-article:3099391 | pubmed:articleTitle | The cytoskeletal protein vinculin contains transformation-sensitive, covalently bound lipid. | lld:pubmed |
| pubmed-article:3099391 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3099391 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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