pubmed-article:2822968 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2822968 | lifeskim:mentions | umls-concept:C0042666 | lld:lifeskim |
pubmed-article:2822968 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:2822968 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
pubmed-article:2822968 | lifeskim:mentions | umls-concept:C1420280 | lld:lifeskim |
pubmed-article:2822968 | lifeskim:mentions | umls-concept:C1419030 | lld:lifeskim |
pubmed-article:2822968 | lifeskim:mentions | umls-concept:C0392760 | lld:lifeskim |
pubmed-article:2822968 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
pubmed-article:2822968 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
pubmed-article:2822968 | pubmed:issue | 11 | lld:pubmed |
pubmed-article:2822968 | pubmed:dateCreated | 1987-11-30 | lld:pubmed |
pubmed-article:2822968 | pubmed:abstractText | Rabbit antiserum prepared against a cyclic 19-amino-acid peptide predicted from the sequence of the viral mos gene (v-mos) of Moloney murine sarcoma virus not only recognized v-mos gene products but also specifically detected a 55,000-Mr polypeptide expressed in a variety of cells that grow on solid surfaces. This normal cellular protein, previously shown to be reduced in amount in cells expressing the v-mos gene, was found to be the intermediate filament structural protein, vimentin. This conclusion was reached by comparing relative mobilities in denaturing gels, isoelectric points, immunoreactivities, location in the cell, and peptide maps. | lld:pubmed |
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pubmed-article:2822968 | pubmed:language | eng | lld:pubmed |
pubmed-article:2822968 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2822968 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:2822968 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2822968 | pubmed:month | Nov | lld:pubmed |
pubmed-article:2822968 | pubmed:issn | 0022-538X | lld:pubmed |
pubmed-article:2822968 | pubmed:author | pubmed-author:GoldmanRR | lld:pubmed |
pubmed-article:2822968 | pubmed:author | pubmed-author:SinghBB | lld:pubmed |
pubmed-article:2822968 | pubmed:author | pubmed-author:ArlinghausR... | lld:pubmed |
pubmed-article:2822968 | pubmed:author | pubmed-author:HuttonLL | lld:pubmed |
pubmed-article:2822968 | pubmed:author | pubmed-author:HerzogN KNK | lld:pubmed |
pubmed-article:2822968 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2822968 | pubmed:volume | 61 | lld:pubmed |
pubmed-article:2822968 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2822968 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2822968 | pubmed:pagination | 3625-9 | lld:pubmed |
pubmed-article:2822968 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:2822968 | pubmed:meshHeading | pubmed-meshheading:2822968-... | lld:pubmed |
pubmed-article:2822968 | pubmed:year | 1987 | lld:pubmed |
pubmed-article:2822968 | pubmed:articleTitle | The P55 protein affected by v-mos expression is vimentin. | lld:pubmed |
pubmed-article:2822968 | pubmed:affiliation | Department of Molecular Pathology, University of Texas System Cancer Center, M. D. Anderson Hospital and Tumor Institute, Houston 77030. | lld:pubmed |
pubmed-article:2822968 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:2822968 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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