| pubmed-article:2138725 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2138725 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:2138725 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:2138725 | lifeskim:mentions | umls-concept:C1150527 | lld:lifeskim |
| pubmed-article:2138725 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:2138725 | lifeskim:mentions | umls-concept:C1515926 | lld:lifeskim |
| pubmed-article:2138725 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:2138725 | pubmed:dateCreated | 1990-5-4 | lld:pubmed |
| pubmed-article:2138725 | pubmed:abstractText | We investigated cell cycle-dependent regulation of protein kinase activity encoded by the viral mos gene by using a normal rat kidney cell line (NRK-6m2) chronically infected with a temperature-sensitive mutant (ts110) of Moloney murine sarcoma virus, which produces the P85gag-mos transforming protein. In elutriation experiments, in which cells in various phases of the cell cycle are separated based upon size, a twofold increase in the specific activity of the P85gag-mos protein kinase was observed as cells progressed from G0/G1 through S and G2/M. A three- to fourfold increase in gas-mos protein kinase specific activity relative to unsynchronized cells was observed in mitotic NRK-6m2 cells synchronized by treatment with thymidine followed by colcemid or with nocodazole alone. Interestingly, the gag-mos protein was structurally altered in mitotic cells generating a protein species moving slower than P85gag-mos in SDS-polyacrylamide gels. Our findings indicate that viral mos protein kinase activity is regulated during the cell cycle via phosphorylation. We propose that the mos transforming protein functions in a pleiotropic manner, affecting both cytoplasmic and nuclear targets. | lld:pubmed |
| pubmed-article:2138725 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2138725 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2138725 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2138725 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2138725 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2138725 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2138725 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2138725 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2138725 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2138725 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2138725 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:2138725 | pubmed:issn | 0950-9232 | lld:pubmed |
| pubmed-article:2138725 | pubmed:author | pubmed-author:SinghBB | lld:pubmed |
| pubmed-article:2138725 | pubmed:author | pubmed-author:ArlinghausR... | lld:pubmed |
| pubmed-article:2138725 | pubmed:author | pubmed-author:LayJ TJT | lld:pubmed |
| pubmed-article:2138725 | pubmed:author | pubmed-author:WlodekDD | lld:pubmed |
| pubmed-article:2138725 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2138725 | pubmed:volume | 5 | lld:pubmed |
| pubmed-article:2138725 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2138725 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2138725 | pubmed:pagination | 171-8 | lld:pubmed |
| pubmed-article:2138725 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:2138725 | pubmed:meshHeading | pubmed-meshheading:2138725-... | lld:pubmed |
| pubmed-article:2138725 | pubmed:meshHeading | pubmed-meshheading:2138725-... | lld:pubmed |
| pubmed-article:2138725 | pubmed:meshHeading | pubmed-meshheading:2138725-... | lld:pubmed |
| pubmed-article:2138725 | pubmed:meshHeading | pubmed-meshheading:2138725-... | lld:pubmed |
| pubmed-article:2138725 | pubmed:meshHeading | pubmed-meshheading:2138725-... | lld:pubmed |
| pubmed-article:2138725 | pubmed:meshHeading | pubmed-meshheading:2138725-... | lld:pubmed |
| pubmed-article:2138725 | pubmed:meshHeading | pubmed-meshheading:2138725-... | lld:pubmed |
| pubmed-article:2138725 | pubmed:meshHeading | pubmed-meshheading:2138725-... | lld:pubmed |
| pubmed-article:2138725 | pubmed:meshHeading | pubmed-meshheading:2138725-... | lld:pubmed |
| pubmed-article:2138725 | pubmed:meshHeading | pubmed-meshheading:2138725-... | lld:pubmed |
| pubmed-article:2138725 | pubmed:meshHeading | pubmed-meshheading:2138725-... | lld:pubmed |
| pubmed-article:2138725 | pubmed:meshHeading | pubmed-meshheading:2138725-... | lld:pubmed |
| pubmed-article:2138725 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2138725 | pubmed:articleTitle | Cell cycle-mediated structural and functional alteration of P85gag-mos protein kinase activity. | lld:pubmed |
| pubmed-article:2138725 | pubmed:affiliation | Department of Molecular Pathology, University of Texas M.D. Anderson Cancer Center, Houston 77030. | lld:pubmed |
| pubmed-article:2138725 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2138725 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2138725 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2138725 | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2138725 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2138725 | lld:pubmed |
