| pubmed-article:6185233 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6185233 | lifeskim:mentions | umls-concept:C0000742 | lld:lifeskim |
| pubmed-article:6185233 | lifeskim:mentions | umls-concept:C1510411 | lld:lifeskim |
| pubmed-article:6185233 | lifeskim:mentions | umls-concept:C0178539 | lld:lifeskim |
| pubmed-article:6185233 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:6185233 | lifeskim:mentions | umls-concept:C0205307 | lld:lifeskim |
| pubmed-article:6185233 | lifeskim:mentions | umls-concept:C0332197 | lld:lifeskim |
| pubmed-article:6185233 | lifeskim:mentions | umls-concept:C1519726 | lld:lifeskim |
| pubmed-article:6185233 | lifeskim:mentions | umls-concept:C1515655 | lld:lifeskim |
| pubmed-article:6185233 | lifeskim:mentions | umls-concept:C1334043 | lld:lifeskim |
| pubmed-article:6185233 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:6185233 | pubmed:dateCreated | 1983-3-24 | lld:pubmed |
| pubmed-article:6185233 | pubmed:abstractText | The transforming gene product of the Abelson murine leukemia virus (A-MuLV) is a phosphoprotein encoded by combined viral and cellular sequences. Previous work has shown the existence of a serologically crossreactive normal cellular phosphoprotein called NCP150. We have utilized two-dimensional phosphopeptide mapping and phosphoamino acid analysis to compare the structures of NCP150 and wild-type and mutant forms of the A-MuLV protein labeled in vivo with 32P-orthophosphate. This analysis demonstrated clear homology between NCP150 and wild-type A-MuLV protein, but a number of phosphorylation differences were seen. Among them, two specific tyrosine phosphorylations present in all transformation-competent Abelson proteins were not observed in NCP150. No other phosphotyrosine-containing peptides were detected. In addition, transformation-defective mutants isolated from either the P120 or P160 wild-type strain lack phosphotyrosine-containing peptides. Double-infection studies with such transformation-defective and transformation-competent A-MuLV strains show that Abelson viral proteins may be substrates for their own tyrosine-specific kinase activity in vivo. These observations suggest that the phosphotyrosine kinase activity of the abl region may be controlled, and may function, differently in its viral and cellular forms. | lld:pubmed |
| pubmed-article:6185233 | pubmed:language | eng | lld:pubmed |
| pubmed-article:6185233 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6185233 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:6185233 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6185233 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6185233 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6185233 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:6185233 | pubmed:issn | 0092-8674 | lld:pubmed |
| pubmed-article:6185233 | pubmed:author | pubmed-author:WitteO NON | lld:pubmed |
| pubmed-article:6185233 | pubmed:author | pubmed-author:RosenbergNN | lld:pubmed |
| pubmed-article:6185233 | pubmed:author | pubmed-author:WhitlockC ACA | lld:pubmed |
| pubmed-article:6185233 | pubmed:author | pubmed-author:PonticelliA... | lld:pubmed |
| pubmed-article:6185233 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6185233 | pubmed:volume | 29 | lld:pubmed |
| pubmed-article:6185233 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6185233 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6185233 | pubmed:pagination | 953-60 | lld:pubmed |
| pubmed-article:6185233 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:6185233 | pubmed:meshHeading | pubmed-meshheading:6185233-... | lld:pubmed |
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| pubmed-article:6185233 | pubmed:meshHeading | pubmed-meshheading:6185233-... | lld:pubmed |
| pubmed-article:6185233 | pubmed:meshHeading | pubmed-meshheading:6185233-... | lld:pubmed |
| pubmed-article:6185233 | pubmed:meshHeading | pubmed-meshheading:6185233-... | lld:pubmed |
| pubmed-article:6185233 | pubmed:meshHeading | pubmed-meshheading:6185233-... | lld:pubmed |
| pubmed-article:6185233 | pubmed:meshHeading | pubmed-meshheading:6185233-... | lld:pubmed |
| pubmed-article:6185233 | pubmed:meshHeading | pubmed-meshheading:6185233-... | lld:pubmed |
| pubmed-article:6185233 | pubmed:meshHeading | pubmed-meshheading:6185233-... | lld:pubmed |
| pubmed-article:6185233 | pubmed:year | 1982 | lld:pubmed |
| pubmed-article:6185233 | pubmed:articleTitle | In vivo tyrosine phosphorylations of the Abelson virus transforming protein are absent in its normal cellular homolog. | lld:pubmed |
| pubmed-article:6185233 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6185233 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:6185233 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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