| pubmed-article:7680388 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7680388 | lifeskim:mentions | umls-concept:C0087140 | lld:lifeskim |
| pubmed-article:7680388 | lifeskim:mentions | umls-concept:C1510411 | lld:lifeskim |
| pubmed-article:7680388 | lifeskim:mentions | umls-concept:C0026882 | lld:lifeskim |
| pubmed-article:7680388 | lifeskim:mentions | umls-concept:C0010654 | lld:lifeskim |
| pubmed-article:7680388 | lifeskim:mentions | umls-concept:C0031727 | lld:lifeskim |
| pubmed-article:7680388 | lifeskim:mentions | umls-concept:C1704708 | lld:lifeskim |
| pubmed-article:7680388 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:7680388 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:7680388 | lifeskim:mentions | umls-concept:C1709915 | lld:lifeskim |
| pubmed-article:7680388 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:7680388 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
| pubmed-article:7680388 | lifeskim:mentions | umls-concept:C0032552 | lld:lifeskim |
| pubmed-article:7680388 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
| pubmed-article:7680388 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:7680388 | pubmed:dateCreated | 1993-4-8 | lld:pubmed |
| pubmed-article:7680388 | pubmed:abstractText | Polyomavirus middle T antigen (MT) interacts with several cellular proteins involved in cell proliferation. MT forms complexes with protein phosphatase 2A (PP2A), pp60c-src (and the related kinases c-fyn and c-yes), and phosphatidylinositol-3 kinase. We made a single point mutation in MT, changing a conserved cysteine residue at position 120 to tryptophan, and characterized the biochemical and biological properties of the mutant (C120W) protein. The mutant MT protein does not associate with PP2A, pp60c-src, or phosphatidylinositol-3 kinase as judged by coimmunoprecipitation and associated phosphatase or kinase activity. The C120W mutant is defective in activation of c-fos expression and in morphological transformation of NIH 3T3 cells. | lld:pubmed |
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| pubmed-article:7680388 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7680388 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7680388 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7680388 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:7680388 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7680388 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:7680388 | pubmed:issn | 0022-538X | lld:pubmed |
| pubmed-article:7680388 | pubmed:author | pubmed-author:EckhartWW | lld:pubmed |
| pubmed-article:7680388 | pubmed:author | pubmed-author:GlennG MGM | lld:pubmed |
| pubmed-article:7680388 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7680388 | pubmed:volume | 67 | lld:pubmed |
| pubmed-article:7680388 | pubmed:owner | NLM | lld:pubmed |
