| pubmed-article:7689721 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7689721 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:7689721 | lifeskim:mentions | umls-concept:C1180347 | lld:lifeskim |
| pubmed-article:7689721 | lifeskim:mentions | umls-concept:C0127306 | lld:lifeskim |
| pubmed-article:7689721 | lifeskim:mentions | umls-concept:C0439064 | lld:lifeskim |
| pubmed-article:7689721 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:7689721 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:7689721 | pubmed:dateCreated | 1993-9-28 | lld:pubmed |
| pubmed-article:7689721 | pubmed:abstractText | A protein product of the mdm-2 oncogene (p90) has been recently shown to associate with the protein encoded by the tumor-suppressor gene p53. The mdm-2 gene was originally identified as a gene amplified in a spontaneously transformed Balb/c 3T3 cell line (3T3DM). This report describes the characterization of mdm-2 gene products and their interactions with the p53 protein. Polyclonal and monoclonal antibodies were generated against murine and human mdm-2 protein. These antibodies detected the mdm-2 p90 protein and at least four additional polypeptides (p85, p76, p74, p58-p57) in cultured cells. These additional proteins may arise from different spliced mRNA forms of the mdm-2 gene or post-translational modifications of the mdm-2 protein. The monoclonal antibodies distinguished at least three sets of mdm-2 proteins with distinct combinations of epitopes (p90 and p85; p76 and p74; p58-57). One or two of these proteins forms a complex with the p53 protein (p90, p58). These mdm-2 proteins were found to be overexpressed in 3T3DM cells and a subset of these proteins were complexed with p53. In 3T3DM cells, p90, like p53, had a short half-life of approximately 20 min and was localized to the cell nucleus. In resting cells stimulated with serum p90 levels and p90/p53 complex levels increased in the late G1 phase of the cell cycle. The p90 mdm-2 protein could regulate p53 activity in the late G1 phase of the cell cycle. | lld:pubmed |
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| pubmed-article:7689721 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:7689721 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7689721 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7689721 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:7689721 | pubmed:issn | 0950-9232 | lld:pubmed |
| pubmed-article:7689721 | pubmed:author | pubmed-author:LevineA JAJ | lld:pubmed |
| pubmed-article:7689721 | pubmed:author | pubmed-author:ChenJJ | lld:pubmed |
| pubmed-article:7689721 | pubmed:author | pubmed-author:OlsonD CDC | lld:pubmed |
| pubmed-article:7689721 | pubmed:author | pubmed-author:MomandJJ | lld:pubmed |
| pubmed-article:7689721 | pubmed:author | pubmed-author:MarechalVV | lld:pubmed |
| pubmed-article:7689721 | pubmed:author | pubmed-author:RomockiCC | lld:pubmed |
| pubmed-article:7689721 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7689721 | pubmed:volume | 8 | lld:pubmed |
| pubmed-article:7689721 | pubmed:geneSymbol | mdm-2 | lld:pubmed |
| pubmed-article:7689721 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7689721 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7689721 | pubmed:pagination | 2353-60 | lld:pubmed |
| pubmed-article:7689721 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:7689721 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:7689721 | pubmed:articleTitle | Identification and characterization of multiple mdm-2 proteins and mdm-2-p53 protein complexes. | lld:pubmed |
| pubmed-article:7689721 | pubmed:affiliation | Department of Molecular Biology, Princeton University, New Jersey 08544-1014. | lld:pubmed |
| pubmed-article:7689721 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7689721 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:7689721 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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