| pubmed-article:10559858 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10559858 | lifeskim:mentions | umls-concept:C1506928 | lld:lifeskim |
| pubmed-article:10559858 | lifeskim:mentions | umls-concept:C1705438 | lld:lifeskim |
| pubmed-article:10559858 | lifeskim:mentions | umls-concept:C0077678 | lld:lifeskim |
| pubmed-article:10559858 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:10559858 | lifeskim:mentions | umls-concept:C0699900 | lld:lifeskim |
| pubmed-article:10559858 | lifeskim:mentions | umls-concept:C0243125 | lld:lifeskim |
| pubmed-article:10559858 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:10559858 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:10559858 | pubmed:dateCreated | 1999-12-7 | lld:pubmed |
| pubmed-article:10559858 | pubmed:abstractText | The transcription factor E2F-1 is important in the control of cell proliferation. Its activity must be tightly regulated in a cell-cycle-dependent manner to enable programs of gene expression to be coupled closely with cell-cycle position. Here we show that, following its accumulation in the late G1 phase of the cell cycle, E2F-1 is rapidly degraded in S/G2 phase. This event is linked to a specific interaction of E2F-1 with the F-box-containing protein p45SKP2, which is the cell-cycle-regulated component of the ubiquitin-protein ligase SCFSKP2 that recognizes substrates for this ligase. Disruption of the interaction between E2F-1 and p45SKP2 results in a reduction in ubiquitination of E2F-1 and the stabilization and accumulation of transcriptionally active E2F-1 protein. These results indicate that an SCFSKP2-dependent ubiquitination pathway may be involved in the downregulation of E2F-1 activity in the S/G2 phase of the cell cycle, and suggest a link between SCFSKP2 and cell-cycle-dependent gene control. | lld:pubmed |
| pubmed-article:10559858 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10559858 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:10559858 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10559858 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10559858 | pubmed:month | May | lld:pubmed |
| pubmed-article:10559858 | pubmed:issn | 1465-7392 | lld:pubmed |
| pubmed-article:10559858 | pubmed:author | pubmed-author:MartiAA | lld:pubmed |
| pubmed-article:10559858 | pubmed:author | pubmed-author:ScheffnerMM | lld:pubmed |
| pubmed-article:10559858 | pubmed:author | pubmed-author:KreyAA | lld:pubmed |
| pubmed-article:10559858 | pubmed:author | pubmed-author:WirbelauerCC | lld:pubmed |
| pubmed-article:10559858 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10559858 | pubmed:volume | 1 | lld:pubmed |
| pubmed-article:10559858 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10559858 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10559858 | pubmed:pagination | 14-9 | lld:pubmed |
| pubmed-article:10559858 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:10559858 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10559858 | pubmed:articleTitle | Interaction between ubiquitin-protein ligase SCFSKP2 and E2F-1 underlies the regulation of E2F-1 degradation. | lld:pubmed |
| pubmed-article:10559858 | pubmed:affiliation | Friedrich Miescher Institut, Basel, Switzerland. | lld:pubmed |
| pubmed-article:10559858 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10559858 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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