| pubmed-article:8524800 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8524800 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
| pubmed-article:8524800 | lifeskim:mentions | umls-concept:C0080113 | lld:lifeskim |
| pubmed-article:8524800 | lifeskim:mentions | umls-concept:C1155873 | lld:lifeskim |
| pubmed-article:8524800 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:8524800 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:8524800 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:8524800 | lifeskim:mentions | umls-concept:C1145667 | lld:lifeskim |
| pubmed-article:8524800 | lifeskim:mentions | umls-concept:C2825311 | lld:lifeskim |
| pubmed-article:8524800 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:8524800 | lifeskim:mentions | umls-concept:C2349209 | lld:lifeskim |
| pubmed-article:8524800 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:8524800 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:8524800 | pubmed:issue | 25 | lld:pubmed |
| pubmed-article:8524800 | pubmed:dateCreated | 1996-1-24 | lld:pubmed |
| pubmed-article:8524800 | pubmed:abstractText | An intact T/E1A-binding domain (the pocket) is necessary, but not sufficient, for the retinoblastoma protein (RB) to bind to DNA-protein complexes containing E2F and for RB to induce a G1/S block. Indirect evidence suggests that the binding of RB to E2F may, in addition to inhibiting E2F transactivation function, generate a complex capable of functioning as a transrepressor. Here we show that a chimera in which the E2F1 transactivation domain was replaced with the RB pocket could, in a DNA-binding and pocket-dependent manner, mimic the ability of RB to repress transcription and induce a cell cycle arrest. In contrast, a transdominant negative E2F1 mutant that is capable of blocking E2F-dependent transactivation did not. Fusion of the RB pocket to a heterologous DNA-binding domain unrelated to E2F likewise generated a transrepressor protein when scored against a suitable reporter. These results suggest that growth suppression by RB is due, at least in part, to transrepression mediated by the pocket domain bound to certain promoters via E2F. | lld:pubmed |
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| pubmed-article:8524800 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8524800 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8524800 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8524800 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8524800 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8524800 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8524800 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8524800 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:8524800 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:8524800 | pubmed:author | pubmed-author:KaelinW GWGJr | lld:pubmed |
| pubmed-article:8524800 | pubmed:author | pubmed-author:SellersW RWR | lld:pubmed |
| pubmed-article:8524800 | pubmed:author | pubmed-author:RodgersJ WJW | lld:pubmed |
| pubmed-article:8524800 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8524800 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:8524800 | pubmed:volume | 92 | lld:pubmed |
| pubmed-article:8524800 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8524800 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8524800 | pubmed:pagination | 11544-8 | lld:pubmed |
| pubmed-article:8524800 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:8524800 | pubmed:meshHeading | pubmed-meshheading:8524800-... | lld:pubmed |
| pubmed-article:8524800 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:8524800 | pubmed:articleTitle | A potent transrepression domain in the retinoblastoma protein induces a cell cycle arrest when bound to E2F sites. | lld:pubmed |
| pubmed-article:8524800 | pubmed:affiliation | Dana-Farber Cancer Institute, Boston, MA, USA. | lld:pubmed |
