pubmed-article:7870179 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7870179 | lifeskim:mentions | umls-concept:C0001483 | lld:lifeskim |
pubmed-article:7870179 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
pubmed-article:7870179 | lifeskim:mentions | umls-concept:C0040649 | lld:lifeskim |
pubmed-article:7870179 | lifeskim:mentions | umls-concept:C1530358 | lld:lifeskim |
pubmed-article:7870179 | lifeskim:mentions | umls-concept:C1334043 | lld:lifeskim |
pubmed-article:7870179 | lifeskim:mentions | umls-concept:C0301039 | lld:lifeskim |
pubmed-article:7870179 | pubmed:issue | 6517 | lld:pubmed |
pubmed-article:7870179 | pubmed:dateCreated | 1995-3-30 | lld:pubmed |
pubmed-article:7870179 | pubmed:abstractText | The 265K nuclear protein CBP was initially identified as a co-activator for the protein kinase A (PKA)-phosphorylated form of the transcription factor CREB. The domains in CBP that are involved in CREB binding and transcriptional activation are highly related to the adenoviral E1A-associated cellular protein p300 (refs 2, 3), and to two hypothetical proteins from Caenorhabditis elegans, R10E11.1 and K03H1.10 (refs 4 and 5, respectively), whose functions are unknown. Here, we show that CBP and p300 have similar binding affinity for the PKA-phosphorylated form of CREB, and that p300 can substitute for CBP in potentiating CREB-activated gene expression. We find that E1A binds to CBP through a domain conserved with p300 and represses the CREB-dependent co-activator functions of both CBP and p300. Our results indicate that the gene repression and cell immortalization functions associated with E1A involve the inactivation of a family of related proteins that normally participate in second-messenger-regulated gene expression. | lld:pubmed |
pubmed-article:7870179 | pubmed:language | eng | lld:pubmed |
pubmed-article:7870179 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7870179 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:7870179 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7870179 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7870179 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7870179 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7870179 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7870179 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7870179 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7870179 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7870179 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7870179 | pubmed:month | Mar | lld:pubmed |
pubmed-article:7870179 | pubmed:issn | 0028-0836 | lld:pubmed |
pubmed-article:7870179 | pubmed:author | pubmed-author:HarterM LML | lld:pubmed |
pubmed-article:7870179 | pubmed:author | pubmed-author:GoodmanR HRH | lld:pubmed |
pubmed-article:7870179 | pubmed:author | pubmed-author:KwokR PRP | lld:pubmed |
pubmed-article:7870179 | pubmed:author | pubmed-author:LundbladJ RJR | lld:pubmed |
pubmed-article:7870179 | pubmed:author | pubmed-author:LauranceM EME | lld:pubmed |
pubmed-article:7870179 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7870179 | pubmed:day | 2 | lld:pubmed |
pubmed-article:7870179 | pubmed:volume | 374 | lld:pubmed |
pubmed-article:7870179 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7870179 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7870179 | pubmed:pagination | 85-8 | lld:pubmed |
pubmed-article:7870179 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
pubmed-article:7870179 | pubmed:meshHeading | pubmed-meshheading:7870179-... | lld:pubmed |
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pubmed-article:7870179 | pubmed:meshHeading | pubmed-meshheading:7870179-... | lld:pubmed |
pubmed-article:7870179 | pubmed:year | 1995 | lld:pubmed |
pubmed-article:7870179 | pubmed:articleTitle | Adenoviral E1A-associated protein p300 as a functional homologue of the transcriptional co-activator CBP. | lld:pubmed |
pubmed-article:7870179 | pubmed:affiliation | Vollum Institute, Oregon Health Sciences University, Portland 97201. | lld:pubmed |
pubmed-article:7870179 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:7870179 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
entrez-gene:2033 | entrezgene:pubmed | pubmed-article:7870179 | lld:entrezgene |
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