pubmed-article:11358671 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:11358671 | lifeskim:mentions | umls-concept:C0034840 | lld:lifeskim |
pubmed-article:11358671 | lifeskim:mentions | umls-concept:C0256079 | lld:lifeskim |
pubmed-article:11358671 | lifeskim:mentions | umls-concept:C0529099 | lld:lifeskim |
pubmed-article:11358671 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
pubmed-article:11358671 | lifeskim:mentions | umls-concept:C1880177 | lld:lifeskim |
pubmed-article:11358671 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:11358671 | pubmed:dateCreated | 2001-5-18 | lld:pubmed |
pubmed-article:11358671 | pubmed:abstractText | Estrogens are essential regulators in the development and control of reproductive functions. The estrogenic signal is now known to be transduced by two estrogen receptors, ERalpha and ERbeta. Hormone-dependent transcriptional activation of ER and other nuclear receptors involves assembly of a coactivation complex which includes various cofactors such as the steroid receptor-coactivators (SRC) and CREB binding protein (CBP). Our findings on ERbeta have revealed a ligand-independent activation pathway which involves growth factor-mediated phosphorylation of ERbeta activation function-1 (AF-1) and subsequent recruitment of SRC-1 independently of the presence of estrogens. The presence of the cointegrator CBP is also shown to potentiate the SRC-1-mediated ERbeta ligand-independent activation, suggesting that CBP may participate in unliganded ERbeta coactivation. These findings demonstrate the ability of alternate signaling pathways to mediate coregulator assembly, hence resulting in ligand-independent activation of ERbeta. | lld:pubmed |
pubmed-article:11358671 | pubmed:language | eng | lld:pubmed |
pubmed-article:11358671 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11358671 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:11358671 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11358671 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:11358671 | pubmed:month | Apr | lld:pubmed |
pubmed-article:11358671 | pubmed:issn | 0960-0760 | lld:pubmed |
pubmed-article:11358671 | pubmed:author | pubmed-author:TremblayAA | lld:pubmed |
pubmed-article:11358671 | pubmed:author | pubmed-author:GiguèreVV | lld:pubmed |
pubmed-article:11358671 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:11358671 | pubmed:volume | 77 | lld:pubmed |
pubmed-article:11358671 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:11358671 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:11358671 | pubmed:pagination | 19-27 | lld:pubmed |
pubmed-article:11358671 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:11358671 | pubmed:year | 2001 | lld:pubmed |
pubmed-article:11358671 | pubmed:articleTitle | Contribution of steroid receptor coactivator-1 and CREB binding protein in ligand-independent activity of estrogen receptor beta. | lld:pubmed |
pubmed-article:11358671 | pubmed:affiliation | Ste-Justine Hospital Research Center, University of Montreal, Montréal, QC, Canada H3T 1C5. atremblay@justine.umontreal.ca | lld:pubmed |
pubmed-article:11358671 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:11358671 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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