| pubmed-article:17185393 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17185393 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:17185393 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:17185393 | lifeskim:mentions | umls-concept:C0205147 | lld:lifeskim |
| pubmed-article:17185393 | lifeskim:mentions | umls-concept:C0665341 | lld:lifeskim |
| pubmed-article:17185393 | lifeskim:mentions | umls-concept:C0040624 | lld:lifeskim |
| pubmed-article:17185393 | lifeskim:mentions | umls-concept:C0872079 | lld:lifeskim |
| pubmed-article:17185393 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:17185393 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:17185393 | lifeskim:mentions | umls-concept:C1709059 | lld:lifeskim |
| pubmed-article:17185393 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:17185393 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:17185393 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:17185393 | pubmed:dateCreated | 2007-3-28 | lld:pubmed |
| pubmed-article:17185393 | pubmed:abstractText | The estrogen receptor (ER)alpha is a biologically and clinically important ligand-modulated transcription factor. The F domain of the ERalpha modulates its functions in a ligand-, promoter-, and cell-specific manner. To identify the region(s) responsible for these functions, we characterized the effects of serial truncations within the F domain. We found that truncating the last 16 residues of the F domain altered the activity of the human ERalpha (hERalpha) on an estrogen response element-driven promoter in response to estradiol or 4-hydroxytamoxifen (4-OHT), its sensitivity to overexpression of the coactivator steroid receptor coactivator-1 in mammalian cells, and its interaction with a receptor-interacting domain of the coactivator steroid receptor coactivator-1 or engineered proteins ("monobodies") that specifically bind to ERalpha/ligand complexes in a yeast two-hybrid system. Most importantly, the ability of the ER to induce pS2 was reduced in MDA-MB-231 cells stably expressing this truncated ER vs. the wild-type ER. The region includes a distinctive segment (residues 579-584; LQKYYIT) having a high content of bulky and/or hydrophobic amino acids that was previously predicted to adopt a beta-strand-like structure. As previously reported, removal of the entire F domain was necessary to eliminate the agonist activity of 4-OHT. In addition, mutation of the vicinal glycine residues between the ligand-binding domain and F domains specifically reduced the 4-OHT-dependent interactions of the hERalpha ligand-binding domain and F domains with monobodies. These results show that regions within the F domain of the hERalpha selectively modulate its activity and its interactions with other proteins. | lld:pubmed |
| pubmed-article:17185393 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17185393 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17185393 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17185393 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17185393 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17185393 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:17185393 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17185393 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17185393 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:17185393 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17185393 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:17185393 | pubmed:issn | 0888-8809 | lld:pubmed |
| pubmed-article:17185393 | pubmed:author | pubmed-author:KoideAkikoA | lld:pubmed |
| pubmed-article:17185393 | pubmed:author | pubmed-author:KoideShoheiS | lld:pubmed |
| pubmed-article:17185393 | pubmed:author | pubmed-author:Deighton-Coll... | lld:pubmed |
| pubmed-article:17185393 | pubmed:author | pubmed-author:ZhaoChangqing... | lld:pubmed |
| pubmed-article:17185393 | pubmed:author | pubmed-author:SkafarDebra... | lld:pubmed |
| pubmed-article:17185393 | pubmed:author | pubmed-author:AbramsJudithJ | lld:pubmed |
| pubmed-article:17185393 | pubmed:author | pubmed-author:NaganumaMisuz... | lld:pubmed |
| pubmed-article:17185393 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17185393 | pubmed:volume | 21 | lld:pubmed |
| pubmed-article:17185393 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17185393 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17185393 | pubmed:pagination | 829-42 | lld:pubmed |
| pubmed-article:17185393 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:17185393 | pubmed:meshHeading | pubmed-meshheading:17185393... | lld:pubmed |
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| pubmed-article:17185393 | pubmed:meshHeading | pubmed-meshheading:17185393... | lld:pubmed |
| pubmed-article:17185393 | pubmed:meshHeading | pubmed-meshheading:17185393... | lld:pubmed |
| pubmed-article:17185393 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17185393 | pubmed:articleTitle | Identification of regions within the F domain of the human estrogen receptor alpha that are important for modulating transactivation and protein-protein interactions. | lld:pubmed |
| pubmed-article:17185393 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois 60637, USA. | lld:pubmed |
| pubmed-article:17185393 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17185393 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:17185393 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:17185393 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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