| pubmed-article:9238003 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9238003 | lifeskim:mentions | umls-concept:C1447749 | lld:lifeskim |
| pubmed-article:9238003 | lifeskim:mentions | umls-concept:C1135650 | lld:lifeskim |
| pubmed-article:9238003 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:9238003 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:9238003 | lifeskim:mentions | umls-concept:C0040624 | lld:lifeskim |
| pubmed-article:9238003 | lifeskim:mentions | umls-concept:C0076920 | lld:lifeskim |
| pubmed-article:9238003 | pubmed:issue | 16 | lld:pubmed |
| pubmed-article:9238003 | pubmed:dateCreated | 1997-9-8 | lld:pubmed |
| pubmed-article:9238003 | pubmed:abstractText | The human androgen receptor (AR) is a ligand-activated transcription factor that regulates genes important for male sexual differentiation and development. To better understand the role of the receptor as a transcription factor we have studied the mechanism of action of the N-terminal transactivation function. In a protein-protein interaction assay the AR N terminus (amino acids 142-485) selectively bound to the basal transcription factors TFIIF and the TATA-box-binding protein (TBP). Reconstitution of the transactivation activity in vitro revealed that AR142-485 fused to the LexA protein DNA-binding domain was competent to activate a reporter gene in the presence of a competing DNA template lacking LexA binding sites. Furthermore, consistent with direct interaction with basal transcription factors, addition of recombinant TFIIF relieved squelching of basal transcription by AR142-485. Taken together these results suggest that one mechanism of transcriptional activation by the AR involves binding to TFIIF and recruitment of the transcriptional machinery. | lld:pubmed |
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| pubmed-article:9238003 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9238003 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9238003 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9238003 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9238003 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:9238003 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:9238003 | pubmed:author | pubmed-author:GustafssonJJ | lld:pubmed |
| pubmed-article:9238003 | pubmed:author | pubmed-author:McEwanI JIJ | lld:pubmed |
| pubmed-article:9238003 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9238003 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:9238003 | pubmed:volume | 94 | lld:pubmed |
| pubmed-article:9238003 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9238003 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9238003 | pubmed:pagination | 8485-90 | lld:pubmed |
| pubmed-article:9238003 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:9238003 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9238003 | pubmed:articleTitle | Interaction of the human androgen receptor transactivation function with the general transcription factor TFIIF. | lld:pubmed |
| pubmed-article:9238003 | pubmed:affiliation | Department of Biosciences, Novum, Karolinska Institute, S-141 57 Huddinge, Sweden. iain.mcewan@abdn.ac.uk | lld:pubmed |
| pubmed-article:9238003 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9238003 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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