| pubmed-article:18096310 | rdf:type | pubmed:Citation | lld:pubmed |
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| pubmed-article:18096310 | lifeskim:mentions | umls-concept:C1705248 | lld:lifeskim |
| pubmed-article:18096310 | lifeskim:mentions | umls-concept:C1552652 | lld:lifeskim |
| pubmed-article:18096310 | lifeskim:mentions | umls-concept:C1301676 | lld:lifeskim |
| pubmed-article:18096310 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:18096310 | lifeskim:mentions | umls-concept:C1552685 | lld:lifeskim |
| pubmed-article:18096310 | lifeskim:mentions | umls-concept:C1548799 | lld:lifeskim |
| pubmed-article:18096310 | lifeskim:mentions | umls-concept:C1524073 | lld:lifeskim |
| pubmed-article:18096310 | lifeskim:mentions | umls-concept:C1705195 | lld:lifeskim |
| pubmed-article:18096310 | lifeskim:mentions | umls-concept:C0449432 | lld:lifeskim |
| pubmed-article:18096310 | pubmed:issue | 1-2 | lld:pubmed |
| pubmed-article:18096310 | pubmed:dateCreated | 2008-2-18 | lld:pubmed |
| pubmed-article:18096310 | pubmed:abstractText | Set/template-activating factor (TAF)-Ibeta, part of the Set-Can oncogene product found in acute undifferentiated leukemia, is a component of the inhibitor of acetyltransferases (INHAT) complex. Set/TAF-Ibeta interacted with the DNA-binding domain of the glucocorticoid receptor (GR) in yeast two-hybrid screening, and repressed GR-induced transcriptional activity of a chromatin-integrated glucocorticoid-responsive and a natural promoter. Set/TAF-Ibeta was co-precipitated with glucocorticoid response elements (GREs) of these promoters in the absence of dexamethasone, while addition of the hormone caused dissociation of Set/TAF-Ibeta from and attraction of the p160-type coactivator GRIP1 to the promoter GREs. Set-Can fusion protein, on the other hand, did not interact with GR, was constitutively co-precipitated with GREs and suppressed GRIP1-induced enhancement of GR transcriptional activity and histone acetylation. Thus, Set/TAF-Ibeta acts as a ligand-activated GR-responsive transcriptional repressor, while Set-Can does not retain physiologic responsiveness to ligand-bound GR, possibly contributing to the poor responsiveness of Set-Can-harboring leukemic cells to glucocorticoids. | lld:pubmed |
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| pubmed-article:18096310 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:18096310 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:18096310 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18096310 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:18096310 | pubmed:issn | 0303-7207 | lld:pubmed |
| pubmed-article:18096310 | pubmed:author | pubmed-author:ChrousosGeorg... | lld:pubmed |
| pubmed-article:18096310 | pubmed:author | pubmed-author:KinoTomoshige... | lld:pubmed |
| pubmed-article:18096310 | pubmed:author | pubmed-author:IchijoTakamas... | lld:pubmed |
| pubmed-article:18096310 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:18096310 | pubmed:day | 13 | lld:pubmed |
| pubmed-article:18096310 | pubmed:volume | 283 | lld:pubmed |
| pubmed-article:18096310 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18096310 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18096310 | pubmed:pagination | 19-31 | lld:pubmed |
