pubmed-article:7760853 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7760853 | lifeskim:mentions | umls-concept:C0040132 | lld:lifeskim |
pubmed-article:7760853 | lifeskim:mentions | umls-concept:C0034843 | lld:lifeskim |
pubmed-article:7760853 | lifeskim:mentions | umls-concept:C0035687 | lld:lifeskim |
pubmed-article:7760853 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
pubmed-article:7760853 | lifeskim:mentions | umls-concept:C0205419 | lld:lifeskim |
pubmed-article:7760853 | lifeskim:mentions | umls-concept:C1512032 | lld:lifeskim |
pubmed-article:7760853 | lifeskim:mentions | umls-concept:C0600508 | lld:lifeskim |
pubmed-article:7760853 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
pubmed-article:7760853 | lifeskim:mentions | umls-concept:C1979845 | lld:lifeskim |
pubmed-article:7760853 | lifeskim:mentions | umls-concept:C1546856 | lld:lifeskim |
pubmed-article:7760853 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:7760853 | pubmed:dateCreated | 1995-6-26 | lld:pubmed |
pubmed-article:7760853 | pubmed:abstractText | The functionally inactive thyroid hormone receptor splicing variant-alpha 2 (TRv alpha 2) can inhibit transcriptional activation by TR alpha 1 or beta 1, demonstrating a dominant negative effect (DNE). We examine here the three commonly proposed mechanisms, namely, competition for binding to thyroid hormone response elements (TREs), formation of inactive heterodimers, and squelching. A mutation introduced into the DNA-binding domain (DBD) of the TRv alpha 2 was designed to prevent its binding to TREs. In transient cotransfection studies, the DBD mutant has nearly the same DNE as does TRv alpha 2 on three different TRE-containing reporter genes. The DNE of TRv alpha 2 is also not reversed by cotransfection with excess retinoid X receptor-alpha. Extracts of COS cells cotransfected with TR alpha 1 and either TRv alpha 2 or DBD mutant at different ratios were analyzed by gel shift assays. Neither TRv alpha 2 or the mutant altered binding of TR alpha 1 to four radiolabeled TREs. TRv alpha 2 itself can inhibit constitutive transactivation by a thymidine kinase promoter-driven reporter construct. Our results suggest that TRv alpha 2 can function in a dominant negative manner without binding to a TRE, at least for certain TREs. It is concluded that the DNE of TRv alpha 2 may occur through another unrecognized mechanism, perhaps by binding to basal transcription factors. | lld:pubmed |
pubmed-article:7760853 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7760853 | pubmed:language | eng | lld:pubmed |
pubmed-article:7760853 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7760853 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:7760853 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7760853 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7760853 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7760853 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7760853 | pubmed:month | Jan | lld:pubmed |
pubmed-article:7760853 | pubmed:issn | 0888-8809 | lld:pubmed |
pubmed-article:7760853 | pubmed:author | pubmed-author:SuzukiSS | lld:pubmed |
pubmed-article:7760853 | pubmed:author | pubmed-author:DeGrootL JLJ | lld:pubmed |
pubmed-article:7760853 | pubmed:author | pubmed-author:TakedaTT | lld:pubmed |
pubmed-article:7760853 | pubmed:author | pubmed-author:MiyamotoTT | lld:pubmed |
pubmed-article:7760853 | pubmed:author | pubmed-author:LiuR TRT | lld:pubmed |
pubmed-article:7760853 | pubmed:author | pubmed-author:OzataMM | lld:pubmed |
pubmed-article:7760853 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7760853 | pubmed:volume | 9 | lld:pubmed |
pubmed-article:7760853 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7760853 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7760853 | pubmed:pagination | 86-95 | lld:pubmed |
pubmed-article:7760853 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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pubmed-article:7760853 | pubmed:meshHeading | pubmed-meshheading:7760853-... | lld:pubmed |
pubmed-article:7760853 | pubmed:year | 1995 | lld:pubmed |
pubmed-article:7760853 | pubmed:articleTitle | The dominant negative effect of thyroid hormone receptor splicing variant alpha 2 does not require binding to a thyroid response element. | lld:pubmed |
pubmed-article:7760853 | pubmed:affiliation | Department of Medicine, University of Chicago, Illinois 60637, USA. | lld:pubmed |
pubmed-article:7760853 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:7760853 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:7760853 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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