| pubmed-article:8389356 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8389356 | lifeskim:mentions | umls-concept:C0040135 | lld:lifeskim |
| pubmed-article:8389356 | lifeskim:mentions | umls-concept:C0376525 | lld:lifeskim |
| pubmed-article:8389356 | lifeskim:mentions | umls-concept:C0140283 | lld:lifeskim |
| pubmed-article:8389356 | lifeskim:mentions | umls-concept:C0040845 | lld:lifeskim |
| pubmed-article:8389356 | lifeskim:mentions | umls-concept:C0042866 | lld:lifeskim |
| pubmed-article:8389356 | lifeskim:mentions | umls-concept:C2698172 | lld:lifeskim |
| pubmed-article:8389356 | lifeskim:mentions | umls-concept:C1708533 | lld:lifeskim |
| pubmed-article:8389356 | pubmed:issue | 16 | lld:pubmed |
| pubmed-article:8389356 | pubmed:dateCreated | 1993-7-7 | lld:pubmed |
| pubmed-article:8389356 | pubmed:abstractText | A subclass of erbA-related nuclear receptors has been shown to require interaction with an auxiliary protein(s) from nuclear extract in order to achieve high affinity DNA binding in vitro. The retinoid X receptor recently has been demonstrated to be such an auxiliary protein as it enhances specific DNA binding by thyroid hormone receptors, retinoic acid receptors, and the vitamin D receptor. Mutation of a highly conserved 20-amino acid region within the ligand-binding domain of thyroid hormone receptor beta disrupts its physical association with auxiliary protein from JEG-3 cells as well as with recombinant retinoid X receptor beta. The homologous 20-amino acid regions from retinoic acid receptor alpha and the vitamin D receptor also are critical determinants of the heterodimeric interaction between these receptors and JEG-3 cell auxiliary protein as well as retinoid X receptor beta. However, the same region of retinoid X receptor beta appears to play a minor, if any, role in heterodimerization. In addition, transfection studies indicate that disruption of heterodimerization impairs the ability of these receptors to function as ligand-dependent transcriptional activators. | lld:pubmed |
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| pubmed-article:8389356 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8389356 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8389356 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8389356 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8389356 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:8389356 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:8389356 | pubmed:author | pubmed-author:KoenigR JRJ | lld:pubmed |
| pubmed-article:8389356 | pubmed:author | pubmed-author:RosenE DED | lld:pubmed |
| pubmed-article:8389356 | pubmed:author | pubmed-author:BeninghofE... | lld:pubmed |
| pubmed-article:8389356 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8389356 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:8389356 | pubmed:volume | 268 | lld:pubmed |
| pubmed-article:8389356 | pubmed:geneSymbol | erbA | lld:pubmed |
| pubmed-article:8389356 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8389356 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8389356 | pubmed:pagination | 11534-41 | lld:pubmed |
| pubmed-article:8389356 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:8389356 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8389356 | pubmed:articleTitle | Dimerization interfaces of thyroid hormone, retinoic acid, vitamin D, and retinoid X receptors. | lld:pubmed |
| pubmed-article:8389356 | pubmed:affiliation | Endocrinology Division, University of Michigan Medical Center, Ann Arbor 48109-0678. | lld:pubmed |
| pubmed-article:8389356 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8389356 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:8389356 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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