| pubmed-article:14668324 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14668324 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:14668324 | lifeskim:mentions | umls-concept:C0034843 | lld:lifeskim |
| pubmed-article:14668324 | lifeskim:mentions | umls-concept:C0140283 | lld:lifeskim |
| pubmed-article:14668324 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:14668324 | lifeskim:mentions | umls-concept:C0023688 | lld:lifeskim |
| pubmed-article:14668324 | lifeskim:mentions | umls-concept:C1709059 | lld:lifeskim |
| pubmed-article:14668324 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:14668324 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:14668324 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:14668324 | pubmed:dateCreated | 2004-2-23 | lld:pubmed |
| pubmed-article:14668324 | pubmed:abstractText | Many members of the type II nuclear receptor subfamily function as heterodimers with the retinoid X receptor (RXR). A permissive heterodimer (e.g. peroxisome proliferator-activated receptor/RXR) allows for ligand binding by both partners of the receptor complex. In contrast, RXR has been thought to be incapable of ligand binding in a nonpermissive heterodimer, such as that of thyroid hormone receptor (TR)/RXR, where it has been referred to as a silent partner. However, we recently presented functional evidence suggesting that RXR in the TR/RXR heterodimer can bind its natural ligand 9-cis-RA in cells. Here we extended our study of the interrelationship of TR and RXR. We examined the potential modulatory effect of RXR and its ligand on the activity of TR, primarily using a Gal4-TR chimera. This study led to several novel and unexpected findings: 1) heterodimerization of apo-RXRalpha (in the absence of 9-cis-RA) with Gal4-TR inhibits T3-mediated transactivation; 2) the inhibition of Gal4-TR activity by RXRalpha is further enhanced by 9-cis-RA; 3) two different RXR subtypes (alpha and beta) differentially modulate the activity of Gal4-TR; 4) the N-terminal A/B domains of RXR alpha and beta are largely responsible for their differential modulation of TR activity; and 5) the RXR ligand 9-cis-RA appears to differentially affect T3-mediated transactivation from the Gal4-TR/RXRalpha (which is inhibited by 9-cis-RA) and TRE-bound TR/RXRalpha (which is further activated by 9-cis-RA) heterodimers. Taken together, these results further support our recent proposal that the RXR component in a TR/RXR heterodimer is not silent and, more importantly, reveal novel aspects of regulation of the activity of the TR/RXR heterodimer by RXR and RXR ligand. | lld:pubmed |
| pubmed-article:14668324 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14668324 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14668324 | pubmed:language | eng | lld:pubmed |
| pubmed-article:14668324 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14668324 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:14668324 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14668324 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14668324 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14668324 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14668324 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14668324 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14668324 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14668324 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14668324 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14668324 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14668324 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14668324 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14668324 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:14668324 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:14668324 | pubmed:author | pubmed-author:YamadaTatsuya... | lld:pubmed |
| pubmed-article:14668324 | pubmed:author | pubmed-author:WangFangF | lld:pubmed |
| pubmed-article:14668324 | pubmed:author | pubmed-author:LiDangshengD | lld:pubmed |
| pubmed-article:14668324 | pubmed:author | pubmed-author:SamuelsHerber... | lld:pubmed |
| pubmed-article:14668324 | pubmed:author | pubmed-author:VulinA IgorAI | lld:pubmed |
| pubmed-article:14668324 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14668324 | pubmed:day | 27 | lld:pubmed |
| pubmed-article:14668324 | pubmed:volume | 279 | lld:pubmed |
| pubmed-article:14668324 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14668324 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14668324 | pubmed:pagination | 7427-37 | lld:pubmed |
| pubmed-article:14668324 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:14668324 | pubmed:meshHeading | pubmed-meshheading:14668324... | lld:pubmed |
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| pubmed-article:14668324 | pubmed:meshHeading | pubmed-meshheading:14668324... | lld:pubmed |
| pubmed-article:14668324 | pubmed:meshHeading | pubmed-meshheading:14668324... | lld:pubmed |
| pubmed-article:14668324 | pubmed:meshHeading | pubmed-meshheading:14668324... | lld:pubmed |
| pubmed-article:14668324 | pubmed:meshHeading | pubmed-meshheading:14668324... | lld:pubmed |
| pubmed-article:14668324 | pubmed:meshHeading | pubmed-meshheading:14668324... | lld:pubmed |
| pubmed-article:14668324 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:14668324 | pubmed:articleTitle | Novel roles of retinoid X receptor (RXR) and RXR ligand in dynamically modulating the activity of the thyroid hormone receptor/RXR heterodimer. | lld:pubmed |
| pubmed-article:14668324 | pubmed:affiliation | Department of Pharmacology, New York University School of Medicine, New York, New York 10016, USA. lid01@med.nyu.edu | lld:pubmed |
| pubmed-article:14668324 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:14668324 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14668324 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14668324 | lld:pubmed |
