FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W1991233048> ?p ?o ?g. }

• W1991233048 endingPage "7931" @default.
• W1991233048 startingPage "7927" @default.
• W1991233048 abstract "To understand the molecular basis of the phosphorylation-enhanced transcriptional activity of human thyroid hormone nuclear receptor subtype beta 1 (hTR beta 1), we studied the effect of phosphorylation on the interaction of hTR beta 1 with the retinoid X receptor beta (RXR beta), we studied the effect of phosphorylation on the interaction of hTR beta 1 with the retinoid X receptor beta (RXR beta). In vitro, the extent of hTR beta 1.RXR beta heterodimer bound to various thyroid hormone response elements (TREs) was compared before and after phosphorylation of hTR beta 1. Without phosphorylation, hTR beta 1.RXR beta heterodimer was barely detectable under the experimental conditions. After phosphorylation of hTR beta 1, heterodimer bound to (i) the chicken lysozyme gene TRE, (ii) a TRE consisting of direct repeats of half-site binding motifs separated by four gaps, and (iii) a palindromic TRE was enhanced by approximately 10-, 7-, and 6-fold, respectively. The effect of phosphorylation on hTR beta 1.RXR beta heterodimerization was reversible. Dephosphorylation of the phosphorylated hTR beta 1 by alkaline phosphatase led to loss of the ability of hTR beta 1 to form a heterodimer with RXR beta in either the absence or the presence of DNA. These results indicate that the heterodimerization is enhanced by phosphorylation. To evaluate the effect of phosphorylation on the interaction of hTR beta 1 with RXR beta in vivo, we cotransfected hTR beta 1, RXR beta and TRE-chloramphenicol acetyltransferase (CAT) expression plasmids into CV-1 cells. CAT activity was assessed in the presence or absence of okadaic acid. Okadaic acid is a potent inhibitor of phosphatases 1 and 2A and increases the in vivo phosphorylation of hTR beta 1 by approximately 10-fold. Using the CAT reporter gene under control of the TRE from the malic enzyme gene, we found that RXR beta increased the okadaic acid-enhanced hTR beta 1-mediated CAT activity by 2- to 3-fold in the presence of 3,3',5-triiodo-L-thyronine. However, 9-cis-retinoic acid did not enhance the effect of okadaic acid. Our results indicate that phosphorylation is essential for the interaction of hTR beta 1 with RXR beta. Thus, phosphorylation plays a pivotal role in the gene-regulating activity of hTR beta 1." @default.
• W1991233048 created "2016-06-24" @default.
• W1991233048 creator A5011463137 @default.
• W1991233048 creator A5029282378 @default.
• W1991233048 creator A5063424506 @default.
• W1991233048 date "1994-08-16" @default.
• W1991233048 modified "2023-10-15" @default.
• W1991233048 title "Phosphorylation enhances the target gene sequence-dependent dimerization of thyroid hormone receptor with retinoid X receptor." @default.
• W1991233048 cites W1501812048 @default.
• W1991233048 cites W1513910831 @default.
• W1991233048 cites W1519834766 @default.
• W1991233048 cites W1558071796 @default.
• W1991233048 cites W1596666097 @default.
• W1991233048 cites W1628490849 @default.
• W1991233048 cites W1896511711 @default.
• W1991233048 cites W1987783037 @default.
• W1991233048 cites W1997873916 @default.
• W1991233048 cites W2029948384 @default.
• W1991233048 cites W2064122825 @default.
• W1991233048 cites W2071839739 @default.
• W1991233048 cites W2075232957 @default.
• W1991233048 cites W2075319759 @default.
• W1991233048 cites W2076690543 @default.
• W1991233048 cites W2082797919 @default.
• W1991233048 cites W2088003425 @default.
• W1991233048 cites W2090244757 @default.
• W1991233048 cites W2117825435 @default.
• W1991233048 cites W2134622570 @default.
• W1991233048 cites W2146131763 @default.
• W1991233048 doi "https://doi.org/10.1073/pnas.91.17.7927" @default.
• W1991233048 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/44517" @default.
• W1991233048 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8058736" @default.
• W1991233048 hasPublicationYear "1994" @default.
• W1991233048 type Work @default.
• W1991233048 sameAs 1991233048 @default.
• W1991233048 citedByCount "55" @default.
• W1991233048 countsByYear W19912330482018 @default.
• W1991233048 countsByYear W19912330482020 @default.
• W1991233048 countsByYear W19912330482021 @default.
• W1991233048 crossrefType "journal-article" @default.
• W1991233048 hasAuthorship W1991233048A5011463137 @default.
• W1991233048 hasAuthorship W1991233048A5029282378 @default.
• W1991233048 hasAuthorship W1991233048A5063424506 @default.
• W1991233048 hasBestOaLocation W19912330482 @default.
• W1991233048 hasConcept C104317684 @default.
• W1991233048 hasConcept C109115496 @default.
• W1991233048 hasConcept C11960822 @default.
• W1991233048 hasConcept C125555471 @default.
• W1991233048 hasConcept C128821507 @default.
• W1991233048 hasConcept C153911025 @default.
• W1991233048 hasConcept C170493617 @default.
• W1991233048 hasConcept C171020997 @default.
• W1991233048 hasConcept C178666793 @default.
• W1991233048 hasConcept C181912034 @default.
• W1991233048 hasConcept C185592680 @default.
• W1991233048 hasConcept C199360897 @default.
• W1991233048 hasConcept C2776174256 @default.
• W1991233048 hasConcept C2776362946 @default.
• W1991233048 hasConcept C41008148 @default.
• W1991233048 hasConcept C55493867 @default.
• W1991233048 hasConcept C63932345 @default.
• W1991233048 hasConcept C758759 @default.
• W1991233048 hasConcept C86339819 @default.
• W1991233048 hasConcept C86803240 @default.
• W1991233048 hasConceptScore W1991233048C104317684 @default.
• W1991233048 hasConceptScore W1991233048C109115496 @default.
• W1991233048 hasConceptScore W1991233048C11960822 @default.
• W1991233048 hasConceptScore W1991233048C125555471 @default.
• W1991233048 hasConceptScore W1991233048C128821507 @default.
• W1991233048 hasConceptScore W1991233048C153911025 @default.
• W1991233048 hasConceptScore W1991233048C170493617 @default.
• W1991233048 hasConceptScore W1991233048C171020997 @default.
• W1991233048 hasConceptScore W1991233048C178666793 @default.
• W1991233048 hasConceptScore W1991233048C181912034 @default.
• W1991233048 hasConceptScore W1991233048C185592680 @default.
• W1991233048 hasConceptScore W1991233048C199360897 @default.
• W1991233048 hasConceptScore W1991233048C2776174256 @default.
• W1991233048 hasConceptScore W1991233048C2776362946 @default.
• W1991233048 hasConceptScore W1991233048C41008148 @default.
• W1991233048 hasConceptScore W1991233048C55493867 @default.
• W1991233048 hasConceptScore W1991233048C63932345 @default.
• W1991233048 hasConceptScore W1991233048C758759 @default.
• W1991233048 hasConceptScore W1991233048C86339819 @default.
• W1991233048 hasConceptScore W1991233048C86803240 @default.
• W1991233048 hasIssue "17" @default.
• W1991233048 hasLocation W19912330481 @default.
• W1991233048 hasLocation W19912330482 @default.
• W1991233048 hasLocation W19912330483 @default.
• W1991233048 hasLocation W19912330484 @default.
• W1991233048 hasOpenAccess W1991233048 @default.
• W1991233048 hasPrimaryLocation W19912330481 @default.
• W1991233048 hasRelatedWork W1986994198 @default.
• W1991233048 hasRelatedWork W1994049684 @default.
• W1991233048 hasRelatedWork W2026140820 @default.
• W1991233048 hasRelatedWork W2032096382 @default.
• W1991233048 hasRelatedWork W2038199810 @default.
• W1991233048 hasRelatedWork W2059625963 @default.
• W1991233048 hasRelatedWork W2068389257 @default.

• next