Heterodimerization among thyroid hormone receptor, retinoic acid receptor, retinoid X receptor, chicken ovalbumin upstream promoter transcription factor, and an endogenous liver protein
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Hypothyroidism Side Effect in Patients Treated with Sunitinib or Sorafenib: Clinical and Structural AnalysesThe orphan receptor Rev-ErbA alpha activates transcription via a novel response elementA dynamic balance between ARP-1/COUP-TFII, EAR-3/COUP-TFI, and retinoic acid receptor:retinoid X receptor heterodimers regulates Oct-3/4 expression in embryonal carcinoma cellsCharacterization of a negative retinoic acid response element in the murine Oct4 promoterScreening methods for thyroid hormone disruptors.Axial (HNF3beta) and retinoic acid receptors are regulators of the zebrafish sonic hedgehog promoterRARs and RXRs: evidence for two autonomous transactivation functions (AF-1 and AF-2) and heterodimerization in vivo.PMLRAR homodimers: distinct DNA binding properties and heteromeric interactions with RXRThe patterns of binding of RAR, RXR and TR homo- and heterodimers to direct repeats are dictated by the binding specificites of the DNA binding domains.Homo- and heterodimers of the retinoid X receptor (RXR) activated transcription in yeast.Transactivation and repression of the alpha-fetoprotein gene promoter by retinoid X receptor and chicken ovalbumin upstream promoter transcription factor.Two orphan receptors binding to a common site are involved in the regulation of the oxytocin gene in the bovine ovaryActivation of Six1 Expression in Vertebrate Sensory Neurons.Retinoid X receptor alpha transactivates the hepatitis B virus enhancer 1 element by forming a heterodimeric complex with the peroxisome proliferator-activated receptor.Postnatal exposure to a high-carbohydrate diet interferes epigenetically with thyroid hormone receptor induction of the adult male rat skeletal muscle glucose transporter isoform 4 expression.Epigenetic modulation of the retinoid X receptor alpha by green tea in the azoxymethane-Apc Min/+ mouse model of intestinal cancer.A 10-amino-acid sequence in the N-terminal A/B domain of thyroid hormone receptor alpha is essential for transcriptional activation and interaction with the general transcription factor TFIIB.The monomer-binding orphan receptor Rev-Erb represses transcription as a dimer on a novel direct repeatWidely spaced, directly repeated PuGGTCA elements act as promiscuous enhancers for different classes of nuclear receptors.Functional evidence for ligand-dependent dissociation of thyroid hormone and retinoic acid receptors from an inhibitory cellular factorA novel retinoid X receptor-independent thyroid hormone response element is present in the human type 1 deiodinase gene.Novel mechanism of positive versus negative regulation by thyroid hormone receptor β1 (TRβ1) identified by genome-wide profiling of binding sites in mouse liver.Dimerization interfaces formed between the DNA binding domains determine the cooperative binding of RXR/RAR and RXR/TR heterodimers to DR5 and DR4 elements.Functional architecture of the retina: development and disease.Functional regulation of thyroid hormone receptor variant TR alpha 2 by phosphorylationMolecular mechanisms of COUP-TF-mediated transcriptional repression: evidence for transrepression and active repression.Myocyte-specific enhancer factor 2 and thyroid hormone receptor associate and synergistically activate the alpha-cardiac myosin heavy-chain gene.DNA bending by thyroid hormone receptor: influence of half-site spacing and RXR.Identification of a regulatory function for an orphan receptor in muscle: COUP-TF II affects the expression of the myoD gene family during myogenesisCOUP-TF II homodimers are formed in preference to heterodimers with RXR alpha or TR beta in intact cells.Chicken ovalbumin upstream-promoter transcription factor (COUP-TF) could act as a transcriptional activator or repressor of the mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase geneEndogenous retinoid X receptors can function as hormone receptors in pituitary cells.Heterodimers of photoreceptor-specific nuclear receptor (PNR/NR2E3) and peroxisome proliferator-activated receptor-γ (PPARγ) are disrupted by retinal disease-associated mutations.
P2860
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P2860
Heterodimerization among thyroid hormone receptor, retinoic acid receptor, retinoid X receptor, chicken ovalbumin upstream promoter transcription factor, and an endogenous liver protein
description
1992 nî lūn-bûn
@nan
1992 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
name
Heterodimerization among thyro ...... nd an endogenous liver protein
@ast
Heterodimerization among thyro ...... nd an endogenous liver protein
@en
Heterodimerization among thyro ...... nd an endogenous liver protein
@nl
type
label
Heterodimerization among thyro ...... nd an endogenous liver protein
@ast
Heterodimerization among thyro ...... nd an endogenous liver protein
@en
Heterodimerization among thyro ...... nd an endogenous liver protein
@nl
prefLabel
Heterodimerization among thyro ...... nd an endogenous liver protein
@ast
Heterodimerization among thyro ...... nd an endogenous liver protein
@en
Heterodimerization among thyro ...... nd an endogenous liver protein
@nl
P2093
P356
P1476
Heterodimerization among thyro ...... nd an endogenous liver protein
@en
P2093
P304
P356
10.1210/MEND.6.9.1331778
P407
P577
1992-09-01T00:00:00Z