The dimerization interfaces formed between the DNA binding domains of RXR, RAR and TR determine the binding specificity and polarity of the full-length receptors to direct repeats.
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A functional Rev-erb alpha responsive element located in the human Rev-erb alpha promoter mediates a repressing activityCooperative formation of high-order oligomers by retinoid X receptors: an unexpected mode of DNA recognitionCharacterization of the DNA-binding and dimerization properties of the nuclear orphan receptor germ cell nuclear factorStructure of the heterodimeric ecdysone receptor DNA-binding complexRIP-140 interacts with multiple nuclear receptors by means of two distinct sitesThe proliferating cell nuclear antigen regulates retinoic acid receptor transcriptional activity through direct protein-protein interaction.Structure of the RXR-RAR DNA-binding complex on the retinoic acid response element DR1Structural basis of VDR-DNA interactions on direct repeat response elementsStructure of a thyroid hormone receptor DNA-binding domain homodimer bound to an inverted palindrome DNA response elementStructure of the full human RXR/VDR nuclear receptor heterodimer complex with its DR3 target DNANew retinoid X receptor subtypes in zebra fish (Danio rerio) differentially modulate transcription and do not bind 9-cis retinoic acidRetinoic acid actions through mammalian nuclear receptors.Cloning retinoid and peroxisome proliferator-activated nuclear receptors of the Pacific oyster and in silico binding to environmental chemicals.Hif1α down-regulation is associated with transposition of great arteries in mice treated with a retinoic acid antagonist.A mutation mimicking ligand-induced conformational change yields a constitutive RXR that senses allosteric effects in heterodimers.Retinoid X receptor alpha forms tetramers in solution.Agonist ligands mediate the transcriptional response of nuclear receptor heterodimers through distinct stoichiometric assemblies with coactivators.A mollusk retinoic acid receptor (RAR) ortholog sheds light on the evolution of ligand binding.High level transactivation by the ecdysone receptor complex at the core recognition motif.Molecular characterization of RXR (Retinoid X Receptor) gene isoforms from the bivalve species Chlamys farreriStructural basis of natural promoter recognition by the retinoid X nuclear receptor.Retinoid activation of retinoic acid receptors but not of retinoid X receptors promotes cellular differentiation and replication of human cytomegalovirus in embryonal cellsSeparation of retinoid X receptor homo- and heterodimerization functionsNatural vitamin D3 response elements formed by inverted palindromes: polarity-directed ligand sensitivity of vitamin D3 receptor-retinoid X receptor heterodimer-mediated transactivation.Determinants of target gene specificity for ROR alpha 1: monomeric DNA binding by an orphan nuclear receptor.Widely spaced, directly repeated PuGGTCA elements act as promiscuous enhancers for different classes of nuclear receptors.Direct repeats bind the EcR/USP receptor and mediate ecdysteroid responses in Drosophila melanogaster.The receptor-DNA complex determines the retinoid response: a mechanism for the diversification of the ligand signal.Vitamin A and retinoid signaling: genomic and nongenomic effects.Nexus between epidermolysis bullosa and transcriptional regulation by thyroid hormone in epidermal keratinocytesDynamic and combinatorial control of gene expression by nuclear retinoic acid receptors (RARs).Understanding nuclear receptor form and function using structural biologyStructural basis of androgen receptor binding to selective androgen response elements.Retinoid X receptor regulates Nur77/TR3-dependent apoptosis [corrected] by modulating its nuclear export and mitochondrial targeting.Dimerization interfaces formed between the DNA binding domains determine the cooperative binding of RXR/RAR and RXR/TR heterodimers to DR5 and DR4 elements.Activation function 2 (AF-2) of retinoic acid receptor and 9-cis retinoic acid receptor: presence of a conserved autonomous constitutive activating domain and influence of the nature of the response element on AF-2 activity.RAR-specific agonist/antagonists which dissociate transactivation and AP1 transrepression inhibit anchorage-independent cell proliferation.Intron retention generates a novel isoform of the murine vitamin D receptor that acts in a dominant negative way on the vitamin D signaling pathway.Transactivation by the thyroid hormone receptor is dependent on the spacer sequence in hormone response elements containing directly repeated half-sitesSubcellular compartmentalization of docking protein-1 contributes to progression in colorectal cancer.
P2860
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P2860
The dimerization interfaces formed between the DNA binding domains of RXR, RAR and TR determine the binding specificity and polarity of the full-length receptors to direct repeats.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on March 1994
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
The dimerization interfaces fo ...... h receptors to direct repeats.
@en
The dimerization interfaces fo ...... h receptors to direct repeats.
@nl
type
label
The dimerization interfaces fo ...... h receptors to direct repeats.
@en
The dimerization interfaces fo ...... h receptors to direct repeats.
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prefLabel
The dimerization interfaces fo ...... h receptors to direct repeats.
@en
The dimerization interfaces fo ...... h receptors to direct repeats.
@nl
P2093
P2860
P1433
P1476
The dimerization interfaces fo ...... th receptors to direct repeats
@en
P2093
P2860
P304
P356
10.1002/J.1460-2075.1994.TB06396.X
P407
P577
1994-03-01T00:00:00Z