The conserved ninth C-terminal heptad in thyroid hormone and retinoic acid receptors mediates diverse responses by affecting heterodimer but not homodimer formation.
about
NRIF3 is a novel coactivator mediating functional specificity of nuclear hormone receptorsA new family of nuclear receptor coregulators that integrate nuclear receptor signaling through CREB-binding proteinThe tau 4 activation domain of the thyroid hormone receptor is required for release of a putative corepressor(s) necessary for transcriptional silencingDifferential transactivation by two isoforms of the orphan nuclear hormone receptor CARNew retinoid X receptor subtypes in zebra fish (Danio rerio) differentially modulate transcription and do not bind 9-cis retinoic acidRegulation of the mdm2 oncogene by thyroid hormone receptorThe peptide near the C terminus regulates receptor CAR nuclear translocation induced by xenochemicals in mouse liver.Physical and functional interaction of the Epstein-Barr virus BZLF1 transactivator with the retinoic acid receptors RAR alpha and RXR alpha.Recombinant thyroid hormone receptor and retinoid X receptor stimulate ligand-dependent transcription in vitro.Thyroid hormone response element half-site organization and its effect on thyroid hormone mediated transcription.Cell type-dependent modulation of the dominant negative action of human mutant thyroid hormone beta 1 receptorsDeterminants of target gene specificity for ROR alpha 1: monomeric DNA binding by an orphan nuclear receptor.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 repeatConstitutive activation of gene expression by thyroid hormone receptor results from reversal of p53-mediated repression.Mutations that alter ligand-induced switches and dimerization activities in the retinoid X receptorFunctional evidence for ligand-dependent dissociation of thyroid hormone and retinoic acid receptors from an inhibitory cellular factorLigand-dependent occupancy of the retinoic acid receptor beta 2 promoter in vivo.A thyroid hormone receptor mutation that dissociates thyroid hormone regulation of gene expression in vivo.Multiple mutations contribute to repression by the v-Erb A oncoprotein.Dimerization interfaces formed between the DNA binding domains determine the cooperative binding of RXR/RAR and RXR/TR heterodimers to DR5 and DR4 elements.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.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.Peroxisome proliferator-activated receptor mediates cross-talk with thyroid hormone receptor by competition for retinoid X receptor. Possible role of a leucine zipper-like heptad repeat.Expression of human all-trans-retinoic acid receptor beta and its ligand-binding domain in Escherichia coli.Ligand modulates the interaction of thyroid hormone receptor beta with the basal transcription machinery.Functional regulation of thyroid hormone receptor variant TR alpha 2 by phosphorylationMutations of CpG dinucleotides located in the triiodothyronine (T3)-binding domain of the thyroid hormone receptor (TR) beta gene that appears to be devoid of natural mutations may not be detected because they are unlikely to produce the clinical phA zebrafish ftz-F1 (Fushi tarazu factor 1) homologue requires multiple subdomains in the D and E regions for its transcriptional activity.Novel regulation of keratin gene expression by thyroid hormone and retinoid receptors.Transcriptional silencing by unliganded thyroid hormone receptor beta requires a soluble corepressor that interacts with the ligand-binding domain of the receptor.Functional evidence for retinoid X receptor (RXR) as a nonsilent partner in the thyroid hormone receptor/RXR heterodimer.The ligand-binding domains of the thyroid hormone/retinoid receptor gene subfamily function in vivo to mediate heterodimerization, gene silencing, and transactivation.Tissue-specific distribution of a novel C-terminal truncation retinoic acid receptor mutant which acts as a negative repressor in a promoter- and cell-type-specific manner.Differential recognition of liganded and unliganded thyroid hormone receptor by retinoid X receptor regulates transcriptional repression.DNA bending by thyroid hormone receptor: influence of half-site spacing and RXR.Definition of the surface in the thyroid hormone receptor ligand binding domain for association as homodimers and heterodimers with retinoid X receptor.Retinoid receptors and keratinocytes.Heterodimerization of ecdysone receptor and ultraspiracle on symmetric and asymmetric response elements.The DNA binding domain of hepatocyte nuclear factor 4 mediates cooperative, specific binding to DNA and heterodimerization with the retinoid X receptor alpha.
P2860
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P2860
The conserved ninth C-terminal heptad in thyroid hormone and retinoic acid receptors mediates diverse responses by affecting heterodimer but not homodimer formation.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年学术文章
@wuu
1993年学术文章
@zh-cn
1993年学术文章
@zh-hans
1993年学术文章
@zh-my
1993年学术文章
@zh-sg
1993年學術文章
@yue
1993年學術文章
@zh
1993年學術文章
@zh-hant
name
The conserved ninth C-terminal ...... r but not homodimer formation.
@en
The conserved ninth C-terminal ...... r but not homodimer formation.
@nl
type
label
The conserved ninth C-terminal ...... r but not homodimer formation.
@en
The conserved ninth C-terminal ...... r but not homodimer formation.
@nl
prefLabel
The conserved ninth C-terminal ...... r but not homodimer formation.
@en
The conserved ninth C-terminal ...... r but not homodimer formation.
@nl
P2093
P2860
P356
P1476
The conserved ninth C-terminal ...... r but not homodimer formation.
@en
P2093
H H Samuels
J Casanova
M Au-Fliegner
P2860
P304
P356
10.1128/MCB.13.9.5725
P407
P577
1993-09-01T00:00:00Z