Differential recognition of liganded and unliganded thyroid hormone receptor by retinoid X receptor regulates transcriptional repression.
about
Human SFMBT is a transcriptional repressor protein that selectively binds the N-terminal tail of histone H3Oligomerization of ETO is obligatory for corepressor interactionNuclear receptor corepressors partner with class II histone deacetylases in a Sin3-independent repression pathwayTranscriptional repression by the SMRT-mSin3 corepressor: multiple interactions, multiple mechanisms, and a potential role for TFIIB.Transcriptional silencing is defined by isoform- and heterodimer-specific interactions between nuclear hormone receptors and corepressorsThe CoRNR motif controls the recruitment of corepressors by nuclear hormone receptors.Multiple subnuclear targeting signals of the leukemia-related AML1/ETO and ETO repressor proteins.LMO7 mediates cell-specific activation of the Rho-myocardin-related transcription factor-serum response factor pathway and plays an important role in breast cancer cell migration.TR alpha 2 exerts dominant negative effects on hypothalamic Trh transcription in vivo.Proteasomal regulation of nuclear receptor corepressor-mediated repressionTranscriptional anti-repression. Thyroid hormone receptor beta-2 recruits SMRT corepressor but interferes with subsequent assembly of a functional corepressor complex.Retinoid isomers differ in the ability to induce release of SMRT corepressor from retinoic acid receptor-alphaTransgenic analysis reveals that thyroid hormone receptor is sufficient to mediate the thyroid hormone signal in frog metamorphosisGlucose and thyroid hormone co-regulate the expression of the intestinal fructose transporter GLUT5.A SANT motif in the SMRT corepressor interprets the histone code and promotes histone deacetylation.Vitamin D-dependent recruitment of corepressors to vitamin D/retinoid X receptor heterodimersA novel role for helix 12 of retinoid X receptor in regulating repression.Aberrant recruitment of the nuclear receptor corepressor-histone deacetylase complex by the acute myeloid leukemia fusion partner ETO.Functional evidence for retinoid X receptor (RXR) as a nonsilent partner in the thyroid hormone receptor/RXR heterodimer.A permissive retinoid X receptor/thyroid hormone receptor heterodimer allows stimulation of prolactin gene transcription by thyroid hormone and 9-cis-retinoic acid.Transcriptional repression by thyroid hormone receptors. A role for receptor homodimers in the recruitment of SMRT corepressor.Molecular mechanisms of transcriptional control by Rev-erbα: An energetic foundation for reconciling structure and binding with biological functionSignaling by tyrosine kinases negatively regulates the interaction between transcription factors and SMRT (silencing mediator of retinoic acid and thyroid hormone receptor) corepressor.A role for helix 3 of the TRbeta ligand-binding domain in coactivator recruitment identified by characterization of a third cluster of mutations in resistance to thyroid hormone.Novel roles of retinoid X receptor (RXR) and RXR ligand in dynamically modulating the activity of the thyroid hormone receptor/RXR heterodimer.Retinoid X receptor isoforms a and p differentially regulate 3,5,3′‐triiodothyronine‐induced transcription
P2860
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P2860
Differential recognition of liganded and unliganded thyroid hormone receptor by retinoid X receptor regulates transcriptional repression.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
1997年论文
@zh
1997年论文
@zh-cn
name
Differential recognition of li ...... es transcriptional repression.
@en
type
label
Differential recognition of li ...... es transcriptional repression.
@en
prefLabel
Differential recognition of li ...... es transcriptional repression.
@en
P2093
P2860
P356
P1476
Differential recognition of li ...... es transcriptional repression.
@en
P2093
P2860
P304
P356
10.1128/MCB.17.12.6887
P407
P577
1997-12-01T00:00:00Z