The N-terminal regions of estrogen receptor alpha and beta are unstructured in vitro and show different TBP binding properties
about
Estrogen and Estrogen Receptor-α-Mediated Transrepression of Bile Salt Export PumpSPBP is a phosphoserine-specific repressor of estrogen receptor alpha.Structure and function of steroid receptor AF1 transactivation domains: induction of active conformationsA progesterone receptor co-activator (JDP2) mediates activity through interaction with residues in the carboxyl-terminal extension of the DNA binding domainTamoxifen represses alcohol-induced transcription of RNA polymerase III-dependent genes in breast cancer cellsRegulation of estrogen receptor α N-terminus conformation and function by peptidyl prolyl isomerase Pin1Physical and functional interaction of Acyl-CoA-binding protein with hepatocyte nuclear factor-4 alphaPartial agonist activity of the progesterone receptor antagonist RU486 mediated by an amino-terminal domain coactivator and phosphorylation of serine400An overview of the importance of conformational flexibility in gene regulation by the transcription factors.Modulation of human estrogen receptor α activity by multivalent estradiol-peptidomimetic conjugates.Aryl hydrocarbon receptor-mediated transcription: ligand-dependent recruitment of estrogen receptor alpha to 2,3,7,8-tetrachlorodibenzo-p-dioxin-responsive promoters.TBP binding-induced folding of the glucocorticoid receptor AF1 domain facilitates its interaction with steroid receptor coactivator-1Regulation of the amino-terminal transcription activation domain of progesterone receptor by a cofactor-induced protein folding mechanism.Chromatin exposes intrinsic differences in the transcriptional activities of estrogen receptors alpha and beta.Transcriptional coactivator PC4 stimulates promoter escape and facilitates transcriptional synergy by GAL4-VP16Influence of domain interactions on conformational mobility of the progesterone receptor detected by hydrogen/deuterium exchange mass spectrometry.Structural and functional analysis of domains of the progesterone receptor.Peptidylprolyl Isomerase Pin1 Directly Enhances the DNA Binding Functions of Estrogen Receptor α.Transcription in four dimensions: nuclear receptor-directed initiation of gene expressionERα mediates alcohol-induced deregulation of Pol III genes in breast cancer cells.Allosteric modulators of steroid hormone receptors: structural dynamics and gene regulation.Natural disordered sequences in the amino terminal domain of nuclear receptors: lessons from the androgen and glucocorticoid receptors.Solution Behavior of the Intrinsically Disordered N-Terminal Domain of Retinoid X Receptor α in the Context of the Full-Length Protein.Regulation of the structurally dynamic N-terminal domain of progesterone receptor by protein-induced folding.Intrinsic disorder in nuclear hormone receptors.HACE1: A novel repressor of RAR transcriptional activity.Proteomics reveals a physical and functional link between hepatocyte nuclear factor 4alpha and transcription factor IID.Minireview: dynamic structures of nuclear hormone receptors: new promises and challenges.Structural and functional relationships of the steroid hormone receptors' N-terminal transactivation domainSupport of a bi-faceted role of estrogen receptor β (ERβ) in ERα-positive breast cancer cellsTATA box binding protein induces structure in the recombinant glucocorticoid receptor AF1 domain.Molecular Mechanisms and Genome-Wide Aspects of PPAR Subtype Specific Transactivation.Estrogen receptors (ERα versus ERβ): friends or foes in human biology?The dynamic structure of the estrogen receptorSmall-molecule hormones: molecular mechanisms of actionWhat are comparative studies telling us about the mechanism of ERbeta action in the ERE-dependent E2 signaling pathway?Conformation of the mineralocorticoid receptor N-terminal domain: evidence for induced and stable structure.Effects of different osmolytes on the induced folding of the N-terminal activation domain (AF1) of the glucocorticoid receptor.Conformational analysis of the androgen receptor amino-terminal domain involved in transactivation. Influence of structure-stabilizing solutes and protein-protein interactions.A novel serine phosphorylation site detected in the N-terminal domain of estrogen receptor isolated from human breast cancer cells.
P2860
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P2860
The N-terminal regions of estrogen receptor alpha and beta are unstructured in vitro and show different TBP binding properties
description
2001 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 2001
@ast
im Dezember 2001 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
wetenschappelijk artikel (gepubliceerd op 2001/12/07)
@nl
наукова стаття, опублікована в грудні 2001
@uk
مقالة علمية (نشرت في 7-12-2001)
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name
The N-terminal regions of estr ...... fferent TBP binding properties
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The N-terminal regions of estr ...... fferent TBP binding properties
@en
type
label
The N-terminal regions of estr ...... fferent TBP binding properties
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The N-terminal regions of estr ...... fferent TBP binding properties
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prefLabel
The N-terminal regions of estr ...... fferent TBP binding properties
@ast
The N-terminal regions of estr ...... fferent TBP binding properties
@en
P2093
P2860
P356
P1476
The N-terminal regions of estr ...... fferent TBP binding properties
@en
P2093
A. P. Wright
A. Wikström
A. Wärnmark
J. A. Gustafsson
P2860
P304
45939–45944
P356
10.1074/JBC.M107875200
P407
P50
P577
2001-12-07T00:00:00Z