Transactivation functions of the N-terminal domains of nuclear hormone receptors: protein folding and coactivator interactions.
about
The structural basis of androgen receptor activation: intramolecular and intermolecular amino-carboxy interactionsThe cell-specific activity of the estrogen receptor alpha may be fine-tuned by phosphorylation-induced structural gymnastics.Steroid hormone receptors and prostate cancer: role of structural dynamics in therapeutic targetingStructural Basis for Agonism and Antagonism for a Set of Chemically Related Progesterone Receptor ModulatorsA progesterone receptor co-activator (JDP2) mediates activity through interaction with residues in the carboxyl-terminal extension of the DNA binding domainPartial 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.Naturally occurring osmolyte, trehalose induces functional conformation in an intrinsically disordered activation domain of glucocorticoid receptor.TBP binding-induced folding of the glucocorticoid receptor AF1 domain facilitates its interaction with steroid receptor coactivator-1Constitutive activation of the mitogen-activated protein kinase pathway impairs vitamin D signaling in human prostate epithelial cells.Binding-folding induced regulation of AF1 transactivation domain of the glucocorticoid receptor by a cofactor that binds to its DNA binding domain.Regulation of the amino-terminal transcription activation domain of progesterone receptor by a cofactor-induced protein folding mechanism.Dynamic access of the glucocorticoid receptor to response elements in chromatin.Ligand binding domain mutations of the glucocorticoid receptor selectively modify the effects with, but not binding of, cofactors.The road less traveled: new views of steroid receptor action from the path of dose-response curves.Structural dynamics, intrinsic disorder, and allostery in nuclear receptors as transcription factors.Estrogen-related Receptor β Reduces the Subnuclear Mobility of Estrogen Receptor α and Suppresses Estrogen-dependent Cellular Function.Structural and functional analysis of domains of the progesterone receptor.Thermodynamic analysis of progesterone receptor-promoter interactions reveals a molecular model for isoform-specific function.Multiple novel signals mediate thyroid hormone receptor nuclear import and exportEcdysone receptor directly binds the promoter of the Drosophila caspase dronc, regulating its expression in specific tissues.Transactivating function (AF) 2-mediated AF-1 activity of estrogen receptor α is crucial to maintain male reproductive tract function.Binding of the N-terminal region of coactivator TIF2 to the intrinsically disordered AF1 domain of the glucocorticoid receptor is accompanied by conformational reorganizationsThermodynamic dissection of estrogen receptor-promoter interactions reveals that steroid receptors differentially partition their self-association and promoter binding energetics.MicroRNAs and Glucocorticoid-Induced Apoptosis in Lymphoid MalignanciesDual-site interactions of p53 protein transactivation domain with anti-apoptotic Bcl-2 family proteins reveal a highly convergent mechanism of divergent p53 pathways.Allosteric modulators of steroid hormone receptors: structural dynamics and gene regulation.Germ Cell Nuclear Factor (GCNF) Represses Oct4 Expression and Globally Modulates Gene Expression in Human Embryonic Stem (hES) Cells.Estrogen receptor-α and estrogen receptor-β in the uterine vascular endothelium during pregnancy: functional implications for regulating uterine blood flow.An androgen receptor N-terminal domain antagonist for treating prostate cancer.Determinants of the heightened activity of glucocorticoid receptor translational isoforms.Variable steroid receptor responses: Intrinsically disordered AF1 is the key.Regulation of the structurally dynamic N-terminal domain of progesterone receptor by protein-induced folding.HACE1: A novel repressor of RAR transcriptional activity.Posttranslational modifications of PPAR-gamma: fine-tuning the metabolic master regulator.Structural and functional relationships of the steroid hormone receptors' N-terminal transactivation domainDifferential regulation of the transcriptional activity of the glucocorticoid receptor through site-specific phosphorylation.TATA box binding protein induces structure in the recombinant glucocorticoid receptor AF1 domain.Rational structure-based drug design and optimization in the ligand-binding domain of the glucocorticoid receptor-α.Rational ligand-based virtual screening and structure-activity relationship studies in the ligand-binding domain of the glucocorticoid receptor-α.
P2860
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P2860
Transactivation functions of the N-terminal domains of nuclear hormone receptors: protein folding and coactivator interactions.
description
2003 nî lūn-bûn
@nan
2003 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年学术文章
@wuu
2003年学术文章
@zh-cn
2003年学术文章
@zh-hans
2003年学术文章
@zh-my
2003年学术文章
@zh-sg
2003年學術文章
@yue
name
Transactivation functions of t ...... and coactivator interactions.
@ast
Transactivation functions of t ...... and coactivator interactions.
@en
type
label
Transactivation functions of t ...... and coactivator interactions.
@ast
Transactivation functions of t ...... and coactivator interactions.
@en
prefLabel
Transactivation functions of t ...... and coactivator interactions.
@ast
Transactivation functions of t ...... and coactivator interactions.
@en
P356
P1476
Transactivation functions of t ...... and coactivator interactions.
@en
P2093
E Brad Thompson
P356
10.1210/ME.2002-0258
P577
2003-01-01T00:00:00Z