Trimethylamine N-oxide-induced cooperative folding of an intrinsically unfolded transcription-activating fragment of human glucocorticoid receptor.
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Structure and function of steroid receptor AF1 transactivation domains: induction of active conformationsOsmolytes stabilize ribonuclease S by stabilizing its fragments S protein and S peptide to compact folding-competent statesAn androgen receptor NH2-terminal conserved motif interacts with the COOH terminus of the Hsp70-interacting protein (CHIP)Solvent-induced collapse of alpha-synuclein and acid-denatured cytochrome cNatively unfolded proteins: a point where biology waits for physicsConditionally disordered proteins: bringing the environment back into the fold.Counteracting chemical chaperone effects on the single-molecule α-synuclein structural landscape.Microscopic stability of cold shock protein A examined by NMR native state hydrogen exchange as a function of urea and trimethylamine N-oxideSite-specific phosphorylation induces functionally active conformation in the intrinsically disordered N-terminal activation function (AF1) domain of the glucocorticoid receptor.An 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.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.FlgM gains structure in living cells.Diversity in genetic in vivo methods for protein-protein interaction studies: from the yeast two-hybrid system to the mammalian split-luciferase system.The osmolyte TMAO stabilizes native RNA tertiary structures in the absence of Mg2+: evidence for a large barrier to folding from phosphate dehydration.Chemical chaperones: a pharmacological strategy for disorders of protein folding and trafficking.Structural dynamics, intrinsic disorder, and allostery in nuclear receptors as transcription factors.Pharmacologic rescue of conformationally-defective proteins: implications for the treatment of human disease.Thermodynamic dissection of the intrinsically disordered N-terminal domain of human glucocorticoid receptor.Restored mutant receptor:Corticoid binding in chaperone complexes by trimethylamine N-oxideBinding of the N-terminal region of coactivator TIF2 to the intrinsically disordered AF1 domain of the glucocorticoid receptor is accompanied by conformational reorganizationsGlucocorticoid receptor-promoter interactions: energetic dissection suggests a framework for the specificity of steroid receptor-mediated gene regulation.Soluble mimics of a chemokine receptor: chemokine binding by receptor elements juxtaposed on a soluble scaffoldAllosteric 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.Potential for therapeutic manipulation of the UPR in disease.Large-scale analysis of thermostable, mammalian proteins provides insights into the intrinsically disordered proteomeStructural 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.Folding propensity of intrinsically disordered proteins by osmotic stress.The Proline/Glycine-Rich Region of the Biofilm Adhesion Protein Aap Forms an Extended Stalk that Resists Compaction.Thermal unfolding of the N-terminal region of p53 monitored by circular dichroism spectroscopy.Crystallization of a functionally intact Hsc70 chaperone.DNA-induced unfolding of the thyroid hormone receptor α A/B domain through allostery.Effects of different osmolytes on the induced folding of the N-terminal activation domain (AF1) of the glucocorticoid receptor.Hydrogen bonding progressively strengthens upon transfer of the protein urea-denatured state to water and protecting osmolytes.Natural osmolyte trimethylamine N-oxide corrects assembly defects of mutant branched-chain alpha-ketoacid decarboxylase in maple syrup urine disease.Osmolytes as modulators of conformational changes in serpins.
P2860
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P2860
Trimethylamine N-oxide-induced cooperative folding of an intrinsically unfolded transcription-activating fragment of human glucocorticoid receptor.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
1999年學術文章
@zh-hant
name
Trimethylamine N-oxide-induced ...... human glucocorticoid receptor.
@en
Trimethylamine N-oxide-induced ...... human glucocorticoid receptor.
@nl
type
label
Trimethylamine N-oxide-induced ...... human glucocorticoid receptor.
@en
Trimethylamine N-oxide-induced ...... human glucocorticoid receptor.
@nl
prefLabel
Trimethylamine N-oxide-induced ...... human glucocorticoid receptor.
@en
Trimethylamine N-oxide-induced ...... human glucocorticoid receptor.
@nl
P2093
P2860
P356
P1476
Trimethylamine N-oxide-induced ...... human glucocorticoid receptor.
@en
P2093
P2860
P304
10693-10696
P356
10.1074/JBC.274.16.10693
P407
P577
1999-04-01T00:00:00Z