Folding of the glucocorticoid receptor by the heat shock protein (hsp) 90-based chaperone machinery. The role of p23 is to stabilize receptor.hsp90 heterocomplexes formed by hsp90.p60.hsp70.
about
A tissue-specific coactivator of steroid receptors, identified in a functional genetic screenHsp90 cochaperones p23 and FKBP4 physically interact with hAgo2 and activate RNA interference-mediated silencing in mammalian cellsChaperoning checkpoint kinase 1 (Chk1), an Hsp90 client, with purified chaperonesGlucocorticoid receptor function regulated by coordinated action of the Hsp90 and Hsp70 chaperone cyclesHuman butyrate-induced transcript 1 interacts with hepatitis C virus NS5A and regulates viral replicationCofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone systemCooperation of heat shock protein 90 and p23 in aryl hydrocarbon receptor signalingGenetic and biochemical analysis of p23 and ansamycin antibiotics in the function of Hsp90-dependent signaling proteinsThe hsp90 chaperone complex regulates intracellular localization of the dioxin receptorRole for Hsp90-associated cochaperone p23 in estrogen receptor signal transductionReview: The HSP90 molecular chaperone-an enigmatic ATPaseGlucocorticoids and endothelial cell barrier functionSBA1 encodes a yeast hsp90 cochaperone that is homologous to vertebrate p23 proteinsContribution of N- and C-terminal domains to the function of Hsp90 in Saccharomyces cerevisiae.A truncated form of p23 down-regulates telomerase activity via disruption of Hsp90 functionFunctional requirement of p23 and Hsp90 in telomerase complexesThe immunophilin-like protein XAP2 regulates ubiquitination and subcellular localization of the dioxin receptorEvidence that the co-chaperone p23 regulates ligand responsiveness of the dioxin (Aryl hydrocarbon) receptorThe molecular chaperones Hsp90 and Hsc70 are both necessary and sufficient to activate hormone binding by glucocorticoid receptorThe Hsp organizer protein hop enhances the rate of but is not essential for glucocorticoid receptor folding by the multiprotein Hsp90-based chaperone systemNucleotide binding states of hsp70 and hsp90 during sequential steps in the process of glucocorticoid receptor.hsp90 heterocomplex assemblyMultiple molecular chaperones interact with apolipoprotein B during its maturation. The network of endoplasmic reticulum-resident chaperones (ERp72, GRP94, calreticulin, and BiP) interacts with apolipoprotein b regardless of its lipidation stateProteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasisHistone deacetylase 6 gates the synaptic action of acute stress in prefrontal cortexcPGES/p23 is required for glucocorticoid receptor function and embryonic growth but not prostaglandin E2 synthesisIdentification and characterization of Harc, a novel Hsp90-associating relative of Cdc37A review of multi-domain and flexible molecular chaperones studies by small-angle X-ray scattering.Genome-wide expression analysis reveals diverse effects of acute nicotine exposure on neuronal function-related genes and pathways.FK506 and the role of the immunophilin FKBP-52 in nerve regeneration.Unsupervised proteome analysis of human leukaemia cells identifies the Valosin-containing protein as a putative marker for glucocorticoid resistance.Nestin modulates glucocorticoid receptor function by cytoplasmic anchoring.Balanced nuclear and cytoplasmic activities of EDS1 are required for a complete plant innate immune responseThe helix 1-3 loop in the glucocorticoid receptor LBD is a regulatory element for FKBP cochaperones.Celastrol inhibits Hsp90 chaperoning of steroid receptors by inducing fibrillization of the Co-chaperone p23Hsp90 binds and regulates Gcn2, the ligand-inducible kinase of the alpha subunit of eukaryotic translation initiation factor 2 [corrected]Influenza virus infection induces the nuclear relocalization of the Hsp90 co-chaperone p23 and inhibits the glucocorticoid receptor response.Characterization of inhibitors of glucocorticoid receptor nuclear translocation: a model of cytoplasmic dynein-mediated cargo transport.Genomic and non-genomic actions of glucocorticoids in asthmaMaturation of steroid receptors: an example of functional cooperation among molecular chaperones and their associated proteinsThe Hsp90 co-chaperones Cdc37 and Sti1 interact physically and genetically.
P2860
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P2860
Folding of the glucocorticoid receptor by the heat shock protein (hsp) 90-based chaperone machinery. The role of p23 is to stabilize receptor.hsp90 heterocomplexes formed by hsp90.p60.hsp70.
description
1997 nî lūn-bûn
@nan
1997 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
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
name
Folding of the glucocorticoid ...... xes formed by hsp90.p60.hsp70.
@ast
Folding of the glucocorticoid ...... xes formed by hsp90.p60.hsp70.
@en
Folding of the glucocorticoid receptor by the heat shock protein
@nl
type
label
Folding of the glucocorticoid ...... xes formed by hsp90.p60.hsp70.
@ast
Folding of the glucocorticoid ...... xes formed by hsp90.p60.hsp70.
@en
Folding of the glucocorticoid receptor by the heat shock protein
@nl
prefLabel
Folding of the glucocorticoid ...... xes formed by hsp90.p60.hsp70.
@ast
Folding of the glucocorticoid ...... xes formed by hsp90.p60.hsp70.
@en
Folding of the glucocorticoid receptor by the heat shock protein
@nl
P2093
P2860
P356
P1476
Folding of the glucocorticoid ...... xes formed by hsp90.p60.hsp70.
@en
P2093
P2860
P304
21213-21220
P356
10.1074/JBC.272.34.21213
P407
P577
1997-08-01T00:00:00Z