A pathway of multi-chaperone interactions common to diverse regulatory proteins: estrogen receptor, Fes tyrosine kinase, heat shock transcription factor Hsf1, and the aryl hydrocarbon receptor
about
In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysisAha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperoneSpecific binding of tetratricopeptide repeat proteins to the C-terminal 12-kDa domain of hsp90Identification of a potential tumor differentiation factor receptor candidate in prostate cancer cellsInteraction of the Hsp90 cochaperone cyclophilin 40 with Hsc70Cooperation of heat shock protein 90 and p23 in aryl hydrocarbon receptor signalingPerturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasomeThe identification of Wos2, a p23 homologue that interacts with Wee1 and Cdc2 in the mitotic control of fission yeastsThe hsp90 chaperone complex regulates intracellular localization of the dioxin receptorRole for Hsp90-associated cochaperone p23 in estrogen receptor signal transductionMolecular chaperones as HSF1-specific transcriptional repressorsChemical communication threatened by endocrine-disrupting chemicalsCrystallographic structure of the tetratricopeptide repeat domain ofPlasmodium falciparumFKBP35 and its molecular interaction with Hsp90 C-terminal pentapeptideRequirement for Hsp90 and a CyP-40-type cyclophilin in negative regulation of the heat shock response.SBA1 encodes a yeast hsp90 cochaperone that is homologous to vertebrate p23 proteinsCns1 is an essential protein associated with the hsp90 chaperone complex in Saccharomyces cerevisiae that can restore cyclophilin 40-dependent functions in cpr7Delta cellsIdentification of SSF1, CNS1, and HCH1 as multicopy suppressors of a Saccharomyces cerevisiae Hsp90 loss-of-function mutation.A truncated form of p23 down-regulates telomerase activity via disruption of Hsp90 functionThe 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 heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATP-binding domain in the carboxyl terminus of the chaperoneStructure and expression of the Ah receptor repressor geneTwo parallel pathways mediate cytoplasmic localization of the dioxin (aryl hydrocarbon) receptorTwo distinct regions of the immunophilin-like protein XAP2 regulate dioxin receptor function and interaction with hsp90Hop modulates Hsp70/Hsp90 interactions in protein foldingAh Receptor Pathway Intricacies; Signaling Through Diverse Protein Partners and DNA-MotifsThe aryl hydrocarbon receptor complex and the control of gene expressionThe physical association of multiple molecular chaperone proteins with mutant p53 is altered by geldanamycin, an hsp90-binding agentIdentification and characterization of Harc, a novel Hsp90-associating relative of Cdc37Essential role for Co-chaperone Fkbp52 but not Fkbp51 in androgen receptor-mediated signaling and physiologyFunctional interaction of human Cdc37 with the androgen receptor but not with the glucocorticoid receptor.Phase I study of 17-allylamino-17 demethoxygeldanamycin, gemcitabine and/or cisplatin in patients with refractory solid tumorsOn mechanisms that control heat shock transcription factor activity in metazoan cells.HSP90 interacts with and regulates the activity of heat shock factor 1 in Xenopus oocytes.Multiple components of the HSP90 chaperone complex function in regulation of heat shock factor 1 In vivoHsp90 binds and regulates Gcn2, the ligand-inducible kinase of the alpha subunit of eukaryotic translation initiation factor 2 [corrected]Chaperones in cell cycle regulation and mitogenic signal transduction: a review.Steroid resistance in the squirrel monkey: an old subject revisited.The heat shock protein-90 co-chaperone, Cyclophilin 40, promotes ALK-positive, anaplastic large cell lymphoma viability and its expression is regulated by the NPM-ALK oncoprotein.Characterization of tumor differentiation factor (TDF) and its receptor (TDF-R).
P2860
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P2860
A pathway of multi-chaperone interactions common to diverse regulatory proteins: estrogen receptor, Fes tyrosine kinase, heat shock transcription factor Hsf1, and the aryl hydrocarbon receptor
description
1996 nî lūn-bûn
@nan
1996 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
A pathway of multi-chaperone i ...... the aryl hydrocarbon receptor
@ast
A pathway of multi-chaperone i ...... the aryl hydrocarbon receptor
@en
A pathway of multi-chaperone i ...... the aryl hydrocarbon receptor
@nl
type
label
A pathway of multi-chaperone i ...... the aryl hydrocarbon receptor
@ast
A pathway of multi-chaperone i ...... the aryl hydrocarbon receptor
@en
A pathway of multi-chaperone i ...... the aryl hydrocarbon receptor
@nl
prefLabel
A pathway of multi-chaperone i ...... the aryl hydrocarbon receptor
@ast
A pathway of multi-chaperone i ...... the aryl hydrocarbon receptor
@en
A pathway of multi-chaperone i ...... the aryl hydrocarbon receptor
@nl
P2093
P1476
A pathway of multi-chaperone i ...... the aryl hydrocarbon receptor
@en
P2093
R A Rimerman
S Hjermstad
T E Smithgall
P304
P356
10.1379/1466-1268(1996)001<0237:APOMCI>2.3.CO;2
P407
P577
1996-12-01T00:00:00Z