The Hsp90 co-chaperones Cdc37 and Sti1 interact physically and genetically.
about
Combined analysis of genome-wide association studies for Crohn disease and psoriasis identifies seven shared susceptibility lociHsp90 cochaperone Aha1 is a negative regulator of the Saccharomyces MAL activator and acts early in the chaperone activation pathway.Effect of mutation of the tetratricopeptide repeat and asparatate-proline 2 domains of Sti1 on Hsp90 signaling and interaction in Saccharomyces cerevisiaeMultiple kinases and system robustness: a link between Cdc37 and genome integrity.Post-translational modifications of Hsp90 and their contributions to chaperone regulationCdc37 goes beyond Hsp90 and kinasesFunctional specificity of co-chaperone interactions with Hsp90 client proteins.HSP90 interacts with RAR1 and SGT1 and is essential for RPS2-mediated disease resistance in Arabidopsis.Hyperactivity and attention deficits in mice with decreased levels of stress-inducible phosphoprotein 1 (STIP1).Functioning of the Hsp90 machine in chaperoning checkpoint kinase I (Chk1) and the progesterone receptor (PR).The Cdc37 protein kinase-binding domain is sufficient for protein kinase activity and cell viability.Tumor-intrinsic and tumor-extrinsic factors impacting hsp90- targeted therapy.Novel interaction of the Hsp90 chaperone machine with Ssl2, an essential DNA helicase in Saccharomyces cerevisiae.Contributions of co-chaperones and post-translational modifications towards Hsp90 drug sensitivity.Sequence and domain conservation of the coelacanth Hsp40 and Hsp90 chaperones suggests conservation of function.Aha1 competes with Hop, p50 and p23 for binding to the molecular chaperone Hsp90 and contributes to kinase and hormone receptor activation.Sti1 and Cdc37 can stabilize Hsp90 in chaperone complexes with a protein kinase.Cdc37-Hsp90 complexes are responsive to nucleotide-induced conformational changes and binding of further cofactors.Functional coevolutionary networks of the Hsp70-Hop-Hsp90 system revealed through computational analyses
P2860
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P2860
The Hsp90 co-chaperones Cdc37 and Sti1 interact physically and genetically.
description
2002 nî lūn-bûn
@nan
2002 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
The Hsp90 co-chaperones Cdc37 and Sti1 interact physically and genetically.
@ast
The Hsp90 co-chaperones Cdc37 and Sti1 interact physically and genetically.
@en
The Hsp90 co-chaperones Cdc37 and Sti1 interact physically and genetically.
@nl
type
label
The Hsp90 co-chaperones Cdc37 and Sti1 interact physically and genetically.
@ast
The Hsp90 co-chaperones Cdc37 and Sti1 interact physically and genetically.
@en
The Hsp90 co-chaperones Cdc37 and Sti1 interact physically and genetically.
@nl
prefLabel
The Hsp90 co-chaperones Cdc37 and Sti1 interact physically and genetically.
@ast
The Hsp90 co-chaperones Cdc37 and Sti1 interact physically and genetically.
@en
The Hsp90 co-chaperones Cdc37 and Sti1 interact physically and genetically.
@nl
P2093
P2860
P356
P1433
P1476
The Hsp90 co-chaperones Cdc37 and Sti1 interact physically and genetically.
@en
P2093
Didier Picard
Olivier Donzé
Pierre-André Briand
Toufik Abbas-Terki
P2860
P304
P356
10.1515/BC.2002.152
P577
2002-09-01T00:00:00Z