The Cdc37 protein kinase-binding domain is sufficient for protein kinase activity and cell viability.
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Quality control and fate determination of Hsp90 client proteinsThe human Cdc37.Hsp90 complex studied by heteronuclear NMR spectroscopyCdc37p is required for stress-induced high-osmolarity glycerol and protein kinase C mitogen-activated protein kinase pathway functionality by interaction with Hog1p and Slt2p (Mpk1p)Cdc37 has distinct roles in protein kinase quality control that protect nascent chains from degradation and promote posttranslational maturationThe Schizosaccharomyces pombe Cdc7 protein kinase required for septum formation is a client protein of Cdc37.An Hsp90 co-chaperone protein in yeast is functionally replaced by site-specific posttranslational modification in humansSpecific regulation of noncanonical p38alpha activation by Hsp90-Cdc37 chaperone complex in cardiomyocyte.Structure of an Hsp90-Cdc37-Cdk4 complex.Cdc37 interacts with the glycine-rich loop of Hsp90 client kinasesMultiple kinases and system robustness: a link between Cdc37 and genome integrity.Cdc37 goes beyond Hsp90 and kinasesThe response to heat shock and oxidative stress in Saccharomyces cerevisiaeMultiple 40-kDa heat-shock protein chaperones function in Tom70-dependent mitochondrial import.Biology of the heat shock response and protein chaperones: budding yeast (Saccharomyces cerevisiae) as a model system.Functional specificity of co-chaperone interactions with Hsp90 client proteins.Novel interaction between the co-chaperone Cdc37 and Rho GTPase exchange factor Vav3 promotes androgen receptor activity and prostate cancer growth.Hsp90/Hsp70 chaperone machine regulation of the Saccharomyces MAL-activator as determined in vivo using noninducible and constitutive mutant allelesPhosphorylated and unphosphorylated serine 13 of CDC37 stabilize distinct interactions between its client and HSP90 binding domains.Hsp90-dependent activation of protein kinases is regulated by chaperone-targeted dephosphorylation of Cdc37.Silencing the cochaperone CDC37 destabilizes kinase clients and sensitizes cancer cells to HSP90 inhibitorsConformational dynamics of the molecular chaperone Hsp90Restricting direct interaction of CDC37 with HSP90 does not compromise chaperoning of client proteinsYdj1 protects nascent protein kinases from degradation and controls the rate of their maturation.Identification of Cdc37 as a novel regulator of the stress-responsive mitogen-activated protein kinaseIdentification of a conserved sequence motif that promotes Cdc37 and cyclin D1 binding to Cdk4.Sti1 and Cdc37 can stabilize Hsp90 in chaperone complexes with a protein kinase.CK2 controls multiple protein kinases by phosphorylating a kinase-targeting molecular chaperone, Cdc37.Molecular Mechanism of Protein Kinase Recognition and Sorting by the Hsp90 Kinome-Specific Cochaperone Cdc37.Investigating the protein-protein interactions of the yeast Hsp90 chaperone system by two-hybrid analysis: potential uses and limitations of this approach.Alteration of the protein kinase binding domain enhances function of the Saccharomyces cerevisiae molecular chaperone Cdc37.Structural bioinformatics and protein docking analysis of the molecular chaperone-kinase interactions: towards allosteric inhibition of protein kinases by targeting the hsp90-cdc37 chaperone machinery.Evidence for Hsp90 Co-chaperones in Regulating Hsp90 Function and Promoting Client Protein Folding.Candida albicans Cdc37 interacts with the Crk1 kinase and is required for Crk1 production.
P2860
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P2860
The Cdc37 protein kinase-binding domain is sufficient for protein kinase activity and cell viability.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年学术文章
@wuu
2002年学术文章
@zh-cn
2002年学术文章
@zh-hans
2002年学术文章
@zh-my
2002年学术文章
@zh-sg
2002年學術文章
@yue
2002年學術文章
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2002年學術文章
@zh-hant
name
The Cdc37 protein kinase-bindi ...... e activity and cell viability.
@ast
The Cdc37 protein kinase-bindi ...... e activity and cell viability.
@en
type
label
The Cdc37 protein kinase-bindi ...... e activity and cell viability.
@ast
The Cdc37 protein kinase-bindi ...... e activity and cell viability.
@en
prefLabel
The Cdc37 protein kinase-bindi ...... e activity and cell viability.
@ast
The Cdc37 protein kinase-bindi ...... e activity and cell viability.
@en
P2093
P2860
P356
P1476
The Cdc37 protein kinase-bindi ...... e activity and cell viability.
@en
P2093
Albert Fliss
Avrom J Caplan
Stephen Garrett
P2860
P304
P356
10.1083/JCB.200210121
P407
P577
2002-12-23T00:00:00Z