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The human Cdc37.Hsp90 complex studied by heteronuclear NMR spectroscopyA two-hybrid screen of the yeast proteome for Hsp90 interactors uncovers a novel Hsp90 chaperone requirement in the activity of a stress-activated mitogen-activated protein kinase, Slt2p (Mpk1p).Cdc37p 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 maturationA visual review of the interactome of LRRK2: Using deep-curated molecular interaction data to represent biology.The Schizosaccharomyces pombe Cdc7 protein kinase required for septum formation is a client protein of Cdc37.Hsp90 cochaperone Aha1 is a negative regulator of the Saccharomyces MAL activator and acts early in the chaperone activation pathway.Hsp90/Cdc37 chaperone/co-chaperone complex, a novel junction anticancer target elucidated by the mode of action of herbal drug Withaferin ASpecific regulation of noncanonical p38alpha activation by Hsp90-Cdc37 chaperone complex in cardiomyocyte.Split Renilla luciferase protein fragment-assisted complementation (SRL-PFAC) to characterize Hsp90-Cdc37 complex and identify critical residues in protein/protein interactions.Cdc37 engages in stable, S14A mutation-reinforced association with the most atypical member of the yeast kinome, Cdk-activating kinase (Cak1).Cdc37 interacts with the glycine-rich loop of Hsp90 client kinasesMultiple kinases and system robustness: a link between Cdc37 and genome integrity.Multiple implications of 3-phosphoinositide-dependent protein kinase 1 in human cancer.Withaferin A targets heat shock protein 90 in pancreatic cancer cells.5-Azacytidine-induced protein 2 (AZI2) regulates bone mass by fine-tuning osteoclast survivalA dynamic view of ATP-coupled functioning cycle of Hsp90 N-terminal domain.Post-translational modifications of Hsp90 and their contributions to chaperone regulationFunctional specificity of co-chaperone interactions with Hsp90 client proteins.Cdc37/Hsp90 protein complex disruption triggers an autophagic clearance cascade for TDP-43 proteinTumor-intrinsic and tumor-extrinsic factors impacting hsp90- targeted therapy.Novel interaction between the co-chaperone Cdc37 and Rho GTPase exchange factor Vav3 promotes androgen receptor activity and prostate cancer growth.The co-chaperone Cdc37 regulates the rabies virus phosphoprotein stability by targeting to Hsp90AA1 machinery.Silencing the cochaperone CDC37 destabilizes kinase clients and sensitizes cancer cells to HSP90 inhibitorsThe chaperones Hsp90 and Cdc37 mediate the maturation and stabilization of protein kinase C through a conserved PXXP motif in the C-terminal tail.Targeting the oncogene and kinome chaperone CDC37.Characterization of celastrol to inhibit hsp90 and cdc37 interaction.Contributions of co-chaperones and post-translational modifications towards Hsp90 drug sensitivity.Hsp90 regulates autophagy and plays a role in cancer therapy.Restricting direct interaction of CDC37 with HSP90 does not compromise chaperoning of client proteinsThe Saccharomyces cerevisiae Ptc1 protein phosphatase attenuates G2-M cell cycle blockage caused by activation of the cell wall integrity pathway.Pink1 Parkinson mutations, the Cdc37/Hsp90 chaperones and Parkin all influence the maturation or subcellular distribution of Pink1.Signal responsiveness of IkappaB kinases is determined by Cdc37-assisted transient interaction with Hsp90.Cdc28 provides a molecular link between Hsp90, morphogenesis, and cell cycle progression in Candida albicans.CK2 controls multiple protein kinases by phosphorylating a kinase-targeting molecular chaperone, Cdc37.Reactivation of ERK and Akt confers resistance of mutant BRAF colon cancer cells to the HSP90 inhibitor AUY922Cdc37 (cell division cycle 37) restricts Hsp90 (heat shock protein 90) motility by interaction with N-terminal and middle domain binding sites.Investigating the protein-protein interactions of the yeast Hsp90 chaperone system by two-hybrid analysis: potential uses and limitations of this approach.Cdc37 regulates Ryk signaling by stabilizing the cleaved Ryk intracellular domainStructural bioinformatics and protein docking analysis of the molecular chaperone-kinase interactions: towards allosteric inhibition of protein kinases by targeting the hsp90-cdc37 chaperone machinery.
P2860
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P2860
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
2003年论文
@zh
2003年论文
@zh-cn
name
Cdc37 goes beyond Hsp90 and kinases
@ast
Cdc37 goes beyond Hsp90 and kinases
@en
type
label
Cdc37 goes beyond Hsp90 and kinases
@ast
Cdc37 goes beyond Hsp90 and kinases
@en
prefLabel
Cdc37 goes beyond Hsp90 and kinases
@ast
Cdc37 goes beyond Hsp90 and kinases
@en
P2860
P1476
Cdc37 goes beyond Hsp90 and kinases
@en
P2093
Didier Picard
P2860
P304
P356
10.1379/1466-1268(2003)008<0114:CGBHAK>2.0.CO;2
P577
2003-01-01T00:00:00Z