Cdc37 interacts with the glycine-rich loop of Hsp90 client kinases
about
Functions of the Hsp90 chaperone system: lifting client proteins to new heightsNovel Hsp90 partners discovered using complementary proteomic approaches.Specific regulation of noncanonical p38alpha activation by Hsp90-Cdc37 chaperone complex in cardiomyocyte.ATP-competitive inhibitors block protein kinase recruitment to the Hsp90-Cdc37 system.Identification of a DYRK1A Inhibitor that Induces Degradation of the Target Kinase using Co-chaperone CDC37 fused with Luciferase nanoKAZ.Regulation of Greatwall kinase by protein stabilization and nuclear localizationOral administration of an HSP90 inhibitor, 17-DMAG, intervenes tumor-cell infiltration into multiple organs and improves survival period for ATL model micePhospho-proteomic analyses of B-Raf protein complexes reveal new regulatory principles.EWS represses cofilin 1 expression by inducing nuclear retention of cofilin 1 mRNA.Signal responsiveness of IkappaB kinases is determined by Cdc37-assisted transient interaction with Hsp90.Cdc37-Hsp90 complexes are responsive to nucleotide-induced conformational changes and binding of further cofactors.Cdc37 regulates Ryk signaling by stabilizing the cleaved Ryk intracellular domainHsp90·Cdc37 Complexes with Protein Kinases Form Cooperatively with Multiple Distinct Interaction Sites.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.The Hsp90 inhibitor geldanamycin abrogates colocalization of eIF4E and eIF4E-transporter into stress granules and association of eIF4E with eIF4G.Arabidopsis TRIGALACTOSYLDIACYLGLYCEROL5 Interacts with TGD1, TGD2, and TGD4 to Facilitate Lipid Transfer from the Endoplasmic Reticulum to Plastids.Targeting the Hsp90-Cdc37-client protein interaction to disrupt Hsp90 chaperone machinery.
P2860
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P2860
Cdc37 interacts with the glycine-rich loop of Hsp90 client kinases
description
2006 nî lūn-bûn
@nan
2006 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Cdc37 interacts with the glycine-rich loop of Hsp90 client kinases
@ast
Cdc37 interacts with the glycine-rich loop of Hsp90 client kinases
@en
Cdc37 interacts with the glycine-rich loop of Hsp90 client kinases
@nl
type
label
Cdc37 interacts with the glycine-rich loop of Hsp90 client kinases
@ast
Cdc37 interacts with the glycine-rich loop of Hsp90 client kinases
@en
Cdc37 interacts with the glycine-rich loop of Hsp90 client kinases
@nl
prefLabel
Cdc37 interacts with the glycine-rich loop of Hsp90 client kinases
@ast
Cdc37 interacts with the glycine-rich loop of Hsp90 client kinases
@en
Cdc37 interacts with the glycine-rich loop of Hsp90 client kinases
@nl
P2093
P2860
P1476
Cdc37 interacts with the glycine-rich loop of Hsp90 client kinases
@en
P2093
Katsuhiko Yoshimatsu
Kazuya Terasawa
Keiji Tanaka
Shun-Ichiro Iemura
Yasufumi Minami
P2860
P304
P356
10.1128/MCB.26.9.3378-3389.2006
P407
P577
2006-05-01T00:00:00Z