1. Girstmair, H., et al., The Hsp90 isoforms from S. cerevisiae differ in structure, function and client range. Nat Commun, 2019. 10(1): p. 3626.2. Verba, K.A., et al., Atomic structure of Hsp90-Cdc37-Cdk4 reveals that Hsp90 traps and stabilizes an unfolded kinase. Science,...
1. Girstmair, H., et al., The Hsp90 isoforms from S. cerevisiae differ in structure, function and client range.Nat Commun, 2019. 10(1): p. 3626. 2. Verba, K.A., et al., Atomic structure of Hsp90-Cdc37-Cdk4 reveals that ...
其中一种化合物是小分子抑制剂DDO-5936[80]。DDO-5936与HSP90的Glu47残基结合,并用Cdc37干扰PPI,随后抑制CRC细胞系中HSP90的激酶客户蛋白。CRC细胞的增殖被抑制是由于随后的周期蛋白依赖性激酶4 (Cdk4)的降解。HSP90抑制剂的另一个限制是它们通过atp结合盒(ABC)转运体输出,使癌细胞对这些抑制剂[13]产生抗性。...
Kinase Regulation Through Dramatic Unfolding, as Told by Hsp90:Cdc37:Cdk4 Atomic Cryoem StructureHsp90 is a ubiquitous ATP-dependent molecular chaperone that accounts for 1–2‥ of the cytosolic proteins and is essential for viability in eukaryotes. It interacts with as much as 10‥ of ...
et al. Regulation of Hsp90 ATPase activity by the co-chaperone Cdc37p/p50cdc37. J. Biol. Chem. 277, 20151–20159 (2002). Article CAS PubMed Google Scholar Verba, K. A. et al. Atomic structure of Hsp90-Cdc37-Cdk4 reveals that Hsp90 traps and stabilizes an unfolded kinase. ...
Furthermore, expression of the mutants was sufficient to protect kinase clients CDK4, CDK6, CRAF and ERBB2 from depletion induced by silencing endogenous CDC37, indicating that CDC37's client stabilising function cannot be inactivated by substantially reducing its direct interaction with HSP90. ...
该基因编码的蛋白质与酿酒酵母的细胞分裂周期控制蛋白质Cdc 37非常相似。 该蛋白是在细胞信号转导中具有特定功能的分子伴侣。 它已经显示与Hsp90和多种蛋白激酶(包括CDK4,CDK6,SRC,RAF-1,MOK以及eIF2α激酶)形成复合物。 据认为在将Hsp90引导至其靶激酶中起关键作用。 本产品仅用于研究用途,不用于人类、或诊断...
et al. Regulation of Hsp90 ATPase activity by the co-chaperone Cdc37p/p50cdc37. J. Biol. Chem. 277, 20151–20159 (2002). Article CAS PubMed Google Scholar Verba, K. A. et al. Atomic structure of Hsp90-Cdc37-Cdk4 reveals that Hsp90 traps and stabilizes an unfolded kinase. ...
Vaughan, C. K. et al. Structure of an Hsp90-Cdc37-Cdk4 complex.Mol. Cell23, 697–707 (2006).This paper describes the first structure of an HSP90–co-chaperone–client protein complex. ArticleCASPubMedPubMed CentralGoogle Scholar
CDC37 与 Hsp90/HSP90AB1 和 CDK6 形成单独的复合物。它与多种蛋白质相互作用,包括 HSP90AA1、AR、CDK4、CDK6、EIF2AK1、RB1、KSR1、FLCN、FNIP1 和 FNIP2。 种属:Mouse 蛋白编号:Q61081 (M1-A379) 基因ID:12539 同用名:Hsp90 co-chaperone Cdc37; CDC37; CDC37A 热销产品:8-Gingerol | ...