The co-chaperone p50/Cdc37 is an important partner for Hsp90, assisting in molecular chaperone activities, particularly with regard to the regulation of protein kinases. The Hsp90/Cdc37complex controls the folding of a large proportion of protein kinases and thus stands at the hub of a multitud...
Hsp90 chaperone protein kinase-targeting subunitMonoclonal Anti-CDC37 antibody produced in mouseAnti-CDC37 cell division cycle 37 homolog (S. cerevisiae) Hsp90 co-chaperone Cdc37 - Physico-chemical PropertiesAppearance buffered aqueous solution Storage Condition -20°C...
英文名字 CDC37, ID (CDC37, CDC37A, Hsp90 co-chaperone Cdc37, Hsp90 chaperone protein kinase-targeting subunit, p50Cdc37)供应商 MyBioSource产品货号 MBS647830产品报价 ￥询价/0.2mL ￥询价/5x0.2mL ￥询价/其它规格产品说明书 点击查看购买方式 MyBioSource中国区金牌代理,部分产品现货库存。银行转账、...
Cdc37 (also known as p50) is a protein kinase-specific adaptor cochaperone, the interaction of which with protein kinases is primarily mediated by the N-terminal segment (Grammatikakis et al., 1999, Shao et al., 2003a), while the middle and C-terminal regions mediate interaction with Hsp9...
Heat shock protein 90 (Hsp90) is a critical molecular chaperone protein that regulates the folding, maturation, and stability of a wide variety of proteins. In recent years, the development of Hsp90-directed inhibitors has grown rapidly, and many of thes
The co-chaperone p50/Cdc37 is an important partner for Hsp90, assisting in molecular chaperone activities, particularly with regard to the regulation of protein kinases. Analysis of the structure of Hsp90-Cdc37-kinase complexes demonstrates the way in which Cdc37 interacts with and controls the ...
Recruitment of protein kinase clients to the Hsp90 complex appears to involve a specialized co-chaperone, Cdc37p/p50(cdc37), whose binding to Hsp90 is mutually exclusive of Sti1/Hop/p60. We now show that Cdc37p/p50(cdc37), like Sti1/Hop/p60, also suppresses ATP turnover by Hsp90 ...
These results demonstrate that F3-T3 oncogenic function is dependent on the HSP90 chaperone system and suggests a new clinical option for targeting this genetic aberration in cancer. 展开 关键词: CDC37 FGFR3-TACC3 HSP90 TMZ resistance glioma glycosylation ...
Replacement of the phosphorylation site by glutamate affects the conformational dynamics of Hsp90 and interaction with the kinase-specific cochaperone Cdc37. 展开 关键词: Hsp90 evolution molecular chaperone phosphorylation post-translational modification ...
functions.We identified an isoform-specific phosphorylation site in human Hsp90β.The phosphorylated site is conserved throughout vertebrates.Phosphorylation of this site is important for the activation of glucocorticoid receptor.Phosphorylation of this site reduces the affinity for Cdc37 cochaperone.关键...