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The protein encoded by CDC37 is highly similar to Cdc 37, a cell division cycle control protein of Sacchromyces cerevisiae. Additionally we are shipping CDC37 Antibodies (5) and many more products for this protein.
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Apart from these distinct Cdc37/Hsp90 interfaces, binding of the B-Raf protein kinase to the cochaperone is conserved between mammals and nematodes.
Suppressing expression of the cochaperone CDC37 in hepatocellular carcinoma cells inhibits cell cycle progression and cell growth.
RIP3 (show RIPK3 Proteins) activation following the induction of necroptosis requires the activity of an HSP90 (show HSP90 Proteins) and CDC37 cochaperone complex.
Correlation between PDZK1 (show PDZK1 Proteins), Cdc37, Akt (show AKT1 Proteins) and breast cancer malignancy: the role of PDZK1 (show PDZK1 Proteins) in cell growth through Akt (show AKT1 Proteins) stabilization by increasing and interacting with Cdc37
The N-terminal tail serves as an intramolecular chaperone ensuring that CDC37 assumes one of two interconvertible states in a manner impacting the interaction of the client binding N-domain and the MC-domains, involved in dimerization and HSP90 (show HSP90 Proteins) binding.
CDC37 has an important role in chaperoning protein kinases; it stabilizes kinase clients by a mechanism that is not dependent on a substantial direct interaction between CDC37 and HSP90 (show HSP90 Proteins), but requires HSP90 (show HSP90 Proteins) activity
As a novel Hsp90 (show HSP90 Proteins) inhibitor, FW-04-806 binds to the N-terminal of Hsp90 (show HSP90 Proteins) and inhibits Hsp90 (show HSP90 Proteins)/Cdc37 interaction, resulting in the disassociation of Hsp90 (show HSP90 Proteins)/Cdc37/client complexes and the degradation of Hsp90 (show HSP90 Proteins) client proteins.
CDC37 is a crucial HSP90 (show HSP90 Proteins)-cofactor for KIT oncogenic expression in gastrointestinal stromal tumors
SGK3 (show SGK3 Proteins) stability and kinase activation are regulated by the Hsp90 (show HSP90 Proteins)-Cdc37 chaperone complex.
Cdc37 (cell division cycle 37) restricts Hsp90 (heat shock protein 90 (show HSP90 Proteins)) motility by interaction with N-terminal and middle domain binding sites.
A series of tyrosine phosphorylation events, involving both p50(Cdc37) and Hsp90 (show HSP90 Proteins), are minimally sufficient to provide directionality to the chaperone cycle.
Hsp90 (show HSP90 Proteins)-Cdc37 complex acta (show ACTC1 Proteins) as an endogenous regulator of noncanonical p38alpha (show MAPK14 Proteins) activity.
CDC37 binds to Akt (show AKT1 Proteins) and HSP90 (show HSP90 Proteins) in the signal transduction pathway in human tumor cells
The interaction between mouse Pem and Cdc37 homolog was then confirmed by glutathione S-transferase (show GSTa2 Proteins) pull-down assay, and the possible interaction model was suggested.
JAK1 (show JAK1 Proteins)/2 are client proteins of Hsp90 alpha (show HSP90AA1 Proteins) and beta; Hsp90 (show HSP90 Proteins) and CDC37 play a critical role in types I and II interferon (show IFNA Proteins) pathways
This growth inhibition is partially rescued by expression of ectopic Gli1 (show GLI1 Proteins), suggesting that Fu may contribute to enhance Hh signaling activity in cancer cells.
The protein encoded by this gene is highly similar to Cdc 37, a cell division cycle control protein of Sacchromyces cerevisiae. This protein is a molecular chaperone with specific function in cell signal transduction. It has been shown to form complex with Hsp90 and a variety of protein kinases including CDK4, CDK6, SRC, RAF-1, MOK, as well as eIF2 alpha kinases. It is thought to play a critical role in directing Hsp90 to its target kinases.
CDC37 (cell division cycle 37, S. cerevisiae, homolog)
, CDC37 cell division cycle 37 homolog
, cell division cycle 37 homolog
, hsp90 chaperone protein kinase-targeting subunit
, hsp90 co-chaperone Cdc37
, CDC37 (cell division cycle 37 S. cerevisiae homolog)