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The protein encoded by CDC37 is highly similar to Cdc 37, a cell division cycle control protein of Sacchromyces cerevisiae. 再加上，我们可以发CDC37 抗体 (150) 和 CDC37 蛋白 (19)和数多这个蛋白质的别的产品。
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The results suggest a re-evaluation of the role of Cdc37 in the kinase lifecycle, and suggest that such interactions potentially allow kinases to more rapidly respond to key signals while simultaneously protecting unstable kinases from degradation and suppressing unwanted basal activity.
Niclosamide ethanolamine disrupted the interaction between cell division cycle 37 and heat shock protein 90 (显示 HSP90 ELISA试剂盒) in hepatocellular carcinoma, reducing tumor growth.
Cdc37 performs a quality control of protein kinases, including b-raf (显示 SNRPE ELISA试剂盒), where induced conformational instability acts as a "flag" for Hsp90 (显示 HSP90 ELISA试剂盒) dependence and stable cochaperone association.
Ulk1 (显示 ULK1 ELISA试剂盒) promoted the degradation of Hsp90 (显示 HSP90 ELISA试剂盒)-Cdc37 client kinases, resulting in increased cellular sensitivity to Hsp90 (显示 HSP90 ELISA试剂盒) inhibitors. Thus, our study provides evidence for an anti-proliferative role of Ulk1 (显示 ULK1 ELISA试剂盒) in response to Hsp90 (显示 HSP90 ELISA试剂盒) inhibition in cancer cells
The authors find that the interaction between sB-Raf (显示 RAF1 ELISA试剂盒) and the Hsp90 chaperone (显示 HSP90 ELISA试剂盒) system is based on contacts with the M domain of Hsp90 (显示 HSP90 ELISA试剂盒), which contributes in forming the ternary complex with Cdc37 as long as the kinase is not stabilized by nucleotide.
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 (显示 RIPK3 ELISA试剂盒) activation following the induction of necroptosis requires the activity of an HSP90 (显示 HSP90 ELISA试剂盒) and CDC37 cochaperone complex.
Correlation between PDZK1 (显示 PDZK1 ELISA试剂盒), Cdc37, Akt (显示 AKT1 ELISA试剂盒) and breast cancer malignancy: the role of PDZK1 (显示 PDZK1 ELISA试剂盒) in cell growth through Akt (显示 AKT1 ELISA试剂盒) 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 (显示 HSP90 ELISA试剂盒) binding.
A series of tyrosine phosphorylation events, involving both p50(Cdc37) and Hsp90 (显示 HSP90 ELISA试剂盒), are minimally sufficient to provide directionality to the chaperone cycle.
Hsp90 (显示 HSP90 ELISA试剂盒)-Cdc37 complex acta (显示 ACTC1 ELISA试剂盒) as an endogenous regulator of noncanonical p38alpha (显示 MAPK14 ELISA试剂盒) activity.
CDC37 binds to Akt (显示 AKT1 ELISA试剂盒) and HSP90 (显示 HSP90 ELISA试剂盒) in the signal transduction pathway in human tumor cells
The interaction between mouse Pem and Cdc37 homolog was then confirmed by glutathione S-transferase (显示 GSTa2 ELISA试剂盒) pull-down assay, and the possible interaction model was suggested.
JAK1 (显示 JAK1 ELISA试剂盒)/2 are client proteins of Hsp90 alpha (显示 HSP90AA1 ELISA试剂盒) and beta; Hsp90 (显示 HSP90 ELISA试剂盒) and CDC37 play a critical role in types I and II interferon (显示 IFNA ELISA试剂盒) pathways
This growth inhibition is partially rescued by expression of ectopic Gli1 (显示 GLI1 ELISA试剂盒), suggesting that Fu may contribute to enhance Hh signaling activity in cancer cells.
Cdc37 has a direct regulatory interaction with endothelial nitric oxide synthase (eNOS (显示 NOS3 ELISA试剂盒)) and may play an important role in mediating the eNOS (显示 NOS3 ELISA试剂盒) protein complex formation.
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 protein
, hsp90 co-chaperone Cdc37
, Hsp90 co-chaperone Cdc37
, hypothetical protein
, 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
, CDC37 (cell division cycle 37 S. cerevisiae homolog)
, CDC37 cell division cycle 37 protein
, CDC37 homolog
, cell division cycle 37 protein
, cell division cycle control protein 37