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The protein encoded by CDC37 is highly similar to Cdc 37, a cell division cycle control protein of Sacchromyces cerevisiae. Zusätzlich bieten wir Ihnen CDC37 Antikörper (150) und CDC37 Proteine (19) und viele weitere Produktgruppen zu diesem Protein an.
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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 (zeige HSP90 ELISA Kits) in hepatocellular carcinoma, reducing tumor growth.
Cdc37 performs a quality control of protein kinases, including b-raf (zeige SNRPE ELISA Kits), where induced conformational instability acts as a "flag" for Hsp90 (zeige HSP90 ELISA Kits) dependence and stable cochaperone association.
Ulk1 (zeige ULK1 ELISA Kits) promoted the degradation of Hsp90 (zeige HSP90 ELISA Kits)-Cdc37 client kinases, resulting in increased cellular sensitivity to Hsp90 (zeige HSP90 ELISA Kits) inhibitors. Thus, our study provides evidence for an anti-proliferative role of Ulk1 (zeige ULK1 ELISA Kits) in response to Hsp90 (zeige HSP90 ELISA Kits) inhibition in cancer cells
The authors find that the interaction between sB-Raf (zeige RAF1 ELISA Kits) and the Hsp90 chaperone (zeige HSP90 ELISA Kits) system is based on contacts with the M domain of Hsp90 (zeige HSP90 ELISA Kits), 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 (zeige RIPK3 ELISA Kits) activation following the induction of necroptosis requires the activity of an HSP90 (zeige HSP90 ELISA Kits) and CDC37 cochaperone complex.
Correlation between PDZK1 (zeige PDZK1 ELISA Kits), Cdc37, Akt (zeige AKT1 ELISA Kits) and breast cancer malignancy: the role of PDZK1 (zeige PDZK1 ELISA Kits) in cell growth through Akt (zeige AKT1 ELISA Kits) 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 (zeige HSP90 ELISA Kits) binding.
A series of tyrosine phosphorylation events, involving both p50(Cdc37) and Hsp90 (zeige HSP90 ELISA Kits), are minimally sufficient to provide directionality to the chaperone cycle.
Hsp90 (zeige HSP90 ELISA Kits)-Cdc37 complex acta (zeige ACTC1 ELISA Kits) as an endogenous regulator of noncanonical p38alpha (zeige MAPK14 ELISA Kits) activity.
CDC37 binds to Akt (zeige AKT1 ELISA Kits) and HSP90 (zeige HSP90 ELISA Kits) in the signal transduction pathway in human tumor cells
The interaction between mouse Pem and Cdc37 homolog was then confirmed by glutathione S-transferase (zeige GSTa2 ELISA Kits) pull-down assay, and the possible interaction model was suggested.
JAK1 (zeige JAK1 ELISA Kits)/2 are client proteins of Hsp90 alpha (zeige HSP90AA1 ELISA Kits) and beta; Hsp90 (zeige HSP90 ELISA Kits) and CDC37 play a critical role in types I and II interferon (zeige IFNA ELISA Kits) pathways
This growth inhibition is partially rescued by expression of ectopic Gli1 (zeige GLI1 ELISA Kits), 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 (zeige NOS3 ELISA Kits)) and may play an important role in mediating the eNOS (zeige NOS3 ELISA Kits) 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