Results 161 to 170 of about 3,509 (196)
Computational investigation of interactions between Cdc37 and celastrol
Molecular Simulation, 2013 Celastrol is a novel inhibitor of the human protein complex Hsp90–Cdc37. It was found that the N-terminal domain of Cdc37 (Cdc37_N) was the molecular target for celastrol binding through covalent bonding. To get insight into the binding mode of celastrol in the active site of Cdc37, herein, the homology models of Cdc37_N and N-terminal/middle domain of
Yaokai Duan +2 more
exaly +3 more sources
Oncogene, 2013 The HSP90 molecular chaperone plays a key role in the maturation, stability and activation of its clients, including many oncogenic proteins. Kinases are a substantial and important subset of clients requiring the key cochaperone CDC37.
Emmanuel de Billy +2 more
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Targeting the oncogene and kinome chaperone CDC37 [PDF]
Nature Reviews Cancer, 2008 CDC37 is a molecular chaperone that physically stabilizes the catalytic domains found in protein kinases and is therefore a wide-spectrum regulator of protein phosphorylation. It is also an overexpressed oncoprotein that mediates carcinogenesis by stabilizing the compromised structures of mutant and/or overexpressed oncogenic kinases. Recent work shows
Thomas Prince +2 more
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Induction of human Cdc37 in prostate cancer correlates with the ability of targeted Cdc37 expression to promote prostatic hyperplasia [PDF]
Oncogene, 2000 The Cdc37 gene encodes a 50 kDa protein which targets intrinsically unstable oncoprotein kinases such as Cdk4, Raf-1, and src to the molecular chaperone Hsp90. This activity is thought to play an important role in the establishment of signaling pathways controlling cell proliferation.
Milton Finegold +2 more
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MZF1 and SCAND1 Reciprocally Regulate CDC37 Gene Expression in Prostate Cancer [PDF]
Cancers, 2019 Cell division control 37 (CDC37) increases the stability of heat shock protein 90 (HSP90) client proteins and is thus essential for numerous intracellular oncogenic signaling pathways, playing a key role in prostate oncogenesis.
Takanori Eguchi +2 more
exaly +3 more sources
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Cdc37 as a Co-chaperone to Hsp90
2022The 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 folding of a large proportion of intracellular protein ...
Thomas L, Prince +4 more
openaire +2 more sources
The molecular chaperone Cdc37 is required for Ste11 function and pheromone-induced cell cycle arrest
FEBS Letters, 2000 The molecular chaperone Cdc37 is thought to act in part as a targeting subunit of the heat-shock protein 90 (Hsp90) chaperone complex. We demonstrate here that Cdc37 is required for activity of the kinase Ste11 in budding yeast.
Olivier Donze, Didier Picard
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Bioorganic and Medicinal Chemistry, 2017
Targeting Hsp90-Cdc37 protein-protein interaction (PPI) is becoming an alternative approach for future anti-cancer drug development. We previously reported the discovery of an eleven-residue peptide (Pep-1) with micromolar activity for the disruption of Hsp90-Cdc37 PPI.
Lei Wang, Zheng-Yu Jiang, Qidong You
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Targeting Hsp90-Cdc37 protein-protein interaction (PPI) is becoming an alternative approach for future anti-cancer drug development. We previously reported the discovery of an eleven-residue peptide (Pep-1) with micromolar activity for the disruption of Hsp90-Cdc37 PPI.
Lei Wang, Zheng-Yu Jiang, Qidong You
exaly +3 more sources
Cdc37 is essential for chromosome segregation and cytokinesis in higher eukaryotes [PDF]
EMBO Journal, 2002 Cdc37 has been shown to be required for the activity and stability of protein kinases that regulate different stages of cell cycle progression. However, little is known so far regarding interactions of Cdc37 with kinases that play a role in cell division. Here we show that the loss of function of Cdc37 in Drosophila leads to defects in mitosis and male
Elena Rebollo, Cayetano Gonzalez
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Protein Expression and Purification, 2013
Hsp90 has emerged as a promising target for cancer treatment. Hsp90 interacts with co-chaperone Cdc37 to mediate the conformational maturation of its kinase client proteins. Screening small molecule inhibitors targeting Hsp90/Cdc37 might be a promising strategy for further cancer therapeutic.
Jing, He +7 more
openaire +2 more sources
Hsp90 has emerged as a promising target for cancer treatment. Hsp90 interacts with co-chaperone Cdc37 to mediate the conformational maturation of its kinase client proteins. Screening small molecule inhibitors targeting Hsp90/Cdc37 might be a promising strategy for further cancer therapeutic.
Jing, He +7 more
openaire +2 more sources