Results 171 to 180 of about 6,022 (190)
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Cdc37: a protein kinase chaperone?
Trends in Cell Biology, 1997The activity of most protein kinases is highly regulated, typically via phosphorylation and/or subunit association. However, the folding of protein kinases into an active state or a form capable of activation is now emerging as another important step through which they can be regulated.
Hunter, Tony R., Poon, Randy Yat Choi
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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
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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
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The Therapeutic Potential of Targeting Hsp90-Cdc37 Interactions in Several Diseases
Current Drug Targets, 2022Abstract: Heat shock protein (Hsp) 90 is an ATP-dependent chaperone and plays a vital role in the folding, maturation, and stability of a protein. Hsp90 and its client proteins have become targets of various diseases through the regulation of disease-related proteins.
Xuerong, Zhang +5 more
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Physical interaction of Cdc28 with Cdc37 in Saccharomyces cerevisiae
Molecular Genetics and Genomics, 2002The Cdc37 protein in Saccharomyces cerevisiae is thought to be a kinase-targeting subunit of the chaperone Hsp90. In a genetic screen, four protein kinases were identified as interacting with Cdc37 - Cdc5, Cdc7, Cdc15 and Cak1. This result underlines the importance of Cdc37 for the folding of protein kinases.
M, Mort-Bontemps-Soret +2 more
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Hsp90 and Cdc37 – a chaperone cancer conspiracy
Current Opinion in Genetics & Development, 2005The Hsp90 molecular chaperone system is involved in the activation of an important set of cell regulatory proteins, including many whose disregulation drives cancer. Recruitment of protein kinases to the Hsp90 system is mediated by the co-chaperone adaptor Cdc37 -- an essential protein whose overexpression is itself, oncogenic.
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Role of Cdc37 in Breast Cancer
1998Abstract : P50CdC37 is a recently discovered gene which functions in the establishment of protein kinase signaling pathways by functioning in complex with molecular chaperone Hsp9O. The proposed mode of function of Cdc37/Hsp9O complex is that Cdc37 targets intrinsically unstable kinases to the complex with Hsp9O, and this transient interaction of newly
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Fission yeast Cdc37 is required for multiple cell cycle functions
Molecular Genetics and Genomics, 2003The identification of a Schizosaccharomyces pombe homologue of the cdc37 gene is described. The gene product is most similar to the budding yeast homologue, but shows similarity to metazoan Cdc37 proteins, with a region of high similarity at the extreme N-terminus. Gene transplacement experiments in diploid cells followed by tetrad dissection show that
P K, Westwood, I V, Martin, P A, Fantes
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Computational investigation of interactions between Cdc37 and celastrol
Molecular Simulation, 2013Celastrol 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 +5 more
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Role of Cdc37 in Breast Cancer
1999Abstract : Estrogen is a key hormonal regulator of mammary epithelial cell growth. Thus, understanding the mechanisms of estrogen-mediated growth regulation is key to understanding to understanding growth disregulation in breast cancer. Current information indicates that estrogen regulates cell growth by activating the Raf-l/Mek/MAP kinase pathway and ...
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Cdk2: A Genuine Protein Kinase Client of Hsp90 and Cdc37
Biochemistry, 2005Hsp90 and its cochaperone Cdc37 cooperate to provide requisite support to numerous protein kinases involved in cellular signal transduction. In this report, we studied the interactions of Hsp90 and Cdc37 with the cyclin-dependent kinase, Cdk2. Treatment of K562 cells with the Hsp90 inhibitor, geldanamycin, caused a 75% reduction in Cdk2 levels and ...
Thomas, Prince +2 more
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