Results 171 to 180 of about 3,509 (196)
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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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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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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
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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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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Domain-Mediated Dimerization of the Hsp90 Cochaperones Harc and Cdc37
Biochemistry, 2005Hsp90 is a highly conserved molecular chaperone that acts in concert with Hsp70 and a cohort of cochaperones to mediate the folding of client proteins into functional conformations. The novel Hsp90 cochaperone Harc was identified previously on the basis of its amino acid sequence similarity to Cdc37.
John, Roiniotis +3 more
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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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Role of Cdc37 in Protein Kinase Folding
2007As nascent chains emerge from the ribosome, they interact with molecular chaperone proteins that prevent aggregation and promote protein folding. Chaperones such as Hsp70 and Hsp40 function together to protect nascent chains while still ribosome bound, and function with little if any specificity for the unfolded polypeptide.
Atin K. Mandal +2 more
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Exposure of protein kinase motifs that trigger binding of Hsp90 and Cdc37
Biochemical and Biophysical Research Communications, 2005Hsp90 and its co-chaperone Cdc37 are required for the activity of numerous eukaryotic protein kinases. c-Jun N-terminal kinases (JNKs) appear to be Hsp90-independent kinases, as their activity is unaffected by Hsp90 inhibition. It is currently unknown why some protein kinases are Hsp90- and Cdc37-dependent for their function, while others are not ...
Thomas, Prince, Robert L, Matts
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