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The Hsp90 chaperone facilitates the maturation of client proteins, which are key players in cancer. Hsp90 inhibitor drugs, such as NVP-AUY922, are promising anti-cancer therapies. Co-chaperones regulate the ATPase-dependent Hsp90 activity and specifically, the co-chaperone Aha1 is the most robust...
Hch1p Acts Differently From Its Homologue, Aha1p, in Regulating Sensitivity of Hsp90 to Hsp90 Inhibitors in YeastDownload
Hsp90 is a molecular chaperone that plays a vital role in the regulation of oncoproteins, is targeted by small molecule Hsp90-inhibitors in cancer studies, and is functionally regulated by a cohort of proteins called co-chaperones. We determined that deletion of the co-chaperone Hch1p, but not...
Investigation of Hsp90 Regulation by the Aha-type Co-chaperones: Mechanistic Insight into Two Conserved MotifsDownload
Hsp90 is a highly conserved and essential molecular chaperone. It regulates the folding, maturation, and activation of client proteins involved in a wide range of cellular processes and pathways, many of which are key players in disease. Hsp90 functions in the context of an ATPase driven...