Search
Skip to Search Results-
Enzymatic and Biochemical Analysis of the Hsp90 Chaperone: Regulation by Co-chaperones, SUMOylation, and Interdomain Dynamics
DownloadFall 2017
Hsp90 is an essential eukaryotic molecular chaperone that plays a critical role in protein folding. It regulates the stability, maturation, and activation of numerous client proteins, many of which are involved in oncogenesis. It has been well established that Hsp90 is tightly regulated by...
-
Hch1p Acts Differently From Its Homologue, Aha1p, in Regulating Sensitivity of Hsp90 to Hsp90 Inhibitors in Yeast
DownloadSpring 2013
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 Motifs
DownloadSpring 2019
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...