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The Biochemical Characterization of the ATPase activity of three Hsp82 point mutants: Hsp82pA587T, Hsp82pG313S, and Hsp82pE381K
DownloadFall 2012
Chaperones are family of proteins that assist in protein folding. 90 kDa Heat shock protein (Hsp90 mammalians, Hsp82 in Saccharomyces cerevisiae) is a well conserved chaperone that is essential for eukaryotic viability. The Hsp90 cycle is regulated by the ability to hydrolyze ATP, and through the...
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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...
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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...
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Characterization of the motif requirements for the function of Aha1p and its homologue Hch1p
DownloadFall 2013
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...