NIH Research Festival
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FAES Terrace
NIDDK
MOLBIO-15
Hsp90 is an abundant, highly conserved molecular chaperone that is essential for eukaryotic life. It is a target for cancer therapy and is implicated the in progression of several neurodegenerative diseases. We recently showed that ATP hydrolysis is dispensable for Hsp90 function in vivo. These and other findings disagree with the current model of Hsp90 as an active machine that uses the energy from ATP hydrolysis to remodel client proteins. Here, we present findings that expand upon our recent work, and we propose a novel theory on the role of ATP in Hsp90 function.
Scientific Focus Area: Molecular Biology and Biochemistry
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