Arches. Photo by Daniel Chia
HOPES: Huntington's Outreach Project for Education, at Stanford

HSP 90

heat shock protein that acts as a molecular chaperone to proteins involved in the progression of cancer. It also binds and associates with HSF-1. Geldenamycin binds to and inhibits Hsp 90, leading to both the misfolding of cancer-associated proteins and the freeing-up of HSF-1, which can then prevent misfolded huntingtin protein aggregation through the effects of Hsp 70 and Hsp 40.