Pharmacologic shifting of a balance between protein refolding and degradation mediated by Hsp90.

@article{Schneider1996PharmacologicSO,
  title={Pharmacologic shifting of a balance between protein refolding and degradation mediated by Hsp90.},
  author={Christof Schneider and Laura Sepp-Lorenzino and Elmar Nimmesgern and Ouathek Ouerfelli and Samuel Danishefsky and Neal Rosen and F. Ulrich Hartl},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1996},
  volume={93 25},
  pages={14536-41}
}
The role of the abundant stress protein Hsp90 in protecting cells against stress-induced damage is not well understood. The recent discovery that a class of ansamycin antibiotics bind specifically to Hsp90 allowed us to address this problem from a new angle. We find that mammalian Hsp90, in cooperation with Hsp70, p60, and other factors, mediates the ATP-dependent refolding of heat-denatured proteins, such as firefly luciferase. Failure to refold results in proteolysis. The ansamycins inhibit… CONTINUE READING
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