Hsp90 stabilizes mutant huntingtin 1 A SCREEN FOR ENHANCERS OF CLEARANCE IDENTIFIES HUNTINGTIN AS AN HEAT SHOCK PROTEIN 90 (HSP90) CLIENT PROTEIN
نویسندگان
چکیده
Background: Molecular chaperones assist in the folding of metastable proteins implicated in neurodegenerative diseases. Results: Huntingtin is a heat shock protein 90 (Hsp90) client protein Conclusion: Hsp90 inhibition mediated degradation of soluble mutant huntingtin is independent of a cellular heat shock response Significance: Mechanisms targeting Hsp90 chaperone function may provide new treatments for Huntington’s disease
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