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Hsp70 and Hsp40 chaperones can inhibit self-assembly of polyglutamine proteins into amyloid-like fibrils
Paul J. Muchowski, Gregor Schaffar, Annie Sittler and 3 more (opens in a new tab)
Proceedings of the National Academy of Sciences of the United States of America · 2000
doi:10.1073/pnas.140202897 (opens in a new tab)
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Cited by papers we hold 6
- Stress granules, RNA-binding proteins and polyglutamine diseases: too much aggregation? · 2021No notice
- Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation · 2016No notice
- Chaperoning Proteins for Destruction: Diverse Roles of Hsp70 Chaperones and their Co-Chaperones in Targeting Misfolded Proteins to the Proteasome · 2014No notice
- Hsp70 and Its Molecular Role in Nervous System Diseases · 2011No notice
- Modulation of Heat Shock Transcription Factor 1 as a Therapeutic Target for Small Molecule Intervention in Neurodegenerative Disease · 2010No notice
- Heat shock protein 90 in neurodegenerative diseases · 2010No notice
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