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Printable Handouts
Navigable Slide Index
- Introduction
- Outcomes of misfolded protein aggregation
- The study of neurodegenerative diseases
- Regulation of Hsp70 function by Hsp40
- Domain structure of Hsp40 family members
- Functional specificity of Type I and Type II HSP40
- Hsp70 and Hsp40s act via opposing mechanisms
- Hsp40s differentially modulate fibril formation
- RNQ+ as a model system for amyloid assembly
- Rnq1 forms self-perpetuating aggregates
- Hsp40 types - opposing roles on RNQ+ assembly
- Sis1 and Ydj1 recognize different regions of Rnq1
- Hsp40 types bind different regions of Rnq1 prions
- Rnq1 elevation kills yeast containing RNQ+ prions
- Overexpression of Sis1 suppresses Rnq1 toxicity
- A possible mechanism for Rnq1 toxicity?
- Sis1 decreases unassembled Rnq1 pool
- Sis1 promotes RNQ prion accumulation
- RNQ prion accumulation may help reduce toxicity
- How type I Hsp40s suppress amyloid formation
- Rnq1 prion domain overexpression in yeast
- Ydj1 required for tolerance of PrD overexpression
- Ydj1 overexpression inhibits PrD aggregation
- PrD accumulation in the absence of Ydj1
- A model for PRD prion formation
- Hsp40s suppress proteotoxicity in different ways
- Acknowledgements
Topics Covered
- Protein aggregation in conformational disease
- The Hsp40 system
- The Hsp70 system
- Small oligomers, prion, yeast, Huntington's disease and protein triage
- Mechanisms for proteotoxicity
- Mechanisms for amyloid disease
Links
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Talk Citation
Cyr, D.M. (2012, February 20). Roles for Hsp40 molecular chaperones in protein misfolding disease [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved April 15, 2025, from https://doi.org/10.69645/GMGJ2525.Export Citation (RIS)
Publication History
- Published on February 20, 2012
Financial Disclosures
- Prof. Douglas M. Cyr has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.