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Printable Handouts
Navigable Slide Index
- Introduction
- Protein folding and aggregation
- Thermotolerance
- Protein synthesis during heat shock
- Hsp104 is crucial for thermotolerance in yeast
- Hsp104 restores ultrastructure after heat shock
- Hsp104-dependent resolubilization of proteins
- Hsp104-dependent enzyme activity reactivation
- Hsp104 has unique properties
- The assay for Hsp104-dependent refolding
- Hsp104 works together with Hsp70/40
- Hsp104 is required for the refolding of proteins
- Bichaperone networks
- The second aggregation mode
- Prions
- Prions in yeast
- The prion form of Sup35 is aggregated
- Prions recruit newly synthesized Sup35
- Self-seeded aggregation of Sup35 in vitro
- Nonsense codon suppression in [PSI+] cells
- Hsp104 and prion stability
- Prion aggregate disassembly
- Hsp104 and Sup35 fibril assembly
- Hsp104: a member of AAA+ superfamily
- AAA+ complexes
- The Clp/Hsp100 family
- Clp/Hsp100 complexes
- A structural model of ClpB
- Hsp100-mediated degradation
- Axial channel loops
- Mutations in axial loops reduce thermotolerance
- Common mechanism of Hsp100 function?
- Aggregates may be dynamic structures
- Partial disaggregation by molecular chaperones
- Hsp104 completes the release of proteins
- Chaperones bind disease-associated proteins
- Hsp104 functions in hybrid bichaperone network
- Hsp104 transgene reduces aggregation
- Future questions
Topics Covered
- Heat shock
- Molecular chaperones and thermotolerance
- Protein aggregation and refolding
- Prions in mammals and yeast
- Molecular chaperones and protein aggregation associated with human disease
Talk Citation
Glover, J.R. (2007, October 1). Hsp104: a specialized chaperone for protein disaggregation [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved December 27, 2024, from https://doi.org/10.69645/AVIT8698.Export Citation (RIS)
Publication History
Financial Disclosures
- Dr. John R. Glover has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.