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- Overview of Molecular Chaperones
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1. History of the molecular chaperone concept: roles in assembly processes
- Prof. Emeritus R. John Ellis
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2. Chaperone mechanisms in cellular protein folding
- Prof. Dr. F. Ulrich Hartl
- Prokaryotic Molecular Chaperones
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3. Mechanistic aspects of chaperonin GroEL/ES function
- Prof. Amnon Horovitz
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4. Structure and function of the ATP-dependent Clp chaperone/protease machines
- Dr. Michael R. Maurizi
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5. The role of chaperones and Sec machinery in protein secretion
- Prof. Koreaki Ito
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6. How can molecular chaperones repair damaged protein structures?
- Prof. Pierre Goloubinoff
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7. Disulfide bond formation in vivo
- Prof. James Bardwell
- Eukaryotic Molecular Chaperones
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8. Overview of eukaryotic molecular chaperones in the cytosol
- Dr. Jason C. Young
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9. Chaperonin-containing TCP-1 (CCT), actin springs, and protein folding fluxes
- Prof. Keith Willison
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10. The functions of the Hsp70 system
- Prof. Jeffrey L. Brodsky
- Role of Chaperones in Diseases
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12. The roles of molecular chaperones in bacterial infection
- Prof. Tomoko Yamamoto
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13. Role of chaperonin-like proteins in Bardet-Biedl syndrome
- Dr. Michel R. Leroux
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14. Roles for molecular chaperones in cystic fibrosis
- Prof. Douglas M. Cyr
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15. Targeting cancer: designing drugs against Hsp90
- Dr. Gabriela Chiosis
- Archived Lectures *These may not cover the latest advances in the field
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16. Overview of prokaryotic molecular chaperones
- Prof. Walid A. Houry
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17. The biogenesis of E. coli inner membrane proteins
- Dr. Joen Luirink
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18. Mechanism of chaperone action of small heat shock proteins
- Prof. Elizabeth Vierling
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19. ClpB: a chaperone for protein disaggregation
- Prof. Michal Zolkiewski
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20. The roles of chaperonins in bacteria
- Dr. Peter Lund
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21. Towards a unifying mechanism for the Hsp70 chaperones
- Prof. Pierre Goloubinoff
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23. Hsp31: a general stress protein of Escherichia coli
- Prof. Francois Baneyx
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24. Hsp104: a specialized chaperone for protein disaggregation
- Dr. John R. Glover
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26. The role of chaperones in Parkinson's disease
- Dr. Konstanze F. Winklhofer
Printable Handouts
Navigable Slide Index
- Introduction
- Neurodegenerative disorders
- Neurodegenerative disorders - inclusion bodies
- Fate of a protein in the cell
- Mutations in UPS components and chaperones
- The ubiquitin-proteasome system
- Role of CHIP in protein degradation
- The aggresome
- Tracing aggresome formation
- Microtubules important for aggresome formation
- Protective role of the aggresome
- Role of HDAC6 in aggresome formation
- Molecular chaperones and neurodegeneration
- Hsp70 overexpression and Kennedy's disease
- Hsp70 overexpression in Drosophila
- CHIP overexpression and Kennedy's disease
- Chemical induction of heat-shock proteins
- Stress and induction of heat-shock proteins
- Heat shock response
- Defects in chaperone system
- Chaperones in Huntington's disease model
- Heat shock response in polyQ-expressing cells
- Defects in UPS
- Measurements of proteasome activity in a cell
- UPS activity inhibition in cells with aggresomes
- Proteasome subunits and Hsp70 in PD brain
- Chaperone system and UPS defects with aging
- Aging signaling pathways
- Decrease in chaperone expression upon aging
- Decrease in proteasome activity upon aging
- Generation of Ubb+1 frameshift mutation
- Age-dependence of aggregation
- Aggregation in long-lived C. elegans mutants
- Neurological problems and aging
Topics Covered
- Aggregation of proteins associated with neurodegenerative disorders
- Mechanisms of aggresome formation
- Suppression of the heat shock response in aging and neurodegeneration
- Role of heat shock proteins in suppression of apoptosis and senescence programs
Links
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Talk Citation
Sherman, M. (2007, October 1). Molecular chaperones and handling of abnormal proteins in neurodegenerative disorders [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved April 1, 2025, from https://doi.org/10.69645/YKLD8439.Export Citation (RIS)
Publication History
Financial Disclosures
- Prof. Michael Sherman has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.
Molecular chaperones and handling of abnormal proteins in neurodegenerative disorders
A selection of talks on Biochemistry
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