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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
- Parkinson's disease (PD)
- Pathophysiology of PD
- Clinical manifestations of PD
- Neuropathology of PD
- Etiology of PD
- Genetics of PD
- Alpha-synuclein
- Mutations in gene encoding alpha-synuclein
- Alpha-synuclein - possible toxicity mechanisms
- Drosophila models of PD and chaperones
- Mouse genetic model of PD and chaperones
- Mouse toxic model of PD and chaperones
- Protective effects of chaperones - explained
- Hsp70 effect on alpha-synuclein aggregation (1)
- Hsp70 effect on alpha-synuclein aggregation (2)
- Model for alpha-synuclein fibrillization pathway
- Parkin
- Parkin mutations
- Parkin inactivation mechanisms (1)
- Chaperone interference with parkin misfolding
- Parkin inactivation mechanisms (2)
- Parkin has an E3 ubiquitin ligase activity
- Parkin inactivation leads to neuronal death (1)
- Parkin inactivation leads to neuronal death (2)
- Summary
Topics Covered
- Parkinson's disease
- Pathophysiology, neuropathology, etiology
- Genes associated with Parkinson's disease
- Role of protein misfolding in Parkinson's disease
- alpha-synuclein: protein misfolding and a gain of toxic function
- Parkin: protein misfolding and a loss of physiological function
- Effect of chaperones in different models of Parkinson's disease
Links
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Talk Citation
Winklhofer, K.F. (2007, October 1). The role of chaperones in Parkinson's disease [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved April 1, 2025, from https://doi.org/10.69645/AOZA9523.Export Citation (RIS)
Publication History
Financial Disclosures
- Dr. Konstanze F. Winklhofer has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.