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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
- Protein self assembly and protein aggregation
- Origins of the molecular chaperone concept (1)
- Rubisco: the world's most abundant protein
- Rubisco characteristics
- Rubisco large subunit binding protein
- Discovery of the chaperonins
- Homologues of BiP form the hsp70 family
- Origins of the molecular chaperone concept (2)
- The march of molecular chaperones
- Definition of molecular chaperones
- The molecular chaperone function
- Protein folding in vivo vs. refolding in vitro
- The principles of protein self assembly
- The distinction between folding and assembly
- Assembly chaperones
- Why are chaperones required in the nucleus?
- Effect of nuclear chaperones on nucleosomes
- Structure and assembly of nucleosomes
- Functions and structure of nucleoplasmin
- Model for chaperone function of nucleoplasmin
- Model for chaperone function of GroEL/GroES
- Effect of RbcX on Rubisco in Synechococcus
- RbcX function in cyanobacterial assembly
- Structure of Rubisco L subunit-RbcX complex
Topics Covered
- Definition of protein self-assembly and aggregation
- First use of the term 'molecular chaperone'
- Nucleoplasmin
- Chloroplast rubisco aggregation
- The chaperonins
- The general chaperone concept
- Definition of 'molecular chaperone'
- The chaperone function
- Protein folding on polysomes
- Macromolecular crowding
- Folding and assembly chaperones
- Nuclear chaperones
- Nucleosome assembly
- Mechanism of nucleoplasmin action
- The rubisco assembly chaperone RbcX
Talk Citation
Ellis, R.J. (2007, October 1). History of the molecular chaperone concept: roles in assembly processes [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved April 1, 2025, from https://doi.org/10.69645/YKNF9012.Export Citation (RIS)
Publication History
- Published on October 1, 2007
Financial Disclosures
- Prof. Emeritus R. John Ellis has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.
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