• Overview of Molecular Chaperones
• 34 min
  1. History of the molecular chaperone concept: roles in assembly processes

  • Prof. Emeritus R. John Ellis
• 34 min
  2. Chaperone mechanisms in cellular protein folding

  • Prof. Dr. F. Ulrich Hartl
• Prokaryotic Molecular Chaperones
• 38 min
  3. Mechanistic aspects of chaperonin GroEL/ES function

  • Prof. Amnon Horovitz
• 99 min
  4. Structure and function of the ATP-dependent Clp chaperone/protease machines

  • Dr. Michael R. Maurizi
• 32 min
  5. The role of chaperones and Sec machinery in protein secretion

  • Prof. Koreaki Ito
• 44 min
  6. How can molecular chaperones repair damaged protein structures?

  • Prof. Pierre Goloubinoff
• 32 min
  7. Disulfide bond formation in vivo

  • Prof. James Bardwell
• Eukaryotic Molecular Chaperones
• 39 min
  8. Overview of eukaryotic molecular chaperones in the cytosol

  • Dr. Jason C. Young
• 36 min
  9. Chaperonin-containing TCP-1 (CCT), actin springs, and protein folding fluxes

  • Prof. Keith Willison
• 35 min
  10. The functions of the Hsp70 system

  • Prof. Jeffrey L. Brodsky
• 26 min
  11. Hsp90: a chaperone for protein kinases and hormone receptors

  • Dr. David Toft
• Role of Chaperones in Diseases
• 38 min
  12. The roles of molecular chaperones in bacterial infection

  • Prof. Tomoko Yamamoto
• 46 min
  13. Role of chaperonin-like proteins in Bardet-Biedl syndrome

  • Dr. Michel R. Leroux
• 53 min
  14. Roles for molecular chaperones in cystic fibrosis

  • Prof. Douglas M. Cyr
• 51 min
  15. Targeting cancer: designing drugs against Hsp90

  • Dr. Gabriela Chiosis
• Archived Lectures *These may not cover the latest advances in the field
• 29 min
  16. Overview of prokaryotic molecular chaperones

  • Prof. Walid A. Houry
• 47 min
  17. The biogenesis of E. coli inner membrane proteins

  • Dr. Joen Luirink
• 39 min
  18. Mechanism of chaperone action of small heat shock proteins

  • Prof. Elizabeth Vierling
• 22 min
  19. ClpB: a chaperone for protein disaggregation

  • Prof. Michal Zolkiewski
• 38 min
  20. The roles of chaperonins in bacteria

  • Dr. Peter Lund
• 44 min
  21. Towards a unifying mechanism for the Hsp70 chaperones

  • Prof. Pierre Goloubinoff
• 29 min
  22. Adaptor mediated activation of the Hsp100/ Clp protein ClpC controls general and regulatory proteolysis in Bacillus subtilis

  • Prof. Dr. Kursad Turgay
• 33 min
  23. Hsp31: a general stress protein of Escherichia coli

  • Prof. Francois Baneyx
• 46 min
  24. Hsp104: a specialized chaperone for protein disaggregation

  • Dr. John R. Glover
• 47 min
  25. Molecular chaperones and handling of abnormal proteins in neurodegenerative disorders

  • Prof. Michael Sherman
• 20 min
  26. The role of chaperones in Parkinson's disease

  • Dr. Konstanze F. Winklhofer

Printable Handouts

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Navigable Slide Index

1. Introduction
2. Protein folding
3. Transitions during protein folding
4. Protein folding in the cytosol - evolution
5. The role of mitochondria in protein folding
6. Protein folding in vitro and in mitochondria
7. Aggregation following productive protein folding
8. Interior of a dyctiostelium cell
9. Reconstitution of GroEL-assisted folding
10. Electron micrographs of GroEL
11. Binding of GroES to GroEL
12. GroES and GroEL function as a cage for proteins
13. GroEL mutant Asn229Cys
14. The effect of blocking protein rebinding to GroEL
15. GroEL/GroES accelerates the folding of proteins
16. Proteomic methods to identify GroEL substrates
17. Hsp70 and chaperonins
18. Hsp70 and GroEL/ES roles in protein folding
19. Co-translational chaperoning
20. Nascent chain-binding chaperones
21. Interaction of DnaK with nascent polypeptides
22. Pulse-chase experiments with DnaK
23. Protein folding in the cytosol
24. Structure of prefoldin
25. Hydrophobic patches as sites for substrate binding
26. Can chaperons suppress toxicity of misfolding?
27. Common features of neurodegenerative disorders
28. Amyloid fibrils in neurogenerative diseases
29. Chaperones and the formation of huntingtin fibrils
30. HSP70/40 action on aggregation process
31. Chaperone capacity and misfolded proteins
32. Geldanamycin inhibits huntingtin aggregation

Topics Covered

• The effect of protein aggregation on productive protein folding
• The function of GroEL and GroES as a folding cage for proteins
• Changes in energy landscape within the folding cage
• Cooperation of different chaperone systems in folding pathways: Hsp70 and chaperonins
• Binding of the Hsp70 homologue protein, DnaK, to newly-synthesized polypeptides
• The role of chaperone mechanisms in toxicity suppression of misfolded disease causing proteins
• Potential uses of the chaperone mechanisms in disease therapeutics

Links

Series:

• Molecular Chaperones
• Protein Folding, Aggregation and Design

Categories:

• Biochemistry
• Cell Biology

Talk Citation

Publication History

• Published on October 1, 2007

Financial Disclosures

• Prof. Dr. F. Ulrich Hartl has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.