• Introduction to Protein Folding and Misfolding
• 69 min
  1. Protein folding and misfolding: from theory to therapy

  • Prof. Christopher Dobson
• Stability and Kinetics of Protein Folding
• 55 min
  2. Mechanisms of protein folding reactions

  • Prof. Thomas Kiefhaber
• Protein Folding Theory
• 53 min
  3. Mapping disordered proteins with single-molecule FRET

  • Dr. Hagen Hofmann
• Protein Folding Simulations
• 36 min
  4. Protein folding

  • Prof. Eugene Shakhnovich
• 42 min
  5. Simulating protein folding with full atomistic detail

  • Prof. Vijay Pande
• 58 min
  6. Molecular dynamics simulations of protein dynamics, unfolding and misfolding

  • Prof. Valerie Daggett
• Protein Folding Inside the Cell: Chaperones
• 42 min
  7. Protein folding Inside the cell: macromolecular crowding and protein aggregation

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

  • Prof. Dr. F. Ulrich Hartl
• 60 min
  9. Quality control of proteins mislocalized to the cytosol

  • Dr. Ramanujan Hegde
• Protein Misfolding and Disease
• 44 min
  10. Protein aggregation, metals and oxidative stress in neurodegenerative diseases

  • Prof. David Allsop
• Protein Design
• 33 min
  11. Designing proteins with life sustaining activities 1

  • Prof. Michael Hecht
• 24 min
  12. Designing proteins with life sustaining activities 2

  • Prof. Michael Hecht
• 48 min
  13. Folding and design of helical repeat proteins

  • Prof. Lynne Regan
• 44 min
  14. Design and engineering of zinc-finger domains

  • Prof. Jacqui Matthews
• 47 min
  15. Prediction and design of protein structures and interactions

  • Prof. David Baker
• Amyloid Fibrils: Structure, Formation and Nanotechnology
• 39 min
  16. Amyloid fibrils as functional nanomaterials

  • Prof. Juliet Gerrard
• 37 min
  17. Functional amyloid fibrils from fungi and viruses

  • Prof. Margaret Sunde
• Intrinsically disordered Proteins
• 40 min
  18. Fuzzy protein theory for disordered proteins

  • Prof. Monika Fuxreiter
• Intersection of RNA, translation and protein aggregation.
• 47 min
  19. Expanding roles of RNA-binding proteins in neurodegenerative diseases

  • Prof. Aaron D. Gitler
• Proteostasis
• 49 min
  20. Adapting proteostasis to ameliorate aggregation-associated amyloid diseases

  • Dr. Jeffery W. Kelly
• Archived Lectures *These may not cover the latest advances in the field
• 60 min
  21. Amyloidosis: disease caused by amyloid

  • Prof. Mark Pepys
• 34 min
  22. Protein folding and dynamics from single molecule spectroscopy

  • Prof. Dr. Benjamin Schuler
• 41 min
  23. Prion diseases

  • Prof. Fred Cohen
• 31 min
  24. Basic studies of protein folding and stability: the folding of related protein families

  • Dr. Jane Clarke
• 38 min
  25. Titin I27: a protein with a complex folding landscape

  • Dr. Jane Clarke
• 49 min
  26. Novel proteins from designed combinatorial libraries

  • Prof. Michael Hecht
• 47 min
  27. Fast folding dynamics of small proteins: placing limits on diffusional limits

  • Dr. Stephen Hagen
• 35 min
  28. The sequence determinants of amyloid fibril formation

  • Prof. Fabrizio Chiti

Printable Handouts

PDF

Navigable Slide Index

1. Introduction
2. 'Protein conformational' brain diseases
3. Alzheimer's disease
4. Senile plaques and neurofibrillary tangles
5. Beta-amyloid (A-beta)
6. Paired helical filaments (PHFs)
7. Tau isoforms
8. Molecular genetics of AD
9. Amyloid precursor protein (APP)
10. APP processing pathways
11. APP mutations
12. Effects of APP and PS mutations
13. Amyloid aggregation
14. A-beta oligomers and mature fibrils
15. 'Amyloid cascade' hypothesis
16. A-beta toxic mechanism?
17. Butterfield (1994) and Bush (1999)
18. Does A-beta generate free radicals?
19. Spin traps
20. ESR results
21. Hydrolysis and breakdown of PBN
22. Conclusions from the spectra
23. Does A-beta generate hydrogen peroxide?
24. DMPO hydroxyl radical spectra
25. Possible mechanism of peroxide formation
26. Parkinson's disease (PD)
27. Degeneration of substantia nigra
28. Lewy bodies
29. Alpha-synuclein filaments
30. Gene mutations in familial PD
31. Alpha-synuclein and 'NAC'
32. Other amyloid peptides
33. Does alpha-synuclein generate peroxide?
34. More data on A-beta and alpha-synuclein
35. Toxic prion fragments
36. Cu(II) binding modulates PrP 106-126 toxicity
37. PrP 106-126 ESR spectra
38. Summary of PrP 106-126 data
39. Prion (PrP 121-231) ESR spectra
40. Prion (PrP 121-231) data
41. A-beta (1-40) aggregation vs. peroxide formation
42. ELISA to detect A-beta oligomers
43. Soluble A-beta oligomers generate peroxide?
44. Mature A-beta fibrils do not generate peroxide
45. Familial British dementia peptide (ABri)
46. Time course for ABri
47. Soluble ABri oligomers generate peroxide?
48. No. of CAG repeats and age of onset
49. Are intranuclear inclusions toxic?
50. Common toxic pathway?
51. Conclusions
52. References

Topics Covered

• Introduction to protein conformational brain diseases
• Alzheimer's disease, A-beta and tau
• A-beta oligomers and toxicity
• A-beta generates hydrogen peroxide
• Results from experiments using electron spin resonance spectroscopy
• Parkinson's disease
• Generation of hydrogen peroxide from alpha synuclein, toxic fragments of the prion protein and the familial British dementia peptide
• Early oligomers appear to generate hydrogen peroxide
• Huntington's disease
• Protein aggregates could be protective
• Potential common toxic pathway for these brain diseases

Links

Series:

• Protein Folding, Aggregation and Design

Categories:

• Biochemistry
• Cell Biology
• Clinical Practice
• Neuroscience

Therapeutic Areas:

• Neurology

Talk Citation

Publication History

• Published on October 1, 2007

Financial Disclosures

• Prof. David Allsop has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.