Non-fibrillar Amyloidogenic Protein Assemblies - Common Cytotoxins Underlying Degenerative Diseases

Aberrant protein folding and self-assembly underlie over 30 human diseases called amyloidoses, for which currently there is no cure. The diseases range from tissue-specific to systemic and from genetic to sporadic. Some of the most devastating amyloidoses are those that affect the central nervous sy...

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Bibliographic Details
Corporate Author: SpringerLink (Online service)
Other Authors: Rahimi, Farid (Editor), Bitan, Gal (Editor)
Format: Electronic eBook
Language:English
Published: Dordrecht : Springer Netherlands, 2012.
Subjects:
Online Access:Full Text via HEAL-Link
Table of Contents:
  • 1. Overview of Fibrillar and Oligomeric Assemblies of Amyloidogenic Proteins
  • 2. Pathologic Lesions in Alzheimer disease and Other Neurodegenerative Diseases—Cellular and Molecular Components
  • 3. Preparation and Structural Characterization of Pre-fibrillar Assemblies of Amyloidogenic Proteins
  • 4. Biological Targeting and Activity of Pre-fibrillar Aβ Assemblies
  • 5. The Role of Aβ and Tau Oligomers in the Pathogenesis of Alzheimer’s disease
  • 6. Oligomers of α-Synuclein in the Pathogenesis of Parkinson’s Disease
  • 7. Cytotoxic Mechanisms of Islet Amyloid Polypeptide in the Pathogenesis of Type-2 Diabetes Mellitus (T2DM)
  • 8. Protein Misfolding and Toxicity in Amyotrophic Lateral Sclerosis
  • 9. Structural Studies of Prion Proteins and Prions
  • 10. Role of Prion Protein Oligomers in the Pathogenesis of Transmissible Spongiform Encephalopathies
  • 11. When More Is Not Better: Expanded Polyglutamine Domains in Neurodegenerative Disease
  • 12. Protein Misfolding and Toxicity in Dialysis-Related Amyloidosis
  • 13. Transthyretin Aggregation and Toxicity
  • 14. Strategies for Inhibiting Protein Aggregation: Therapeutic Approaches to Protein-Aggregation Diseases.