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

  • Book
  • © 2012

Overview

Editors:
  1. Farid Rahimi

    1. , Research School of Biology, Australian National University, Canberra, Australia

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    You can also search for this editor in PubMed   Google Scholar

  2. Gal Bitan

    1. , Neurology, University of California at Los Angeles, Los Angeles, USA

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    You can also search for this editor in PubMed   Google Scholar

  • An up-to-date review of protein-misfolding diseases which will serve as a complete reference point for readers
  • Up-to-date chapters that discuss different diseases associated with protein misfolding and neurodegeneration
  • A good reference collection for a broad spectrum of readers

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Table of contents (14 chapters)

  1. Front Matter

    Pages i-viii
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  2. Overview of Fibrillar and Oligomeric Assemblies of Amyloidogenic Proteins

    • Farid Rahimi, Gal Bitan
    Pages 1-36

  3. Pathologic Lesions in Alzheimer Disease and Other Neurodegenerative Diseases—Cellular and Molecular Components

    • Harry V. Vinters, Spencer Tung, Orestes E. Solis
    Pages 37-60

  4. Preparation and Structural Characterization of Pre-fibrillar Assemblies of Amyloidogenic Proteins

    • Anat Frydman-Marom, Yaron Bram, Ehud Gazit
    Pages 61-102

  5. Biological Targeting and Activity of Pre-fibrillar Aβ Assemblies

    • Kyle C. Wilcox, Jason Pitt, Adriano Sebollela, Helen Martirosova, Pascale N. Lacor, William L. Klein
    Pages 103-133

  6. The Role of Aβ and Tau Oligomers in the Pathogenesis of Alzheimer’s Disease

    • Kiran Bhaskar, Bruce T. Lamb
    Pages 135-188

  7. Oligomers of α-Synuclein in the Pathogenesis of Parkinson’s Disease

    • Dong-Pyo Hong, Wenbo Zhou, Aaron Santner, Vladimir N. Uversky
    Pages 189-216

  8. Cytotoxic Mechanisms of Islet Amyloid Polypeptide in the Pathogenesis of Type-2 Diabetes Mellitus (T2DM)

    • Theri Leica Degaki, Dahabada H. J. Lopes, Mari Cleide Sogayar
    Pages 217-255

  9. Protein Misfolding and Toxicity in Amyotrophic Lateral Sclerosis

    • Aaron Kerman, Avijit Chakrabartty
    Pages 257-288

  10. Structural Studies of Prion Proteins and Prions

    • Giuseppe Legname, Gabriele Giachin, Federico Benetti
    Pages 289-317

  11. Role of Prion Protein Oligomers in the Pathogenesis of Transmissible Spongiform Encephalopathies

    • Rodrigo Morales, Claudia A. Duran-Aniotz, Claudio Soto
    Pages 319-335

  12. When More Is Not Better: Expanded Polyglutamine Domains in Neurodegenerative Disease

    • Regina M. Murphy, Robert H. Walters, Matthew D. Tobelmann, Joseph P. Bernacki
    Pages 337-375

  13. Protein Misfolding and Toxicity in Dialysis-Related Amyloidosis

    • John P. Hodkinson, Alison E. Ashcroft, Sheena E. Radford
    Pages 377-405

  14. Transthyretin Aggregation and Toxicity

    • Maria João Saraiva, Isabel Santos Cardoso
    Pages 407-432

  15. Strategies for Inhibiting Protein Aggregation: Therapeutic Approaches to Protein-Aggregation Diseases

    • Jennifer D. Lanning, Stephen C. Meredith
    Pages 433-560

  16. Back Matter

    Pages 561-565
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Keywords

About this book

Amyloid-forming proteins are implicated in over 30 human diseases. The proteins involved in each disease have unrelated sequences and dissimilar native structures, but they all undergo conformational alterations to form fibrillar polymers. The fibrillar assemblies accumulate progressively into disease-specific lesions in vivo. Substantial evidence suggests these lesions are the end state of aberrant protein folding whereas the actual disease-causing culprits likely are soluble, non-fibrillar assemblies preceding the aggregates. The non-fibrillar protein assemblies range from small, low-order oligomers to spherical, annular, and protofibrillar species. Oligomeric species are believed to mediate various pathogenic mechanisms that lead to cellular dysfunction, cytotoxicity, and cell loss, eventuating in disease-specific degeneration and systemic morbidity. The particular pathologies thus are determined by the afflicted cell types, organs, systems, and the proteins involved. Evidence suggests that the oligomeric species may share structural features and possibly common mechanisms of action. In many cases, the structure–function interrelationships amongst the various protein assemblies described in vitro are still elusive. Deciphering these intricate structure–function correlations will help understanding a complex array of pathogenic mechanisms, some of which may be common across different diseases albeit affecting different cell types and systems.

Editors and Affiliations

  • , Research School of Biology, Australian National University, Canberra, Australia

    Farid Rahimi

  • , Neurology, University of California at Los Angeles, Los Angeles, USA

    Gal Bitan

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