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

  • Farid Rahimi
  • Gal Bitan

Table of contents

  1. Front Matter
    Pages i-viii
  2. Kyle C. Wilcox, Jason Pitt, Adriano Sebollela, Helen Martirosova, Pascale N. Lacor, William L. Klein
    Pages 103-133
  3. Dong-Pyo Hong, Wenbo Zhou, Aaron Santner, Vladimir N. Uversky
    Pages 189-216
  4. Theri Leica Degaki, Dahabada H. J. Lopes, Mari Cleide Sogayar
    Pages 217-255
  5. Aaron Kerman, Avijit Chakrabartty
    Pages 257-288
  6. Giuseppe Legname, Gabriele Giachin, Federico Benetti
    Pages 289-317
  7. Rodrigo Morales, Claudia A. Duran-Aniotz, Claudio Soto
    Pages 319-335
  8. Regina M. Murphy, Robert H. Walters, Matthew D. Tobelmann, Joseph P. Bernacki
    Pages 337-375
  9. John P. Hodkinson, Alison E. Ashcroft, Sheena E. Radford
    Pages 377-405
  10. Maria João Saraiva, Isabel Santos Cardoso
    Pages 407-432
  11. Back Matter
    Pages 561-565

About this book

Introduction

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 system (CNS), such as Alzheimer’s disease (AD), Parkinson’s disease (PD), prionoses (e.g., mad-cow disease), and amyotrophic lateral sclerosis (Lou Gehrig’s disease). In each disease, one or more proteins self-associate into toxic oligomers that disrupt cellular function and communication, and proceed to form insoluble amyloid aggregates characterized by fibrillar morphology and cross-β structure.

The first decade of the 21st century has brought with it significant progress in our understanding of amyloid diseases, including the physiological and pathological processes involving each of the offending proteins. Important developments also provide now improved diagnoses of different amyloidoses and new approaches are being developed towards disease-modifying therapies. This book covers the current state-of-the-art knowledge on amyloidoses as a general phenomenon and offers detailed reviews of individual amyloid-forming proteins and specific diseases.

Features:

  • Coverage of the pathologic and pathogenic structures of amyloidogenic proteins from the pathological lesions to the evasive oligomers that are believed to be the main culprits.
  • Detailed discussions of diseases of epidemic proportion, such as Alzheimer’s disease, Parkinson’s disease, and type-2 diabetes.
  • Current reviews of multiple diseases, including amyotrophic lateral sclerosis, prionoses, expanded polyglutamine diseases, dialysis-related amyloidosis, and transthyretin-related amyloidoses.
  • Mechanism-based strategies for inhibiting protein aggregation and potential therapeutic applications in different diseases.

Keywords

Amyloidogenic proteins Degenerative/neurodegenerative diseases Mechanisms of disease Non-fibrillar oligomeric assemblies Protein-misfolding diseases

Editors and affiliations

  • Farid Rahimi
    • 1
  • Gal Bitan
    • 2
  1. 1., Research School of BiologyAustralian National UniversityCanberraAustralia
  2. 2., NeurologyUniversity of California at Los AngelesLos AngelesUSA

Bibliographic information

  • DOI https://doi.org/10.1007/978-94-007-2774-8
  • Copyright Information Springer Science+Business Media B.V. 2012
  • Publisher Name Springer, Dordrecht
  • eBook Packages Biomedical and Life Sciences
  • Print ISBN 978-94-007-2773-1
  • Online ISBN 978-94-007-2774-8
  • About this book