Skip to main content
SpringerLink
Log in
Book cover

Proteopathic Seeds and Neurodegenerative Diseases

  • Book
  • © 2013

Overview

Editors:
  1. Mathias Jucker

    1. , Dept. Cellular Neurology, University of Tübingen, Tübingen, Germany

    View editor publications

    You can also search for this editor in PubMed   Google Scholar

  2. Yves Christen

    1. Fondation IPSEN, Boulogne-Billancourt Cedex, France

    View editor publications

    You can also search for this editor in PubMed   Google Scholar

  • With contributions from nobel laureats Eric Kandel and Stanley Prusiner
  • Latest research on prion diseases
  • Presents developing therapies ?
  • Includes supplementary material: sn.pub/extras

Part of the book series: Research and Perspectives in Alzheimer's Disease (ALZHEIMER)

This is a preview of subscription content, log in via an institution to check access.

Access this book

Log in via an institution
eBook USD 129.00
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book USD 169.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book USD 169.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Other ways to access

Licence this eBook for your library

Institutional subscriptions

Table of contents (11 chapters)

  1. Front Matter

    Pages i-xi
    Download chapter PDF

  2. Widening Spectrum of Prions Causing Neurodegenerative Diseases

    • Stanley B. Prusiner
    Pages 1-17

  3. β-Amyloid Fibril Structures, In Vitro and In Vivo

    • Robert Tycko
    Pages 19-31

  4. Structure-Activity Relationship of Amyloids

    • Jason Greenwald, Roland Riek
    Pages 33-46

  5. Seeding and Cross-seeding in Amyloid Diseases

    • Per Westermark, Gunilla T. Westermark
    Pages 47-60

  6. The Prion-Like Aspect of Alzheimer Pathology

    • Sarah K. Fritschi, Bahareh Eftekharzadeh, Giusi Manfredi, Tsuyoshi Hamaguchi, Götz Heilbronner, Amudha Nagarathinam et al.
    Pages 61-69

  7. Amyloid-β Transmissibility

    • C. Duran-Aniotz, R. Morales, I. Moreno-Gonzalez, C. Soto
    Pages 71-86

  8. Prion-Like Properties of Assembled Tau Protein

    • Florence Clavaguera, Markus Tolnay, Michel Goedert
    Pages 87-95

  9. Accumulating Evidence Suggests that Parkinson’s Disease Is a Prion-Like Disorder

    • Nolwen L. Rey, Elodie Angot, Christopher Dunning, Jennifer A. Steiner, Patrik Brundin
    Pages 97-113

  10. Propagation and Replication of Misfolded SOD1: Implications for Amyotrophic Lateral Sclerosis

    • Anne Bertolotti
    Pages 115-122

  11. Development of Drugs That Target Proteopathic Seeds Will Require Measurement of Drug Mechanism in Human Brain

    • Peter T. Lansbury Jr
    Pages 123-130

  12. The Role of Functional Prions in the Persistence of Memory Storage

    • Eric R. Kandel, Irina Derkatch, Elias Pavlopoulos
    Pages 131-152

  13. Back Matter

    Pages 153-155
    Download chapter PDF
Back to top

Keywords

About this book

The misfolding and aggregation of specific proteins is an early and obligatory event in many of the age-related neurodegenerative diseases of humans. The initial cause of this pathogenic cascade and the means whereby disease spreads through the nervous system, remain uncertain. A recent surge of research, first instigated by pathologic similarities between prion disease and Alzheimer’s disease, increasingly implicates the conversion of disease-specific proteins into an aggregate-prone b-sheet-rich state as the prime mover of the neurodegenerative process. This prion-like corruptive protein templating or seeding now characterizes such clinically and etiologically diverse neurological disorders as Alzheimer´s disease, Parkinson’s disease, Huntington’s disease, amyotrophic lateral sclerosis, and frontotemporal lobar degeneration. Understanding the misfolding, aggregation, trafficking and pathogenicity of the affected proteins could therefore reveal universal pathomechanistic principles for some of the most devastating and intractable human brain disorders. It is time to accept that the prion concept is no longer confined to prionoses but is a promising concept for the understanding and treatment of a remarkable variety of diseases that afflict primarily our aging society. ​

Editors and Affiliations

  • , Dept. Cellular Neurology, University of Tübingen, Tübingen, Germany

    Mathias Jucker

  • Fondation IPSEN, Boulogne-Billancourt Cedex, France

    Yves Christen

Bibliographic Information

Publish with us

Policies and ethics

Back to top

Search

Navigation