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Methods for Studying Prion Protein Amyloid

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Prion Diseases

Part of the book series: Methods in Molecular Medicine ((MIMM,volume 3))

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Abstract

Prion encephalopathies are neurodegenerative diseases characterized by the accumulation of abnormal isoforms of the prion protein (PrP) and the deposition of PrP amyloid in the central nervous systein (CNS) (1, 2) The diseasespecific PrP molecules are distinguishable froin their normal homologs by their relative resistance to proteinase K digestion (1, 2), they are thought to be derived from protease-sensitive precursors by a posttranslational process that involves a conformational change with a shift from α-helix to β-sheet structure (3–5)

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Author information

Authors and Affiliations

  1. Istituto Nazionale Neurologico Carlo Besta, Milano, Italy

    Fabrizio Tagliavini, Giorgio Giaccone & Orso Bugiani

  2. Department of Pathology, New York University Medical Center, New York, NY

    Frances Prelli

  3. Istituto di Ricerche Farmacologiche Mario Negri, Milano, Italy

    Gianluigi Forloni & Mario Salmona

  4. Department of Pathology, Indiana University School of Medicine, Indianapolis, IN

    Pedro Piccardo & Bernardino Ghetti

Authors
  1. Fabrizio Tagliavini
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  2. Frances Prelli
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  3. Giorgio Giaccone
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  4. Gianluigi Forloni
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  5. Mario Salmona
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  6. Pedro Piccardo
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  7. Bernardino Ghetti
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  8. Blas Frangione
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  9. Orso Bugiani
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Editor information

Editors and Affiliations

  1. Cambridge University, Cambridge, UK

    Harry F. Baker  & Rosalind M. Ridley  & 

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© 1996 Humana Press Inc., Totowa, NJ

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Tagliavini, F. et al. (1996). Methods for Studying Prion Protein Amyloid. In: Baker, H.F., Ridley, R.M. (eds) Prion Diseases. Methods in Molecular Medicine, vol 3. Springer, Totowa, NJ. https://doi.org/10.1385/0-89603-342-2:265

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  • DOI: https://doi.org/10.1385/0-89603-342-2:265

  • Publisher Name: Springer, Totowa, NJ

  • Print ISBN: 978-0-89603-342-9

  • Online ISBN: 978-1-59259-587-7

  • eBook Packages: Springer Protocols

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