19 Citations (Scopus)

Abstract

The aggregation of a soluble protein into insoluble, beta-sheet rich amyloid fibrils is a defining characteristic of many neurodegenerative diseases, including prion disorders. The prion protein has so far been considered unique because of its infectious nature. Recent investigations, however, suggest that other amyloid-forming proteins associated with much more common diseases, such as tau, alpha-synuclein, amyloid beta and polyglutamine proteins, while not infectious in the classical sense, share certain essential properties with prions that may explain phenotypic diversity, and patterns of spread within the nervous system. We suggest a common mechanism of pathogenesis of myriad sporadic and inherited neurodegenerative diseases based on templated conformational change.

Original languageEnglish (US)
Pages (from-to)74-77
Number of pages4
JournalPrion
Volume3
Issue number2
StatePublished - Apr 2009

Fingerprint

Neurodegenerative diseases
Prions
Amyloid
Neurodegenerative Diseases
Amyloidogenic Proteins
alpha-Synuclein
Amyloid beta-Peptides
Nervous System
Proteins
Neurology
Agglomeration
beta-Strand Protein Conformation
polyglutamine
Prion Proteins

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Infectious Diseases
  • Cellular and Molecular Neuroscience

Cite this

The expanding realm of prion phenomena in neurodegenerative disease. / Frost, Bess; Diamond, Marc I.

In: Prion, Vol. 3, No. 2, 04.2009, p. 74-77.

Research output: Contribution to journalArticle

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