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Mammalian prions and their wider relevance in neurodegenerative diseases

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  • John Collinge

    (Medical Research Council Prion Unit, University College London Institute of Neurology
    University College London Institute of Neurology)

Abstract

Prions are notorious protein-only infectious agents that cause invariably fatal brain diseases following silent incubation periods that can span a lifetime. These diseases can arise spontaneously, through infection or be inherited. Remarkably, prions are composed of self-propagating assemblies of a misfolded cellular protein that encode information, generate neurotoxicity and evolve and adapt in vivo. Although parallels have been drawn with Alzheimer's disease and other neurodegenerative conditions involving the deposition of assemblies of misfolded proteins in the brain, insights are now being provided into the usefulness and limitations of prion analogies and their aetiological and therapeutic relevance.

Suggested Citation

  • John Collinge, 2016. "Mammalian prions and their wider relevance in neurodegenerative diseases," Nature, Nature, vol. 539(7628), pages 217-226, November.
    • Handle: RePEc:nat:nature:v:539:y:2016:i:7628:d:10.1038_nature20415
    DOI: 10.1038/nature20415
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    Cited by:

    1. Szymon W. Manka & Wenjuan Zhang & Adam Wenborn & Jemma Betts & Susan Joiner & Helen R. Saibil & John Collinge & Jonathan D. F. Wadsworth, 2022. "2.7 Å cryo-EM structure of ex vivo RML prion fibrils," Nature Communications, Nature, vol. 13(1), pages 1-11, December.
    2. Christine Rother & Ruth E. Uhlmann & Stephan A. Müller & Juliane Schelle & Angelos Skodras & Ulrike Obermüller & Lisa M. Häsler & Marius Lambert & Frank Baumann & Ying Xu & Carina Bergmann & Giulia Sa, 2022. "Experimental evidence for temporal uncoupling of brain Aβ deposition and neurodegenerative sequelae," Nature Communications, Nature, vol. 13(1), pages 1-11, December.

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