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The activities of amyloids from a structural perspective

Author

Listed:
  • Roland Riek

    (Laboratory of Physical Chemistry, ETH Zurich)

  • David S. Eisenberg

    (UCLA-DOE Institute
    Howard Hughes Medical Institute)

Abstract

The aggregation of proteins into structures known as amyloids is observed in many neurodegenerative diseases, including Alzheimer's disease. Amyloids are composed of pairs of tightly interacting, many stranded and repetitive intermolecular β-sheets, which form the cross-β-sheet structure. This structure enables amyloids to grow by recruitment of the same protein and its repetition can transform a weak biological activity into a potent one through cooperativity and avidity. Amyloids therefore have the potential to self-replicate and can adapt to the environment, yielding cell-to-cell transmissibility, prion infectivity and toxicity.

Suggested Citation

  • Roland Riek & David S. Eisenberg, 2016. "The activities of amyloids from a structural perspective," Nature, Nature, vol. 539(7628), pages 227-235, November.
    • Handle: RePEc:nat:nature:v:539:y:2016:i:7628:d:10.1038_nature20416
    DOI: 10.1038/nature20416
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    Cited by:

    1. Mohammad Peydayesh & Sabrina Kistler & Jiangtao Zhou & Viviane Lutz-Bueno & Francesca Damiani Victorelli & Andréia Bagliotti Meneguin & Larissa Spósito & Tais Maria Bauab & Marlus Chorilli & Raffaele , 2023. "Amyloid-polysaccharide interfacial coacervates as therapeutic materials," Nature Communications, Nature, vol. 14(1), pages 1-11, December.
    2. Nikolaos Louros & Meine Ramakers & Emiel Michiels & Katerina Konstantoulea & Chiara Morelli & Teresa Garcia & Nele Moonen & Sam D’Haeyer & Vera Goossens & Dietmar Rudolf Thal & Dominique Audenaert & F, 2022. "Mapping the sequence specificity of heterotypic amyloid interactions enables the identification of aggregation modifiers," Nature Communications, Nature, vol. 13(1), pages 1-20, December.

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