Journal
NATURE
Volume 539, Issue 7628, Pages 227-235Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nature20416
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Funding
- Swiss National Science Foundation (SNSF)
- US National Institutes of Health
- Howard Hughes Medical Institute
- SNSF Sinergia grant
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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 beta-sheets, which form the cross-beta-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.
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