4.6 Editorial Material

Protein Amyloid Cofactors: Charged Side-Chain Arrays Meet Their Match?

Journal

TRENDS IN BIOCHEMICAL SCIENCES
Volume 46, Issue 8, Pages 626-629

Publisher

CELL PRESS
DOI: 10.1016/j.tibs.2021.05.003

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Funding

  1. National Institutes of Health (NIH) [GM067260, GM135158]

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Recent high-resolution structural studies have revealed parallel in-register cross-beta-sheets with periodic arrays of closely spaced identical residues in protein amyloids, shedding light on the mechanisms of common amyloid-promoting factors.
Recent advances in high-resolution structural studies of protein amyloids have revealed parallel in-register cross-beta-sheets with periodic arrays of closely spaced identical residues. What do these structures tell us about the mechanisms of action of common amyloid-promoting factors, such as heparan sulfate (HS), nucleic acids, polyphosphates, anionic phospholipids, and acidic pH?

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