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    In this issue of Structure, van der Kant and colleagues use a computational approach to uncover what dictates assembly of proteins into amyloid fibrils. Structurally distinct amyloids have about 30% of their residues predisposed to cross-β conformation, while less favorable regions may be the source of polymorphism by interacting with stabilizing cofactors. Copyright © 2022 Elsevier Ltd. All rights reserved.


    Lukasz A Joachimiak. The interactions that shape amyloid fibrils in disease. Structure (London, England : 1993). 2022 Aug 04;30(8):1045-1047

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    PMID: 35931058

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