The interactions that shape amyloid fibrils in disease

Lukasz A. Joachimiak

doi:10.1016/j.str.2022.07.003

The interactions that shape amyloid fibrils in disease

Research output: Contribution to journal › Comment/debate › peer-review

Abstract

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.

Original language	English (US)
Pages (from-to)	1045-1047
Number of pages	3
Journal	Structure
Volume	30
Issue number	8
DOIs	https://doi.org/10.1016/j.str.2022.07.003
State	Published - Aug 4 2022

ASJC Scopus subject areas

Structural Biology
Molecular Biology

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10.1016/j.str.2022.07.003

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abstract = "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.",

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The interactions that shape amyloid fibrils in disease

Abstract

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