Issue 24, 2023

Amyloids and protein aggregation

Abstract

A general discovery in protein science in the past few decades has been the finding that a number of unrelated proteins and peptides all have a marked propensity to form amyloid fibrils in vivo and in vitro. These structures have become known as the pathological hallmark of some of the most prevalent neurodegenerative diseases. More recently, the process of amyloid formation has been demystified through a number of key mechanistic findings, some of which are highlighted in this themed collection.

Graphical abstract: Amyloids and protein aggregation

Article information

Article type
Editorial
First published
06 6 2023
This article is Open Access

All publication charges for this article have been paid for by the Royal Society of Chemistry
Creative Commons BY license

Chem. Sci., 2023,14, 6491-6492

Amyloids and protein aggregation

S. Linse and T. Knowles, Chem. Sci., 2023, 14, 6491 DOI: 10.1039/D2SC90225G

This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. You can use material from this article in other publications without requesting further permissions from the RSC, provided that the correct acknowledgement is given.

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