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Amyloids and protein aggregation

Linse, Sara LU and Knowles, Tuomas (2023) In Chemical Science 14(24). p.6491-6492
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.

Please use this url to cite or link to this publication:
author
and
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Chemical Science
volume
14
issue
24
pages
2 pages
publisher
Royal Society of Chemistry
external identifiers
  • pmid:37350828
  • scopus:85162261437
ISSN
2041-6520
DOI
10.1039/d2sc90225g
language
English
LU publication?
yes
id
310f9898-29e5-4587-ba4e-cf086a827659
date added to LUP
2023-09-18 13:38:53
date last changed
2024-04-19 01:18:30
@article{310f9898-29e5-4587-ba4e-cf086a827659,
  abstract     = {{<p>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.</p>}},
  author       = {{Linse, Sara and Knowles, Tuomas}},
  issn         = {{2041-6520}},
  language     = {{eng}},
  number       = {{24}},
  pages        = {{6491--6492}},
  publisher    = {{Royal Society of Chemistry}},
  series       = {{Chemical Science}},
  title        = {{Amyloids and protein aggregation}},
  url          = {{http://dx.doi.org/10.1039/d2sc90225g}},
  doi          = {{10.1039/d2sc90225g}},
  volume       = {{14}},
  year         = {{2023}},
}