Visualizing and trapping transient oligomers in amyloid assembly pathways-Reference-Cited by-同舟云学术

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Visualizing and trapping transient oligomers in amyloid assembly pathways

Published:2021-01 Issue: Volume:268 Page:106505
ISSN:0301-4622
Container-title:Biophysical Chemistry
language:en
Short-container-title:Biophysical Chemistry

Author:

Cawood Emma E.,Karamanos Theodoros K.,Wilson Andrew J.,Radford Sheena E.

Funder

European Research Council

Engineering and Physical Sciences Research Council

Leverhulme Trust

Wellcome Trust

Publisher

Elsevier BV

Subject

Organic Chemistry,Biochemistry,Biophysics

Reference259 articles.

1. Protein misfolding, amyloid formation, and human disease: a summary of progress over the last decade;Chiti;Annu. Rev. Biochem.,2017

2. A new era for understanding amyloid structures and disease;Iadanza;Nat. Rev. Mol. Cell Biol.,2018

3. Why are functional amyloids non-toxic in humans?;Jackson;Biomolecules,2017

4. Spot the difference: function versus toxicity in amyloid fibrils;Ulamec;Trends Biochem. Sci.,2020

5. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases;Bucciantini;Nature,2002

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