Amelioration of aggregate cytotoxicity by catalytic conversion of protein oligomers into amyloid fibrils-Reference-Cited by-同舟云学术

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Amelioration of aggregate cytotoxicity by catalytic conversion of protein oligomers into amyloid fibrils

Published:2020 Issue:36 Volume:12 Page:18663-18672
ISSN:2040-3364
Container-title:Nanoscale
language:en
Short-container-title:Nanoscale

Author:

Yang Jie¹²³⁴⁵,Dear Alexander J.⁶⁷⁸⁹¹⁰^ORCID,Yao Qiong-Qiong¹²³⁴⁵^ORCID,Liu Zhenyan¹²³⁴⁵,Dobson Christopher M.⁶⁷⁸⁹¹⁰,Knowles Tuomas P. J.⁶⁷⁸⁹¹⁰^ORCID,Wu Si¹²³⁴⁵^ORCID,Perrett Sarah¹²³⁴⁵^ORCID

Affiliation:

1. National Laboratory of Biomacromolecules

2. CAS Center for Excellence in Biomacromolecules

3. Institute of Biophysics

4. Chinese Academy of Sciences

5. Chaoyang District

6. Centre for Misfolding Diseases

7. Department of Chemistry

8. University of Cambridge

9. Cambridge CB2 1EW

10. UK

Abstract

Peptide vesicles catalyze conversion of toxic amyloid oligomers into benign fibrillar species.

Funder

National Natural Science Foundation of China

National Laboratory of Biomacromolecules

Ministry of Science and Technology of the People's Republic of China

Publisher

Royal Society of Chemistry (RSC)

Subject

General Materials Science

Link

http://pubs.rsc.org/en/content/articlepdf/2020/NR/D0NR01481H

Reference56 articles.

1. Functional amyloid – from bacteria to humans

2. The amyloid state and its association with protein misfolding diseases

3. Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade

4. From Macroscopic Measurements to Microscopic Mechanisms of Protein Aggregation

5. Nucleated polymerization with secondary pathways. I. Time evolution of the principal moments

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