Mechanism of Secondary Nucleation at the Single Fibril Level from Direct Observations of Aβ42 Aggregation-Reference-Cited by-同舟云学术

Mechanism of Secondary Nucleation at the Single Fibril Level from Direct Observations of Aβ42 Aggregation

Published:2021-09-28 Issue:40 Volume:143 Page:16621-16629
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Zimmermann Manuela R.¹^ORCID,Bera Subhas C.²³^ORCID,Meisl Georg¹^ORCID,Dasadhikari Sourav²,Ghosh Shamasree²,Linse Sara⁴^ORCID,Garai Kanchan²,Knowles Tuomas P. J.¹⁵^ORCID

Affiliation:

1. Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, CB2 1EW Cambridge, United Kingdom

2. TIFR Centre for Interdisciplinary Sciences, 500046 Hyderabad, India

3. Interdisciplinary Center for Clinical Research, Friedrich-Alexander-University, Erlangen-Nürnberg (FAU), 91058 Erlangen, Germany

4. Department of Chemistry, Division for Biochemistry and Structural Biology, Lund University, 221 00 Lund, Sweden

5. Cavendish Laboratory, University of Cambridge, CB3 0HE Cambridge, United Kingdom

Funder

Vetenskapsr??det

Department of Atomic Energy, Government of India

Science and Engineering Research Board

Frances and Augustus Newman Foundation

H2020 European Research Council

Herchel Smith Fund

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/jacs.1c07228

Reference43 articles.

1. Protein Misfolding, Functional Amyloid, and Human Disease

2. Dynamics of oligomer populations formed during the aggregation of Alzheimer’s Aβ42 peptide

3. Proliferation of amyloid- 42 aggregates occurs through a secondary nucleation mechanism

4. Kinetic fingerprints differentiate the mechanisms of action of anti-Aβ antibodies

5. Thermodynamic and kinetic design principles for amyloid-aggregation inhibitors

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