Secondary nucleation in amyloid formation-Reference-Cited by-同舟云学术

Secondary nucleation in amyloid formation

Published:2018 Issue:63 Volume:54 Page:8667-8684
ISSN:1359-7345
Container-title:Chemical Communications
language:en
Short-container-title:Chem. Commun.

Author:

Törnquist Mattias¹²³⁴⁵^ORCID,Michaels Thomas C. T.⁶⁷⁸⁹¹⁰,Sanagavarapu Kalyani¹²³⁴⁵^ORCID,Yang Xiaoting¹²³⁴⁵^ORCID,Meisl Georg⁶⁷⁸⁹^ORCID,Cohen Samuel I. A.⁶⁷⁸⁹,Knowles Tuomas P. J.⁶⁷⁸⁹⁶^ORCID,Linse Sara¹²³⁴⁵^ORCID

Affiliation:

1. Lund University

2. Department of Biochemistry and Structural Biology

3. Chemical Centre

4. SE221 00 Lund

5. Sweden

6. Cambridge University

7. Department of Chemistry

8. Cambridge

9. UK

10. Paulson School of Engineering and Applied Sciences

Abstract

Nucleation of new peptide and protein aggregates on the surfaces of amyloid fibrils of the same peptide or protein has emerged in the past two decades as a major pathway for both the generation of molecular species responsible for cellular toxicity and for the autocatalytic proliferation of peptide and protein aggregates.

Funder

Alzheimerfonden

European Research Council

Vetenskapsrådet

Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung

Sidney Sussex College, University of Cambridge

Publisher

Royal Society of Chemistry (RSC)

Subject

Materials Chemistry,Metals and Alloys,Surfaces, Coatings and Films,General Chemistry,Ceramics and Composites,Electronic, Optical and Magnetic Materials,Catalysis

Link

http://pubs.rsc.org/en/content/articlepdf/2018/CC/C8CC02204F

Reference176 articles.

1. Atomic Resolution Structure of Monomorphic Aβ42 Amyloid Fibrils

2. Protein Misfolding, Functional Amyloid, and Human Disease

3. The Amyloid State of Proteins in Human Diseases

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

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