Origin of metastable oligomers and their effects on amyloid fibril self-assembly-Reference-Cited by-同舟云学术

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Origin of metastable oligomers and their effects on amyloid fibril self-assembly

Published:2018 Issue:27 Volume:9 Page:5937-5948
ISSN:2041-6520
Container-title:Chemical Science
language:en
Short-container-title:Chem. Sci.

Author:

Hasecke Filip¹²³⁴,Miti Tatiana⁵⁶⁷⁸,Perez Carlos⁵⁶⁷⁸,Barton Jeremy⁵⁶⁷⁸,Schölzel Daniel¹²³⁴⁹,Gremer Lothar¹²³⁴⁹^ORCID,Grüning Clara S. R.¹²³⁴,Matthews Garrett⁵⁶⁷⁸,Meisl Georg¹⁰¹¹¹²¹³^ORCID,Knowles Tuomas P. J.¹⁰¹¹¹²¹³^ORCID,Willbold Dieter¹²³⁴⁹^ORCID,Neudecker Philipp¹²³⁴⁹^ORCID,Heise Henrike¹²³⁴⁹^ORCID,Ullah Ghanim⁵⁶⁷⁸,Hoyer Wolfgang¹²³⁴⁹^ORCID,Muschol Martin⁵⁶⁷⁸^ORCID

Affiliation:

1. Institut für Physikalische Biologie

2. Heinrich-Heine-Universität

3. 40204 Düsseldorf

4. Germany

5. Department of Physics

6. University of South Florida

7. Tampa

8. USA

9. Institute of Complex Systems (ICS-6)

10. Department of Chemistry

11. University of Cambridge

12. Cambridge CB2 1EW

13. UK

Abstract

Simultaneous analysis of oligomer and fibril assembly kinetics reveals inhibitory effects of metastable oligomers on amyloid fibril formation.

Funder

National Institutes of Health

H2020 European Research Council

Sidney Sussex College, University of Cambridge

Alzheimer Forschung Initiative

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2018/SC/C8SC01479E

Reference100 articles.

1. Amyloid diseases: Abnormal protein aggregation in neurodegeneration

2. Protein aggregation and neurodegenerative disease

3. Protein Misfolding, Functional Amyloid, and Human Disease

4. Protein misfolding and aggregation: new examples in medicine and biology of the dark side of the protein world

5. From the globular to the fibrous state: protein structure and structural conversion in amyloid formation

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