Implications of peptide assemblies in amyloid diseases-Reference-Cited by-同舟云学术

Implications of peptide assemblies in amyloid diseases

Published:2017 Issue:21 Volume:46 Page:6492-6531
ISSN:0306-0012
Container-title:Chemical Society Reviews
language:en
Short-container-title:Chem. Soc. Rev.

Author:

Ke Pu Chun¹²³⁴⁵^ORCID,Sani Marc-Antonie⁶⁷⁸⁴⁵^ORCID,Ding Feng⁹¹⁰¹¹¹²^ORCID,Kakinen Aleksandr¹²³⁴⁵^ORCID,Javed Ibrahim¹²³⁴⁵^ORCID,Separovic Frances⁶⁷⁸⁴⁵^ORCID,Davis Thomas P.¹²³⁴⁵^ORCID,Mezzenga Raffaele¹³¹⁴¹⁵¹⁶^ORCID

Affiliation:

1. ARC Center of Excellence in Convergent Bio-Nano Science and Technology

2. Monash Institute of Pharmaceutical Sciences

3. Monash University

4. Parkville

5. Australia

6. School of Chemistry

7. Bio21 Institute

8. The University of Melbourne

9. Department of Physics and Astronomy

10. Clemson University

11. Clemson

12. USA

13. ETH Zurich

14. Department of Health Science & Technology

15. 8092 Zurich

16. Switzerland

Abstract

We highlight the role of molecular self-assembly in eliciting the mesoscopic and pathological properties of amyloid proteins. This knowledge is pivotal for the development of theranostics against amyloid diseases.

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2017/CS/C7CS00372B

Reference524 articles.

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5. Designing conditions for in vitro formation of amyloid protofilaments and fibrils

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