Effects ofin vivoconditions on amyloid aggregation-Reference-Cited by-同舟云学术

Effects ofin vivoconditions on amyloid aggregation

Published:2019 Issue:14 Volume:48 Page:3946-3996
ISSN:0306-0012
Container-title:Chemical Society Reviews
language:en
Short-container-title:Chem. Soc. Rev.

Author:

Owen Michael C.¹²³⁴^ORCID,Gnutt David⁵⁶⁷⁸⁹^ORCID,Gao Mimi¹⁰¹¹¹²⁸¹³,Wärmländer Sebastian K. T. S.¹⁴¹⁵¹⁶¹⁷,Jarvet Jüri¹⁴¹⁵¹⁶¹⁷^ORCID,Gräslund Astrid¹⁴¹⁵¹⁶¹⁷^ORCID,Winter Roland¹⁰¹¹¹²⁸^ORCID,Ebbinghaus Simon⁵⁶⁷⁸^ORCID,Strodel Birgit¹⁸¹⁹⁸²⁰²¹^ORCID

Affiliation:

1. CEITEC – Central European Institute of Technology

2. Masaryk University

3. Brno 625 00

4. Czech Republic

5. Institute of Physical and Theoretical Chemistry

6. TU Braunschweig

7. 38106 Braunschweig

8. Germany

9. Lead Discovery Wuppertal

10. Faculty of Chemistry and Chemical Biology

11. TU Dortmund University

12. 44227 Dortmund

13. Sanofi-Aventis Deutschland GmbH, R&D

14. Department of Biochemistry and Biophysics

15. Stockholm University

16. 106 91 Stockholm

17. Sweden

18. Institute of Complex Systems: Structural Biochemistry

19. 42525 Jülich

20. Institute of Theoretical and Computational Chemistry, Heinrich Heine University Düsseldorf

21. 40225 Düsseldorf

Abstract

One of the grand challenges of biophysical chemistry is to understand the principles that govern protein aggregation leading to amyloid fibrils, which is a highly complex and sensitive process. This review provides a comprehensive overview of how amyloid aggregation is affected by the variousin vivoconstituents and conditions.

Funder

German-Israeli Foundation for Scientific Research and Development

Human Frontier Science Program

H2020 Marie Skłodowska-Curie Actions

Bundesministerium für Bildung und Forschung

Deutsche Forschungsgemeinschaft

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2019/CS/C8CS00034D