Energy landscape of polymorphic amyloid generation of β2-microglobulin revealed by calorimetry-Reference-Cited by-同舟云学术

Energy landscape of polymorphic amyloid generation of β2-microglobulin revealed by calorimetry

Published:2018 Issue:57 Volume:54 Page:7995-7998
ISSN:1359-7345
Container-title:Chemical Communications
language:en
Short-container-title:Chem. Commun.

Author:

Kinoshita Misaki¹²³⁴,Lin Yuxi⁵⁶⁷⁸,Dai Itoh¹²³⁴,Okumura Masaki⁹¹⁰¹¹⁴,Markova Natalia¹²¹³¹⁴,Ladbury John E.¹⁵¹⁶¹⁷¹⁸,Sterpone Fabio¹⁹²⁰²¹²²²³,Lee Young-Ho¹²³⁴^ORCID

Affiliation:

1. Institute for Protein research

2. Osaka University

3. Suita

4. Japan

5. Department of Chemistry

6. Sookmyung Women's University

7. Seoul

8. Korea

9. Frontier Research Institute for Interdisciplinary Sciences (FRIS)

10. Tohoku University

11. Sendai 980-8578

12. Malvern Panalytical

13. Northampton

14. USA

15. School of Molecular and Cellular Biology

16. University of Leeds

17. Leeds

18. UK

19. CNRS Laboratoire de Biochimie Théorique

20. Institut de Biologie Physico-Chimique

21. Université Paris Denis Diderot

22. Sorbonne Paris Cité

23. PSL Research University

Abstract

ITC-based energy landscape provides a comprehensive understanding of amyloid aggregation in terms of thermodynamics and kinetics.

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/C8CC02718H

Reference14 articles.

1. Structural Studies of Amyloid Proteins at the Molecular Level

2. Heat of supersaturation-limited amyloid burst directly monitored by isothermal titration calorimetry

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

4. Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology

5. Calorimetry as a tool for understanding biomolecular interactions and an aid to drug design

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