Tracking the Structural Development of Amyloid Precursors in the Insulin B Chain and the Inhibition Effect by Fibrinogen-Reference-Cited by-同舟云学术

Tracking the Structural Development of Amyloid Precursors in the Insulin B Chain and the Inhibition Effect by Fibrinogen

Published:2022-12-19 Issue:51 Volume:126 Page:10797-10812
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Yamamoto Naoki¹^ORCID,Inoue Rintaro²,Makino Yoshiteru³,Sekiguchi Hiroshi⁴^ORCID,Shibayama Naoya¹^ORCID,Naito Akira³^ORCID,Sugiyama Masaaki²,Chatani Eri⁵^ORCID

Affiliation:

1. Division of Biophysics, Physiology, School of Medicine, Jichi Medical University, 3311-1 Yakushiji, Shimotsuke, Tochigi329-0498, Japan

2. Institute for Integrated Radiation and Nuclear Science, Kyoto University, 2 Asashiro-Nishi, Kumatori, Sennan-gun, Osaka590-0494, Japan

3. Graduate School of Engineering, Yokohama National University, 79-5 Tokiwadai, Hotogaya-ku, Yokohama240-8501, Japan

4. Japan Synchrotron Radiation Research Institute, 1-1-1, Koto, Sayo-cho, Sayo-gun, Hyogo679-5148, Japan

5. Graduate School of Science, Kobe University, 1-1 Rokkodai-cho, Nada-ku, Kobe657-8501, Japan

Funder

Takeda Science Foundation

Jichi Medical University

Japan Society for the Promotion of Science

Publisher

American Chemical Society (ACS)

Subject

Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jpcb.2c05136

Reference49 articles.

1. Protein folding and misfolding

2. The formation, function and regulation of amyloids: insights from structural biology

3. Recent progress on understanding the mechanisms of amyloid nucleation

4. Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade

5. Nucleated Conformational Conversion and the Replication of Conformational Information by a Prion Determinant

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