Polyphenol‐solubility alters amyloid fibril formation of α‐synuclein-Reference-Cited by-同舟云学术

Polyphenol‐solubility alters amyloid fibril formation of α‐synuclein

Published:2021-06-02 Issue:8 Volume:30 Page:1701-1713
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

So Masatomo¹²^ORCID,Kimura Yuto¹,Yamaguchi Keiichi¹³,Sugiki Toshihiko¹,Fujiwara Toshimichi¹,Aguirre Cesar¹⁴,Ikenaka Kensuke⁴,Mochizuki Hideki⁴,Kawata Yasushi⁵,Goto Yuji¹³^ORCID

Affiliation:

1. Institute for Protein Research Osaka University Osaka Japan

2. Astbury Centre for Structural Molecular Biology University of Leeds Leeds UK

3. Global Center for Medical Engineering and Informatics Osaka University Osaka Japan

4. Department of Neurology, Graduate School of Medicine Osaka University Osaka Japan

5. Department of Chemistry and Biotechnology, Graduate School of Engineering Tottori University Tottori Japan

Funder

Japan Society for the Promotion of Science

Ministry of Education, Culture, Sports, Science and Technology

Osaka University

Hokkaido University

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/pro.4130

Reference69 articles.

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

2. Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins

3. PASTA 2.0: an improved server for protein aggregation prediction

4. The CamSol Method of Rational Design of Protein Mutants with Enhanced Solubility

5. WALTZ-DB 2.0: an updated database containing structural information of experimentally determined amyloid-forming peptides

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