Cross-Seeding of Fibrils from Two Types of Insulin Induces New Amyloid Strains-Reference-Cited by-同舟云学术

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Cross-Seeding of Fibrils from Two Types of Insulin Induces New Amyloid Strains

Published:2012-11-14 Issue:47 Volume:51 Page:9460-9469
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Surmacz-Chwedoruk Weronika¹²,Nieznańska Hanna³,Wójcik Sławomir⁴,Dzwolak Wojciech⁴

Affiliation:

1. Institute of Biotechnology and Antibiotics, Staroscinska 5, 02-516 Warsaw, Poland

2. Institute of High Pressure Physics, Polish Academy of Sciences, Sokolowska 29/37, 01-142 Warsaw, Poland

3. Nencki Institute of Experimental Biology, Polish Academy of Sciences, Pasteura 3, 02-093 Warsaw, Poland

4. Department of Chemistry, University of Warsaw, Pasteura 1, 02-093 Warsaw, Poland

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi301144d

Reference69 articles.

1. Protein Misfolding, Functional Amyloid, and Human Disease

2. The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation

3. The Common Architecture of Cross-β Amyloid

4. Principles that Govern the Folding of Protein Chains

5. Structural Insights into the Polymorphism of Amyloid-Like Fibrils Formed by Region 20−29 of Amylin Revealed by Solid-State NMR and X-ray Fiber Diffraction

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2. Amyloid oligomers and their membrane toxicity - A perspective study;Progress in Biophysics and Molecular Biology;2024-03

3. Acetone-induced structural variant of insulin amyloid fibrils;International Journal of Biological Macromolecules;2024-02

4. Insulin amyloidosis: A case report;Frontiers in Medicine;2023-04-06

5. Amyloid Protein Cross-Seeding Provides a New Perspective on Multiple Diseases In Vivo;Biomacromolecules;2022-12-12

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