Influences of amino-terminal modifications on amyloid fibril formation of human serum amyloid A-Reference-Cited by-同舟云学术

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Influences of amino-terminal modifications on amyloid fibril formation of human serum amyloid A

Published:2023-07 Issue: Volume:742 Page:109615
ISSN:0003-9861
Container-title:Archives of Biochemistry and Biophysics
language:en
Short-container-title:Archives of Biochemistry and Biophysics

Author:

Tanaka Masafumi,Takarada Toru,Nadanaka Satomi,Kojima Risa,Hosoi Kimiko,Machiba Yuki,Kitagawa Hiroshi,Yamada Toshiyuki

Funder

Japan Society for the Promotion of Science

Promotion and Mutual Aid Corporation for Private Schools of Japan

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics

Reference39 articles.

1. Amyloid fibril proteins and amyloidosis: chemical identification and clinical classification International Society of Amyloidosis 2016 Nomenclature Guidelines;Sipe;Amyloid,2016

2. AA amyloidosis: pathogenesis and targeted therapy;Westermark;Annu. Rev. Pathol.,2015

3. The N-terminal segment of protein AA determines its fibrillogenic property;Westermark;Biochem. Biophys. Res. Commun.,1992

4. Plasma protein carbamylation and decreased acidic drug protein binding in uremia;Erill;Clin. Pharmacol. Ther.,1980

5. Protein carbamylation links inflammation, smoking, uremia and atherogenesis;Wang;Nat. Med.,2007

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4. Study on Interaction with High-Abundant Blood Proteins and Identification of Low-Abundant Proteins to 5-Phenyl-1-(P-Tolyl)-1h-1,2,3-Triazole by Serum Proteomics;2024

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