Art

J-GLOBAL ID：201802256340872041   Reference number：18A1369760

Protein Aggregation and its Suppression by Molecular Chaperone

蛋白質の凝集形成と分子シャペロンによる凝集抑制

Author (1)： KAWATA YASUSHI (鳥取大学大学院工学研究科化学・生物応用工学専攻, 医学系研究科機能再生医科学専攻)
Material： 日本白内障学会誌  (Journal of the Japanese Society for Cataract Research)
Volume： 30  Issue： 1  Page： 44-47(J-STAGE)  Publication year： 2018 
JST Material Number： L1720A  ISSN： 0915-4302  Document type： Article
Article type： 解説  Country of issue： Japan (JPN)  Language： JAPANESE (JA)

Thesaurus term： human ,...
Semi thesaurus term： *Amyloid beta ,...

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JST classification (2)： Proteins and peptides in general  (EB03010N) ,  Nervous system diseases  (GN03000O)

Substance index (1)： Delphinidin

Reference (4)：

• 1) Fukui N, Araki K, Hongo K et al: Modulating the effects of the bacterial chaperonin GroEL on fibrillogenic polypeptides through modification of domain hinge architecture. J Biol Chem 291: 25217-25226, 2016
• 2) Ojha B, Fukui N, Hongo K et al: Suppression of amyloid fibrils using the GroEL apical domain. Sci Rep 32: 433-440, 2016
• 3) Yamakawa MY, Uchino K, Watanabe Y et al: Anthocyanin suppresses the toxicity of Aβ deposits in in vitro and in vivo models of Alzheimer's disease. Nutr Neurosci 19: 32-42, 2015
• 4) Machida K, Fujiwara R, Tanaka T et al: Gly192 at hinge 2 site in the chaperonin GroEL plays a pivotal role in the dynamic apical domain movement that leads to GroES binding and efficient encapsulation of substrate proteins. Biochim Biophys Acta 1794: 1344-1354, 2009

Terms in the title (3)： 蛋白質 ,  凝集 ,  分子シャペロン