淀粉样蛋白(真菌学)
多态性(计算机科学)
淀粉样纤维
淀粉样β
淀粉样变性
β淀粉样蛋白
生物
遗传学
阿尔茨海默病
医学
基因型
病理
疾病
基因
作者
Anton B. Matiiv,Nina P. Trubitsina,Andrew G. Matveenko,Yury A. Barbitoff,Galina A. Zhouravleva,Stanislav A. Bondarev
出处
期刊:Biokhimiya
[Springer Nature]
日期:2022-05-01
卷期号:87 (5): 450-463
被引量:3
标识
DOI:10.1134/s0006297922050066
摘要
Amyloids are protein aggregates with the cross-β structure. The interest in amyloids is explained, on the one hand, by their role in the development of socially significant human neurodegenerative diseases, and on the other hand, by the discovery of functional amyloids, whose formation is an integral part of cellular processes. To date, more than a hundred proteins with the amyloid or amyloid-like properties have been identified. Studying the structure of amyloid aggregates has revealed a wide variety of protein conformations. In the review, we discuss the diversity of protein folds in the amyloid-like aggregates and the characteristic features of amyloid aggregates that determine their unusual properties, including stability and interaction with amyloid-specific dyes. The review also describes the diversity of amyloid aggregates and its significance for living organisms.
科研通智能强力驱动
Strongly Powered by AbleSci AI