Back to Search Start Over

Structure and Polymorphism of Amyloid and Amyloid-Like Aggregates.

Authors :
Matiiv, Anton B.
Trubitsina, Nina P.
Matveenko, Andrew G.
Barbitoff, Yury A.
Zhouravleva, Galina A.
Bondarev, Stanislav A.
Source :
Biochemistry (00062979). May2022, Vol. 87 Issue 5, p450-463. 14p.
Publication Year :
2022

Abstract

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. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
00062979
Volume :
87
Issue :
5
Database :
Academic Search Index
Journal :
Biochemistry (00062979)
Publication Type :
Academic Journal
Accession number :
156861256
Full Text :
https://doi.org/10.1134/S0006297922050066