Research output: Contribution to journal › Review article › peer-review
Structure and Polymorphism of Amyloid and Amyloid-Like Aggregates. / Matiiv, Anton B.; Trubitsina, Nina P.; Matveenko, Andrew G.; Barbitoff, Yury A.; Zhouravleva, Galina A.; Bondarev, Stanislav A.
In: Biochemistry (Moscow), Vol. 87, No. 5, 05.2022, p. 450-463.Research output: Contribution to journal › Review article › peer-review
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TY - JOUR
T1 - Structure and Polymorphism of Amyloid and Amyloid-Like Aggregates
AU - Matiiv, Anton B.
AU - Trubitsina, Nina P.
AU - Matveenko, Andrew G.
AU - Barbitoff, Yury A.
AU - Zhouravleva, Galina A.
AU - Bondarev, Stanislav A.
N1 - Publisher Copyright: © 2022, Pleiades Publishing, Ltd.
PY - 2022/5
Y1 - 2022/5
N2 - 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.
AB - 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.
KW - amyloid polymorphism
KW - amyloid-like aggregates
KW - amyloids
KW - cross-β structure
KW - Amyloid/metabolism
KW - Amyloidosis/genetics
KW - Humans
KW - Protein Conformation
KW - Amyloidogenic Proteins
KW - Polymorphism, Genetic
UR - http://www.scopus.com/inward/record.url?scp=85132609247&partnerID=8YFLogxK
UR - https://www.mendeley.com/catalogue/368d4812-83d4-3992-8740-c7193b5fe8cb/
U2 - 10.1134/s0006297922050066
DO - 10.1134/s0006297922050066
M3 - Review article
C2 - 35790379
AN - SCOPUS:85132609247
VL - 87
SP - 450
EP - 463
JO - Biochemistry (Moscow)
JF - Biochemistry (Moscow)
SN - 0006-2979
IS - 5
ER -
ID: 97488764