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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.

в: Biochemistry (Moscow), Том 87, № 5, 05.2022, стр. 450-463.

Результаты исследований: Научные публикации в периодических изданиях › Обзорная статья › Рецензирование

Harvard

Matiiv, AB, Trubitsina, NP, Matveenko, AG, Barbitoff, YA, Zhouravleva, GA & Bondarev, SA 2022, 'Structure and Polymorphism of Amyloid and Amyloid-Like Aggregates', Biochemistry (Moscow), Том. 87, № 5, стр. 450-463. https://doi.org/10.1134/s0006297922050066

APA

Matiiv, A. B., Trubitsina, N. P., Matveenko, A. G., Barbitoff, Y. A., Zhouravleva, G. A., & Bondarev, S. A. (2022). Structure and Polymorphism of Amyloid and Amyloid-Like Aggregates. Biochemistry (Moscow), 87(5), 450-463. https://doi.org/10.1134/s0006297922050066

Vancouver

Matiiv AB, Trubitsina NP, Matveenko AG, Barbitoff YA, Zhouravleva GA, Bondarev SA. Structure and Polymorphism of Amyloid and Amyloid-Like Aggregates. Biochemistry (Moscow). 2022 Май;87(5):450-463. https://doi.org/10.1134/s0006297922050066

Author

Matiiv, Anton B. ; Trubitsina, Nina P. ; Matveenko, Andrew G. ; Barbitoff, Yury A. ; Zhouravleva, Galina A. ; Bondarev, Stanislav A. / Structure and Polymorphism of Amyloid and Amyloid-Like Aggregates. в: Biochemistry (Moscow). 2022 ; Том 87, № 5. стр. 450-463.

BibTeX

@article{97d803750fa2423e952e6a9428739252,
title = "Structure and Polymorphism of Amyloid and Amyloid-Like Aggregates",
abstract = "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.",
keywords = "amyloid polymorphism, amyloid-like aggregates, amyloids, cross-β structure, Amyloid/metabolism, Amyloidosis/genetics, Humans, Protein Conformation, Amyloidogenic Proteins, Polymorphism, Genetic",
author = "Matiiv, {Anton B.} and Trubitsina, {Nina P.} and Matveenko, {Andrew G.} and Barbitoff, {Yury A.} and Zhouravleva, {Galina A.} and Bondarev, {Stanislav A.}",
note = "Publisher Copyright: {\textcopyright} 2022, Pleiades Publishing, Ltd.",
year = "2022",
month = may,
doi = "10.1134/s0006297922050066",
language = "English",
volume = "87",
pages = "450--463",
journal = "Biochemistry (Moscow)",
issn = "0006-2979",
publisher = "МАИК {"}Наука/Интерпериодика{"}",
number = "5",

}

RIS

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