Amyloids: from Pathogenesis to Function

Research output

19 Citations (Scopus)

Abstract

The term "amyloids" refers to fibrillar protein aggregates with cross-β structure. They have been a subject of intense scrutiny since the middle of the previous century. First, this interest is due to association of amyloids with dozens of incurable human diseases called amyloidoses, which affect hundreds of millions of people. However, during the last decade the paradigm of amyloids as pathogens has changed due to an increase in understanding of their role as a specific variant of quaternary protein structure essential for the living cell. Thus, functional amyloids are found in all domains of the living world, and they fulfill a variety of roles ranging from biofilm formation in bacteria to long-term memory regulation in higher eukaryotes. Prions, which are proteins capable of existing under the same conditions in two or more conformations at least one of which having infective properties, also typically have amyloid features. There are weighty reasons to believe that the currently known amyloids are only a minority of their real number. This review provides a retrospective analysis of stages in the development of amyloid biology that during the last decade resulted, on one hand, in reinterpretation of the biological role of amyloids, and on the other hand, in the development of systems biology of amyloids, or amyloidomics.

Original languageEnglish
Pages (from-to)1127-1144
Number of pages18
JournalBiochemistry (Moscow)
Volume80
Issue number9
DOIs
Publication statusPublished - 2015

Fingerprint

Amyloid
Quaternary Protein Structure
Systems Biology
Long-Term Memory
Prions
Biofilms
Pathogens
Amyloidosis
Eukaryota
Conformations
Bacteria
Proteins
Cells
Association reactions
Data storage equipment

Cite this

Nizhnikov, A A ; Antonets, K S ; Inge-Vechtomov, S G. / Amyloids : from Pathogenesis to Function. In: Biochemistry (Moscow). 2015 ; Vol. 80, No. 9. pp. 1127-1144.
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Amyloids : from Pathogenesis to Function. / Nizhnikov, A A; Antonets, K S; Inge-Vechtomov, S G.

In: Biochemistry (Moscow), Vol. 80, No. 9, 2015, p. 1127-1144.

Research output

TY - JOUR

T1 - Amyloids

T2 - from Pathogenesis to Function

AU - Nizhnikov, A A

AU - Antonets, K S

AU - Inge-Vechtomov, S G

PY - 2015

Y1 - 2015

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AB - The term "amyloids" refers to fibrillar protein aggregates with cross-β structure. They have been a subject of intense scrutiny since the middle of the previous century. First, this interest is due to association of amyloids with dozens of incurable human diseases called amyloidoses, which affect hundreds of millions of people. However, during the last decade the paradigm of amyloids as pathogens has changed due to an increase in understanding of their role as a specific variant of quaternary protein structure essential for the living cell. Thus, functional amyloids are found in all domains of the living world, and they fulfill a variety of roles ranging from biofilm formation in bacteria to long-term memory regulation in higher eukaryotes. Prions, which are proteins capable of existing under the same conditions in two or more conformations at least one of which having infective properties, also typically have amyloid features. There are weighty reasons to believe that the currently known amyloids are only a minority of their real number. This review provides a retrospective analysis of stages in the development of amyloid biology that during the last decade resulted, on one hand, in reinterpretation of the biological role of amyloids, and on the other hand, in the development of systems biology of amyloids, or amyloidomics.

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DO - 10.1134/S0006297915090047

M3 - Review article

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VL - 80

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JO - Biochemistry (Moscow)

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