Protein aggregation: An overview.


Journal

Progress in molecular biology and translational science
ISSN: 1878-0814
Titre abrégé: Prog Mol Biol Transl Sci
Pays: Netherlands
ID NLM: 101498165

Informations de publication

Date de publication:
2024
Historique:
medline: 30 5 2024
pubmed: 30 5 2024
entrez: 29 5 2024
Statut: ppublish

Résumé

In order for an ordered protein to perform its specific function, it must have a specific molecular structure. Information about this structure is encoded in the protein's amino acid sequence. The unique functional state is achieved as a result of a specific process, known as protein folding. However, as a result of partial or complete unfolding of the polypeptide chain, proteins may misfold and aggregate, leading to the formation of various aggregated structures, such as like amyloid aggregates with the cross-β structure. A variety of cellular biological processes can be affected by protein aggregates that consume essential factors necessary for maintaining proteostasis, which leads to the proteostasis imbalance and further accumulation of protein aggregates, often resulting in age-related neurodegenerative disease progression and aging. However, in addition to their well-established pathological effects, amyloids also play various physiological roles, and many important biological processes involve such 'functional amyloids'. This chapter represents a brief overview of the protein aggregation phenomenon outlines a timeline provides of some key discoveries in this exciting field.

Identifiants

pubmed: 38811077
pii: S1877-1173(24)00062-0
doi: 10.1016/bs.pmbts.2024.03.007
pii:
doi:

Substances chimiques

Protein Aggregates 0
Amyloid 0
Proteins 0

Types de publication

Journal Article Review

Langues

eng

Sous-ensembles de citation

IM

Pagination

1-10

Informations de copyright

Copyright © 2024. Published by Elsevier Inc.

Auteurs

Bahareh Dabirmanesh (B)

Department of Biochemistry, Faculty of Biological Sciences, Tarbiat Modares University, Tehran, Iran.

Khosro Khajeh (K)

Department of Biochemistry, Faculty of Biological Sciences, Tarbiat Modares University, Tehran, Iran.

Vladimir N Uversky (VN)

Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, Institute for Biological Instrumentation, Pushchino, Moscow, Russia; Department of Molecular Medicine and USF Health Byrd Alzheimer's Research Institute, Morsani College of Medicine, University of South Florida, Tampa, FL, United States. Electronic address: vuversky@usf.edu.

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Classifications MeSH