Protein aggregation: An overview.
Amyloid fibril
Cross-β
Protein aggregation
Proteostasis
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
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
1-10Informations de copyright
Copyright © 2024. Published by Elsevier Inc.