ArticleProceedings of the National Academy of Sciences of the United States of America2020
Amyloid formation of fish β-parvalbumin involves primary nucleation triggered by disulfide-bridged protein dimers.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 14 citations in OpenAlex.
- Investigating the structural changes of myosin under high pressure processing by molecular dynamics simulations.Current research in food science · 2026Article
- Pathological Disulfide Bond Crosslinking: Molecular Insights into Amyloidogenesis and Diseases Progression.Chembiochem : a European journal of chemical biology · 2025Review
- Comparative studies of seafood and reptile α- and β-parvalbumins.Protein science : a publication of the Protein Society · 2024Article
- Amyloid formation and depolymerization of tumor suppressor p16Nature communications · 2024Article
- Comprehensive Sequence Analysis of Parvalbumins in Fish and Their Comparison with Parvalbumins in Tetrapod Species.Biology · 2022Article
- Survey of the Intermolecular Disulfide Bonds Observed in Protein Crystal Structures Deposited in the Protein Data Bank.Life (Basel, Switzerland) · 2022Article
- Reaction ofInternational journal of molecular sciences · 2022Article
- Age-Related Changes in the Primary Motor Cortex of Newborn to Adult Domestic PigAnimals : an open access journal from MDPI · 2021Article
- Response to crowded conditions reveals compact nucleus for amyloid formation of folded protein.QRB discovery · 2021Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amyloid formation involves the conversion of soluble protein species to an aggregated state. Amyloid fibrils of β-parvalbumin, a protein abundant in fish, act as an allergen but also inhibit the in vitro assembly of the Parkinson protein α-synuclein. However, the intrinsic aggregation mechanism of β-parvalbumin has not yet been elucidated. We performed biophysical experiments in combination with mathematical modeling of aggregation kinetics and discovered that the aggregation of β-parvalbumin is initiated by the formation of dimers stabilized by disulfide bonds and then proceeds via primary nucleation and fibril elongation processes. Dimer formation is accelerated by H
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