ArticleScientific reports2018
Abundant fish protein inhibits α-synuclein amyloid formation.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 28 citations in OpenAlex.
- Comparative Analysis of Aggregation of β- and γ-Synucleins in Vertebrates.Biomolecules · 2025Article
- Biological Amyloids Chemically Damage DNA.ACS chemical neuroscience · 2025Article
- Amyloids of α-Synuclein Promote Chemical Transformations of Neuronal Cell Metabolites.International journal of molecular sciences · 2023Article
- Could the Urease of the Gut BacteriumMicroorganisms · 2023Article
- Distinct growth regimes of α-synuclein amyloid elongation.Biophysical journal · 2023Article
- Structural Specificity of Polymorphic Forms of α-Synuclein Amyloid.Biomedicines · 2023Article
- Amyloid Fibers of α-Synuclein Catalyze Chemical Reactions.ACS chemical neuroscience · 2023Article
- Food protein-derived amyloids do not accelerate amyloid β aggregation.Scientific reports · 2023Article
- Protective Effects of Fish (Alaska Pollock) Protein Intake against Short-Term Memory Decline in Senescence-Accelerated Mice.Nutrients · 2022Article
- Microbiome Impact on Amyloidogenesis.Frontiers in molecular biosciences · 2022Review
- Macromolecular crowding modulates α-synuclein amyloid fiber growth.Biophysical journal · 2021Article
- Response to crowded conditions reveals compact nucleus for amyloid formation of folded protein.QRB discovery · 2021Article
- Amyloid formation of fish β-parvalbumin involves primary nucleation triggered by disulfide-bridged protein dimers.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Differential effects of CuBiometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2020Article
- Crosstalk Between Alpha-Synuclein and Other Human and Non-Human Amyloidogenic Proteins: Consequences for Amyloid Formation in Parkinson's Disease.Journal of Parkinson's disease · 2020Review
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
The most common allergen in fish, the highly-abundant protein β-parvalbumin, forms amyloid structures as a way to avoid gastrointestinal degradation and transit to the blood. In humans, the same amyloid structures are mostly associated with neurodegenerative disorders such as Alzheimer's and Parkinson's. We here assessed a putative connection between these amyloids using recombinant Atlantic cod β-parvalbumin and the key amyloidogenic protein in Parkinson's disease, α-synuclein. Using a set of in vitro biophysical methods, we discovered that β-parvalbumin readily inhibits amyloid formation of α-synuclein. The underlying mechanism was found to involve α-synuclein binding to the surface of β-parvalbumin amyloid fibers. In addition to being a new amyloid inhibition mechanism, the data suggest that health benefits of fish may be explained in part by cross-reaction of β-parvalbumin with human amyloidogenic proteins.
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