{"entity": "researcher", "timestamp": "2026-10-17T03:11:27.467Z", "family": "Scheers", "given": "Nathalie", "initials": "N", "orcid": "0000-0001-8812-9025", "affiliations": [], "links": {"self": {"href": "https://publications.scilifelab.se/researcher/247e0ccd008f4795af5d666a181269b5.json"}, "display": {"href": "https://publications.scilifelab.se/researcher/247e0ccd008f4795af5d666a181269b5"}}, "publications": [{"entity": "publication", "iuid": "99256f2660b146e589a8e734ce7e0fe2", "links": {"self": {"href": "https://publications.scilifelab.se/publication/99256f2660b146e589a8e734ce7e0fe2.json"}, "display": {"href": "https://publications.scilifelab.se/publication/99256f2660b146e589a8e734ce7e0fe2"}}, "title": "Abundant fish protein inhibits \u03b1-synuclein amyloid formation.", "authors": [{"family": "Werner", "given": "Tony", "initials": "T"}, {"family": "Kumar", "given": "Ranjeet", "initials": "R"}, {"family": "Horvath", "given": "Istvan", "initials": "I"}, {"family": "Scheers", "given": "Nathalie", "initials": "N", "orcid": "0000-0001-8812-9025", "researcher": {"href": "https://publications.scilifelab.se/researcher/247e0ccd008f4795af5d666a181269b5.json"}}, {"family": "Wittung-Stafshede", "given": "Pernilla", "initials": "P", "orcid": "0000-0003-1058-1964", "researcher": {"href": "https://publications.scilifelab.se/researcher/9016aa00d62f439fb15532a1f4ba814e.json"}}], "type": "journal article", "published": "2018-04-03", "journal": {"title": "Sci Rep", "issn": "2045-2322", "volume": "8", "issue": "1", "pages": "5465", "issn-l": "2045-2322"}, "abstract": "The most common allergen in fish, the highly-abundant protein \u03b2-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 \u03b2-parvalbumin and the key amyloidogenic protein in Parkinson's disease, \u03b1-synuclein. Using a set of in vitro biophysical methods, we discovered that \u03b2-parvalbumin readily inhibits amyloid formation of \u03b1-synuclein. The underlying mechanism was found to involve \u03b1-synuclein binding to the surface of \u03b2-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 \u03b2-parvalbumin with human amyloidogenic proteins.", "doi": "10.1038/s41598-018-23850-0", "pmid": "29615738", "labels": {"Integrated Microscopy Technologies Gothenburg": "Service"}, "xrefs": [{"db": "pii", "key": "10.1038/s41598-018-23850-0"}, {"db": "pmc", "key": "PMC5882657"}], "notes": [], "created": "2020-01-23T16:33:32.278Z", "modified": "2021-06-21T13:56:47.848Z"}]}