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• W3094150239 abstract "Significance Amyloid fibrils are generally related to neurodegenerative diseases, but they can also be part of normal protein function. Amyloid formation involves numerous steps and intermediate species. In this study, we investigated a fish protein, beta-parvalbumin, which readily forms amyloid on ligand removal. Using biophysical experiments, we provide evidence that the underlying mechanism of amyloid formation includes primary nucleation and elongation processes; we also reveal a key role for a disulfide-bridged dimer in the nucleation step. Little is known about intermolecular disulfides in amyloid formation, but covalent dimers and dimer-induced aggregation may be of clinical relevance, because oxidative stress, which can trigger covalent bond formation, is often a hallmark of human neurodegenerative diseases." @default.
• W3094150239 created "2020-10-29" @default.
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• W3094150239 date "2020-10-22" @default.
• W3094150239 modified "2023-09-30" @default.
• W3094150239 title "Amyloid formation of fish β-parvalbumin involves primary nucleation triggered by disulfide-bridged protein dimers" @default.
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• W3094150239 doi "https://doi.org/10.1073/pnas.2015503117" @default.
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