Protein misfolding, oligomerization and aggregation are implicated in a variety of neurodegenerative disorders, including Alzheimer's and Parkinson's diseases. New research sheds light on the process of amyloid-β aggregation in vitro, identifying nucleated conformational conversion of oligomers as the mechanism for generating amyloid fibrils.
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Few-layer bismuth selenides exfoliated by hemin inhibit amyloid-β1–42 fibril formation
Scientific Reports Open Access 28 May 2015
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Outeiro, T. FlAsH illuminates Aβ aggregation. Nat Chem Biol 7, 581–582 (2011). https://doi.org/10.1038/nchembio.636
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DOI: https://doi.org/10.1038/nchembio.636
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Few-layer bismuth selenides exfoliated by hemin inhibit amyloid-β1–42 fibril formation
Scientific Reports (2015)