Protein amyloid aggregation is a histological hallmark of neurodegenerative diseases (NDs). 1 , 2 In synucleinopathies including Parkinson’s disease (PD), Parkinson’s disease dementia (PDD), dementia with Lewy body and multiple system atrophy, α-synuclein (α-syn) is commonly characterized to form amyloid aggregates presenting distinct pathological activities in diseased brains. 3 , 4 Structural characterization of α-syn amyloid fibrils formed in different diseases could provide mechanistic understanding of heterogeneous α-syn pathologies. 5 , 6
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Fan et al. (2022) studied this question.
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