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α-synuclein folds: the cards are on the table

All current evidence indicates a central role for α-synuclein (α-SYN) amyloid fibrils in Parkinson's disease and other synucleinopathies, but the precise relationship between amyloid aggregates and the resulting phenotype remains poorly understood, partly because of the lack of reliable three-dimensional structures. In this issue, the structure of a toxic α-SYN fibril is now presented at unprecedented resolution.

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Figure 1: Proposed structure of a complete α-SYN fibril.


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Correspondence to Veerle Baekelandt.

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Peelaerts, W., Baekelandt, V. α-synuclein folds: the cards are on the table. Nat Struct Mol Biol 23, 359–360 (2016).

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