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α-synuclein folds: the cards are on the table

Nature Structural & Molecular Biology volume 23, pages 359360 (2016) | Download Citation

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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Author information

Affiliations

  1. Wouter Peelaerts and Veerle Baekelandt are at the Department of Neurosciences, KU Leuven, Leuven, Belgium.

    • Wouter Peelaerts
    •  & Veerle Baekelandt

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Competing interests

The authors declare no competing financial interests.

Corresponding author

Correspondence to Veerle Baekelandt.

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DOI

https://doi.org/10.1038/nsmb.3209

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