An ultra-high-resolution structure of the core segment of assembled α-synuclein — the protein that aggregates in the brains of patients with Parkinson's disease — has been determined. A neurobiologist and a structural biologist discuss the implications of this advance. See Article p.486
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References
Rodriguez, J. A. et al. Nature 525, 486–490 (2015).
Goedert, M., Spillantini, M. G., Del Tredici, K. & Braak, H. Nature Rev. Neurol. 9, 13–24 (2013).
Osterberg, V. R. et al. Cell Rep. 10, 1252–1260 (2015).
El-Agnaf, O. M. A. & Irvine, B. G. Biochem. Soc. Trans. 30, 559–565 (2002).
Sawaya, M. R. et al. Nature 447, 453–457 (2007).
Sievers, S. A. et al. Nature 475, 96–100 (2011).
Cheng, Y. Cell 161, 450–457 (2015).
Shi, D., Nannenga, B. L., Iadanza, M. G. & Gonen, T. eLife 2, e01345 (2013).
Gonen, T. et al. Nature 438, 633–638 (2005).
Nannenga, B. L., Shi, D., Leslie, A. G. & Gonen, T. Nature Methods 11, 927–930 (2014).
Mitsuoka, K. et al. J. Mol. Biol. 286, 861–882 (1999).
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Goedert, M., Cheng, Y. Crystals of a toxic core. Nature 525, 458–459 (2015). https://doi.org/10.1038/nature15630
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DOI: https://doi.org/10.1038/nature15630
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