Cryo-EM structures of chemical-compound-bound α-synuclein amyloid fibrils shed light on the mechanism by which small molecules bind to cross-beta-sheet amyloid structures, opening the gateway to rational drug design for targeting pathological amyloid assemblies.
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References
Fitzpatrick, A. W. P. et al. Nature 547, 185–190 (2017).
Tuttle, M. D. et al. Nat. Struct. Mol. Biol. 23, 409–415 (2016).
Yang, Y. et al. Science 375, 167–172 (2022).
Yang, Y. et al. Nature 610, 791–795 (2022).
Pujols, J., Pena-Diaz, S., Pallares, I. & Ventura, S. Trends Mol. Med. 26, 408–421 (2020).
Shi, Y. et al. Acta Neuropathol. 141, 697–708 (2021).
Seidler, P. M. et al. Nat. Commun. 13, 5451 (2022).
Liu, C. Nat. Chem. Biol. https://doi.org/10.1038/s41589-023-01370-x (2023).
Calabresi, P. et al. Cell Death Dis. 14, 176 (2023).
Pujols, J. et al. Proc. Natl Acad. Sci. USA 115, 10481–10486 (2018).
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Garcia-Pardo, J., Ventura, S. Chemical targeting of amyloids. Nat Chem Biol 19, 1176–1177 (2023). https://doi.org/10.1038/s41589-023-01394-3
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DOI: https://doi.org/10.1038/s41589-023-01394-3