Cellular milieu imparts distinct pathological α-synuclein strains in α-synucleinopathies
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DOI: 10.1038/s41586-018-0104-4
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Cited by:
- Martin Wilkinson & Rodrigo U. Gallardo & Roberto Maya Martinez & Nicolas Guthertz & Masatomo So & Liam D. Aubrey & Sheena E. Radford & Neil A. Ranson, 2023. "Disease-relevant β2-microglobulin variants share a common amyloid fold," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
- Jinjian Hu & Wencheng Xia & Shuyi Zeng & Yeh-Jun Lim & Youqi Tao & Yunpeng Sun & Lang Zhao & Haosen Wang & Weidong Le & Dan Li & Shengnan Zhang & Cong Liu & Yan-Mei Li, 2024. "Phosphorylation and O-GlcNAcylation at the same α-synuclein site generate distinct fibril structures," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
- Youqi Tao & Yunpeng Sun & Shiran Lv & Wencheng Xia & Kun Zhao & Qianhui Xu & Qinyue Zhao & Lin He & Weidong Le & Yong Wang & Cong Liu & Dan Li, 2022. "Heparin induces α-synuclein to form new fibril polymorphs with attenuated neuropathology," Nature Communications, Nature, vol. 13(1), pages 1-9, December.
- Norihito Uemura & Nicholas P. Marotta & Jahan Ara & Emily S. Meymand & Bin Zhang & Hiroshi Kameda & Masato Koike & Kelvin C. Luk & John Q. Trojanowski & Virginia M.-Y. Lee, 2023. "α-Synuclein aggregates amplified from patient-derived Lewy bodies recapitulate Lewy body diseases in mice," Nature Communications, Nature, vol. 14(1), pages 1-17, December.
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