Cryo-EM structure of full-length α-synuclein amyloid fibril with Parkinson’s disease familial A53T mutationYunpeng Sun, Cong Liu, Shouqiao Hou et al.|Cell Research|2020Cited by 149
Parkinson’s disease associated mutation E46K of α-synuclein triggers the formation of a distinct fibril structureKun Zhao, Cong Liu, Yunpeng Sun et al.|Nature Communications|2020Cited by 141
Cryo-EM structure of an amyloid fibril formed by full-length human SOD1 reveals its conformational conversionLiqiang Wang, Yi Liang, Yeyang Ma et al.|Nature Communications|2022Cited by 49
Amyloid fibril structures and ferroptosis activation induced by ALS-causing SOD1 mutationsLiqiang Wang, Yi Liang, Yeyang Ma et al.|Science Advances|2024Cited by 20
Distinct amyloid fibril structures formed by ALS-causing SOD1 mutants G93A and D101NMu-Ya Zhang, Yi Liang, Yeyang Ma et al.|EMBO Reports|2025Cited by 3