Cryo-EM structure of full-length α-synuclein amyloid fibril with Parkinson's disease familial A53T mutation

Yunpeng Sun; Shouqiao Hou; Kun Zhao; Houfang Long; Zhenying Liu; Jing Gao; Yaoyang Zhang; Xiao-Dong Su; Dan Li; Cong Liu

doi:10.1038/s41422-020-0299-4

Cryo-EM structure of full-length α-synuclein amyloid fibril with Parkinson's disease familial A53T mutation

Cell Res. 2020 Apr;30(4):360-362. doi: 10.1038/s41422-020-0299-4. Epub 2020 Mar 12.

Authors

Yunpeng Sun^#^{1

2}, Shouqiao Hou^#^{1

2}, Kun Zhao^#^{1

2}, Houfang Long^{1

2}, Zhenying Liu^{1

2}, Jing Gao^{1

2}, Yaoyang Zhang^{1

2}, Xiao-Dong Su³, Dan Li^{4

5}, Cong Liu^{6

7}

Affiliations

¹ Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai, 201210, China.
² University of Chinese Academy of Sciences, Beijing, 100049, China.
³ State Key Laboratory of Protein and Plant Gene Research, and Biomedical Pioneering Innovation Center (BIOPIC), School of Life Sciences, Peking University, Beijing, 100871, China.
⁴ Bio-X-Renji Hospital Research Center, Renji Hospital, School of Medicine, Shanghai Jiao Tong University, Shanghai, 200240, China. lidan2017@sjtu.edu.cn.
⁵ Bio-X Institutes, Key Laboratory for the Genetics of Developmental and Neuropsychiatric Disorders, Ministry of Education, Shanghai Jiao Tong University, Shanghai, 200030, China. lidan2017@sjtu.edu.cn.
⁶ Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai, 201210, China. liulab@sioc.ac.cn.
⁷ University of Chinese Academy of Sciences, Beijing, 100049, China. liulab@sioc.ac.cn.

^# Contributed equally.

No abstract available

Publication types

Letter
Research Support, Non-U.S. Gov't

MeSH terms

Amyloid / chemistry*
Animals
Cryoelectron Microscopy
Humans
Mutation
Parkinson Disease / genetics*
Protein Conformation
Rats
alpha-Synuclein* / chemistry
alpha-Synuclein* / genetics

Substances

Amyloid
alpha-Synuclein