Cryo-EM structure of an amyloid fibril formed by full-length human SOD1 reveals its conformational conversion

Misfolded SOD1 has been linked to both familial and sporadic ALS. Here the authors have determined the cryo-EM structure of SOD1 fibrils, providing insights into the conversion of SOD1 from its immature form into an aggregated form during pathogenesis of ALS.

Bibliographic Details
Main Authors: Li-Qiang Wang, Yeyang Ma, Han-Ye Yuan, Kun Zhao, Mu-Ya Zhang, Qiang Wang, Xi Huang, Wen-Chang Xu, Bin Dai, Jie Chen, Dan Li, Delin Zhang, Zhengzhi Wang, Liangyu Zou, Ping Yin, Cong Liu, Yi Liang
Format: Article
Language:English
Published: Nature Portfolio 2022-06-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-022-31240-4
Description
Summary:Misfolded SOD1 has been linked to both familial and sporadic ALS. Here the authors have determined the cryo-EM structure of SOD1 fibrils, providing insights into the conversion of SOD1 from its immature form into an aggregated form during pathogenesis of ALS.
ISSN:2041-1723