Two New Polymorphs in H50Q Determined by CryoEM Suggest a Mechanism That Explains Its Faster Kinetics In Vitro

被引:3
作者
Aguirre, Cesar [1 ]
Ikenaka, Kensuke [1 ]
Mochizuki, Hideki [1 ]
机构
[1] Osaka Univ, Grad Sch Med, Dept Neurol, 2-2 Yamadaoka, Suita, Osaka 5650871, Japan
基金
日本学术振兴会;
关键词
amyloid structure; CryoEM; familial mutation; alpha-synuclein;
D O I
10.1002/mds.28100
中图分类号
R74 [神经病学与精神病学];
学科分类号
摘要
引用
收藏
页码:935 / 936
页数:2
相关论文
共 5 条
[1]   The α-synuclein hereditary mutation E46K unlocks a more stable, pathogenic fibril structure [J].
Boyer, David R. ;
Li, Binsen ;
Sun, Chuanqi ;
Fan, Weijia ;
Zhou, Kang ;
Hughes, Michael P. ;
Sawaya, Michael R. ;
Jiang, Lin ;
Eisenberg, David S. .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2020, 117 (07) :3592-3602
[2]   Structures of fibrils formed by α-synuclein hereditary disease mutant H50Q reveal new polymorphs [J].
Boyer, David R. ;
Li, Binsen ;
Sun, Chuanqi ;
Fan, Weijia ;
Sawaya, Michael R. ;
Jiang, Lin ;
Eisenberg, David S. .
NATURE STRUCTURAL & MOLECULAR BIOLOGY, 2019, 26 (11) :1044-+
[3]   Cryo-EM structure of alpha-synuclein fibrils [J].
Guerrero-Ferreira, Ricardo ;
Taylor, Nicholas M. I. ;
Mona, Daniel ;
Ringler, Philippe ;
Lauer, Matthias E. ;
Riek, Roland ;
Britschgi, Markus ;
Stahlberg, Henning .
ELIFE, 2018, 7
[4]  
HAYAKAWA H, 2019, MOVEMENT DISORD, P1
[5]   Cryo-EM of full-length α-synuclein reveals fibril polymorphs with a common structural kernel [J].
Li, Binsen ;
Ge, Peng ;
Murray, Kevin A. ;
Sheth, Phorum ;
Zhang, Meng ;
Nair, Gayatri ;
Sawaya, Michael R. ;
Shin, Woo Shik ;
Boyer, David R. ;
Ye, Shulin ;
Eisenberg, David S. ;
Zhou, Z. Hong ;
Jiang, Lin .
NATURE COMMUNICATIONS, 2018, 9