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Advanced Science (Weinheim, Baden-Wurttemberg, Germany)|February 14, 2025
Single-Molecule Insight Into α-Synuclein Fibril Structure and Mechanics Modulated by Chemical CompoundsXiang Li, Lulu Bi, Shenqing Zhang, et al.
Nature Communications|December 14, 2020
The nuclear localization sequence mediates hnRNPA1 amyloid fibril formation revealed by cryoEM structureYunpeng Sun, Kun Zhao, Wencheng Xia, et al.
EMBO Reports|August 26, 2025
Distinct amyloid fibril structures formed by ALS-causing SOD1 mutants G93A and D101NMu-Ya Zhang, Yeyang Ma, Li-Qiang Wang, et al.
Journal of the American Chemical Society|November 29, 2021
O-Glycosylation Induces Amyloid-β To Form New Fibril Polymorphs Vulnerable for DegradationDangliang Liu, Qijia Wei, Wencheng Xia, et al.
Nature Communications|March 28, 2024
Phosphorylation and O-GlcNAcylation at the same α-synuclein site generate distinct fibril structuresJinjian Hu, Wencheng Xia, Shuyi Zeng, et al.
Proceedings of the National Academy of Sciences of the United States of America|August 22, 2024
Binding adaptability of chemical ligands to polymorphic α-synuclein amyloid fibrilsKaien Liu, Youqi Tao, Qinyue Zhao, et al.
Structure (London, England : 1993)|December 13, 2022
Conformational change of α-synuclein fibrils in cerebrospinal fluid from different clinical phases of Parkinson's diseaseYun Fan, Yunpeng Sun, Wenbo Yu, et al.
Nature Communications|July 2, 2025
An O-glycopeptide participates in the formation of distinct Aβ42 fibril structures and attenuates Aβ42 neurotoxicityQijia Wei, Dangliang Liu, Wencheng Xia, et al.
Cell|May 26, 2026
TPPP/p25 amyloid seeding activity as a specific biomarker for multiple system atrophyShuyi Zeng, Shenqing Zhang, Shengnan Zhang, et al.
Science Advances|October 30, 2024
Amyloid fibril structures and ferroptosis activation induced by ALS-causing SOD1 mutationsLi-Qiang Wang, Yeyang Ma, Mu-Ya Zhang, et al.
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