Explanipedia

Intercellular propagation of RIPK1/RIPK3 amyloid fibrils Open

Yeyang Ma, Qiuyuan Zhang, Dekang Li, Kun Zhao, Zefei Li , et al. · 2025

The canonical necrosome formed by receptor-interacting protein kinase 1 (RIPK1) and RIPK3 is a functional amyloid fibril structure critical to intracellularly drive necroptosis. Since necroptosis leads to the release of intracellular conte…

Distinct amyloid fibril structures formed by ALS-causing SOD1 mutants G93A and D101N Open

Mu-Ya Zhang, Yeyang Ma, Liqiang Wang, Wencheng Xia, Xiangning Li , et al. · 2025

Amyloid fibril structures and ferroptosis activation induced by ALS-causing SOD1 mutations Open

Liqiang Wang, Yeyang Ma, Mu-Ya Zhang, Han‐Ye Yuan, Xiang-Ning Li , et al. · 2024

Over 200 genetic mutations in copper-zinc superoxide dismutase (SOD1) have been linked to amyotrophic lateral sclerosis (ALS). Among these, two ALS-causing mutants, histidine-46→arginine (H46R) and glycine-85→arginine (G85R), exhibit a dec…

Creating an Amyloid ‘Kaleidoscope’ Using Short Iodinated Peptides Open

Danni Li, Yeyang Ma, Wencheng Xia, Youqi Tao, Shujun Zhang , et al. · 2023

Amyloid fibrils formed by peptides with different sequences exhibit diversified morphologies, material properties and activities, making them valuable for developing functional bionanomaterials. However, the molecular understanding underly…

Inside Front Cover: Protein amyloid aggregate: Structure and function Open

Qianhui Xu, Yeyang Ma, Yunpeng Sun, Dan Li, Xin Zhang , et al. · 2023

Amyloid protein aggregation represents a crucial biological process with notable physiological relevance and significant implications in disease pathology. These amyloid aggregates, characterized by their unique structures, gain a variety …

ALS-causing SOD1 mutations H46R and G85R form similar novel amyloid fibril structures and promote ferroptosis in cells Open

Liqiang Wang, Yeyang Ma, Mu-Ya Zhang, Han‐Ye Yuan, Xiang-Ning Li , et al. · 2023

More than two hundred genetic mutations of Cu, Zn-superoxide dismutase (SOD1) have been identified in amyotrophic lateral sclerosis (ALS), a neurodegenerative disease characterized by the selective death of motor neurons through ferroptosi…

Protein amyloid aggregate: Structure and function Open

Qianhui Xu, Yeyang Ma, Yunpeng Sun, Dan Li, Xin Zhang , et al. · 2023

Protein amyloid aggregation has been widely observed to occur and plays important roles in both physiological processes and pathological diseases. Remarkably, amyloid aggregates assembled by native proteins gain a variety of different biol…

Prefrontal brain function in patients with chronic insomnia disorder: A pilot functional near-infrared spectroscopy study Open

Haiyan Gong, Hui Sun, Yeyang Ma, Ya-Ling Tan, Minglong Cui , et al. · 2022

Purpose Insomnia is one of the most common diseases in elderly patients, which seriously affect the quality of life and psychological state of patients. The purpose of this study was to investigate the changes in the functional network pat…

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

Liqiang Wang, Yeyang Ma, Han‐Ye Yuan, Kun Zhao, Mu-Ya Zhang , et al. · 2022

Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disease. Misfolded Cu, Zn-superoxide dismutase (SOD1) has been linked to both familial and sporadic ALS. SOD1 fibrils formed in vitro share toxic properties with ALS inclusions. He…

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

Liqiang Wang, Yeyang Ma, Han‐Ye Yuan, Kun Zhao, Mu-Ya Zhang , et al. · 2021

Amyotrophic lateral sclerosis (ALS) is a progressive, fatal neurodegenerative disease characterized by the selective death of motor neurons. Misfolded Cu, Zn-superoxide dismutase (SOD1) has been linked to both familial ALS and sporadic ALS…

Genetic prion disease–related mutation E196K displays a novel amyloid fibril structure revealed by cryo-EM Open

Liqiang Wang, Kun Zhao, Han‐Ye Yuan, Xiangning Li, Hai-Bin Dang , et al. · 2021

The cryo-EM structure of genetic CJD mutation E196K fibril reveals a novel fibril polymorph of human prion protein.

The structure of a minimum amyloid fibril core formed by necroptosis-mediating RHIM of human RIPK3 Open

Xialian Wu, Yeyang Ma, Kun Zhao, Jing Zhang, Yunpeng Sun , et al. · 2021

Significance Receptor-interacting protein kinases 3 (RIPK3), a hub player in necrotic cell death, forms amyloid-like polymers in response to upstream mediators. This work, by using cryo-EM and solid-state NMR, reports the structure of huma…

Familial prion disease-related mutation E196K displays a novel amyloid fibril structure revealed by cryo-EM Open

Liqiang Wang, Kun Zhao, Han‐Ye Yuan, Xiangning Li, Hai-Bin Dang , et al. · 2021

Prion diseases are caused by the conformational conversion of prion protein (PrP) from its cellular form (PrP C ) into a protease-resistant, aggregated form (PrP Sc ). 42 different familial mutations were identified in human PrP, which lea…

The nuclear localization sequence mediates hnRNPA1 amyloid fibril formation revealed by cryoEM structure Open

Yunpeng Sun, Kun Zhao, Wencheng Xia, Guoqin Feng, Jinge Gu , et al. · 2020

The nuclear localization sequence mediates hnRNPA1 amyloid fibril formation revealed by cryoEM structure Open

Yunpeng Sun, Kun Zhao, Wencheng Xia, Jinge Gu, Yeyang Ma , et al. · 2020

Human heterogeneous nuclear ribonucleoprotein A1 (hnRNPA1) serves as a key regulating protein in RNA metabolism. Malfunction of hnRNPA1 in nucleo-cytoplasmic transport or dynamic phase separation leads to abnormal amyloid aggregation and n…

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