Han-Ye Yuan on Muck Rack

Han-Ye Yuan

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Articles

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

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By Li-Qiang Wang, Yeyang Ma, Mu-Ya Zhang, Han-Ye Yuan
| biorxiv.org
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Cryo-EM structure of an amyloid fibril formed by full-length human SOD1 reveals its conformational conversion - Nature Communications

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By Li-Qiang Wang, Han-Ye Yuan, Kun Zhao, Qiang Wang, Xi Huang, Dan Li, Delin Zhang, Zhengzhi Wang, Ping Yin, Yi Liang, Yeyang Ma, Mu-Ya Zhang, Liangyu Zou
| Nature Verified
Abstract 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. Here we produced cytotoxic amyloid fibrils from full-length apo human SOD1 under reducing conditions and determined the atomic structure using cryo-EM. The SOD1 fibril consists of a single protofilament with a left-handed helix.
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Cryo-EM structure of an amyloid fibril formed by full-length human prion protein

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By Li-Qiang Wang, Zeyuan Guan, Dan Li, Han-Ye Yuan
| Nature Verified
Abstract Prion diseases are caused by the misfolding of prion protein (PrP). Misfolded PrP forms protease-resistant aggregates in vivo (PrPSc) that are able to template the conversion of the native form of the protein (PrPC), a property shared by in vitro–produced PrP fibrils. Here we produced amyloid fibrils in vitro from recombinant, full-length human PrPC (residues 23–231) and determined their structure using cryo-EM, building a model for the fibril core comprising residues 170−229.
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