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Yingshan Li

As seen in: Nature, ACS Publications, Cell Reports Physical Science
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Articles

Structural Basis of Amyloid Fibril Assembly by Plant Seed Storage Proteins

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By Yiling Zhang, Danni Li, Qinyue Zhao, Shiran Lv, Wencheng Xia, Yongyi Xu, Yingshan Li, Yunxia Li, Yaoyang Zhang, Dan Li, Bo Sun, Wenyan Kang, Cong Liu, Bin Dai
| Nature Verified
Abstract Amyloid fibrils are highly ordered protein assemblies characterized by a cross-β architecture. A wide range of proteins can adopt amyloid states, contributing to both disease-related pathology and normal physiological function. While animal-derived amyloids have been extensively examined in atomic detail, amyloid fibrils formed by plant proteins remain relatively understudied.
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Structural Basis of Amyloid Fibril Assembly by Plant Seed Storage Proteins

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By Yiling Zhang, Danni Li, Qinyue Zhao, Shiran Lv, Wencheng Xia, Yongyi Xu, Yingshan Li, Yunxia Li, Yaoyang Zhang, Dan Li, Bo Sun, Wenyan Kang, Cong Liu, Bin Dai
| Nature Verified
Abstract Amyloid fibrils are highly ordered protein assemblies characterized by a cross-β architecture. A wide range of proteins can adopt amyloid states, contributing to both disease-related pathology and normal physiological function. While animal-derived amyloids have been extensively examined in atomic detail, amyloid fibrils formed by plant proteins remain relatively understudied.
Open in Who Shared Issue with article?

Ultrastructural and atomic characterization of biofilm-associated extracellular filaments in Shewanella oneidensis MR-1

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By Danni Li, Hui Dong, Guicong Zhang, Yingshan Li, Xingwu Liu, Yaru Chen, Lin Xiao, Xinyu Wang, Dan Li, Chao Zhong, Qin Cao, Bin Dai, Cong Liu
| Nature Verified
Abstract Biofilms formed by Shewanella oneidensis MR-1 are crucial for metal reduction, underpinning bioremediation and bioenergy applications, yet detailed structural insights into biofilm components remain limited. Here we show that MR-1 biofilms contain abundant filamentous networks, membrane vesicles, and distinct square-shaped aggregates, as revealed by cryo-electron tomography and cryo-electron microscopy.
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