Author

Xue Lyu

University of East Anglia

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Plant Biology· 2

Signature Assays, Organisms & Methods

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Organism:Arabidopsis· 2 Approach:experimental assay· 2 Assay:protein structure· 2 Research Focus:protein structure prediction· 2 Research Focus:cell type annotation· 1 Assay:cryo-EM· 1 Approach:deep learning· 1 Assay:imaging· 1

Frequent Co-Authors

He ZhaoiD· 2 shared Jonathan D. G. JonesiD· 2 shared Muniyandi SelvarajiD· 2 shared Sophien KamouniD· 2 shared Baoge Huang· 1 shared Camille-Madeleine SzymanskyiD· 1 shared Chao WangiD· 1 shared Chenchen Hu· 1 shared

Activity by Year

2026-2026 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 37 mutual co-author links

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2 shared papersPlant Biology

He ZhaoORCID

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Author profile →

2 papers

Recent·Most cited

An activated wheat CCG10-NLR immune receptor forms an octameric resistosome

Guanghao Guo, He Zhao, Kaihong Bai, Professor Jian Lu, Qiuhong Wu, Lei Lu, Yue Zhang, Lingli Dong, Guangwei Li, Yongxing Chen, Yikun Hou, Ping Lu, Miaomiao Li, Huaizhi Zhang, Gaojie Wang, , Jonathan D. G. Jones

Activated wheat CCG10-NLR immune receptor WAI3 and Arabidopsis RPS2 assemble into octameric calcium-permeable resistosomes with an inverted coiled-coil domain topology associated with lacking the conserved EDVID motif.

Cell · Mar 20, 2026Peer-reviewedPlant Biology✦ In-depth digest

Structural basis for the broad recognition specificity of an Arabidopsis immune receptor

He Zhao, Camille-Madeleine Szymansky, Xue Lyu, Jianhua Huang, Paul Derbyshire, Frank L.H. Menke, Michael W Webster, Sophien Kamoun, Muniyandi Selvaraj, Jonathan D. G. Jones

This study determines the structural basis of broad recognition by the Arabidopsis NLR WRR4A, revealing a shape-based mechanism that enables recognition of diverse effectors with similar three-dimensional architectures.

bioRxiv · Feb 7, 2026 · PreprintPlant Biology