Author

Chongyuan Wang

Memorial Sloan Kettering Cancer CenterORCID 0000-0001-7477-5376Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Biochemistry· 1 Biophysics· 1 Molecular Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:protein structure prediction· 3 Organism:human· 2 Assay:cryo-EM· 1 Assay:DNA methylation· 1 Organism:fungi (other)· 1 Assay:structural biology· 1

Frequent Co-Authors

Ai-Xin Zhang· 1 shared Bei-Bei Ding· 1 shared Beiduo RaoiD· 1 shared Bin CuiiD· 1 shared Bryce D. DelgadoiD· 1 shared Chang-Run GuoiD· 1 shared Changzhu LiiD· 1 shared Dinshaw J. PateliD· 1 shared

Activity by Year

2021-2026 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 18 mutual co-author links

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1 shared paperBiophysics

Ai-Xin Zhang

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3 papers

Recent·Most cited

Cryo-EM elucidation of stoichiometric plasticity, asymmetric ligand recognition and allosteric coupling in human P2X2/3 heterotrimeric channels

Dong-Ping Wang, Wanbiao Chen, Xiao-Na Yang, Meng-Yang Sun, Ai-Xin Zhang, Yuan Gao, Xi Chen, Bin Cui, Xing Zhou, Yu Gao, Bei-Bei Ding, Yu Tian, Michael X. Zhu, Changzhu Li, Chang-Run Guo, , Ye Yu

The paper reports cryo-EM structures of human P2X2/3 heterotrimers in different functional states, revealing asymmetric ligand recognition and allosteric coupling mechanisms.

bioRxiv · Apr 6, 2026 · PreprintBiophysics

Structure of the human TWIK-2 potassium channel and its inhibition by pimozide

Nandish Khanra, Chongyuan Wang, Bryce D. Delgado, Stephen Barstow Long

This paper reports the cryo-EM structure of the human TWIK-2 potassium channel and shows that pimozide inhibits it by displacing acyl chains and blocking ion conduction.

Proceedings of the National Academy of Sciences · May 9, 2025Peer-reviewedBiochemistry

Structural basis of ATP-dependent high-fidelity epigenome maintenance

Juncheng Wang, Sandra Catania, Chongyuan Wang, M. Jason de la Cruz, Beiduo Rao, Hiten D. Madhani, Dinshaw J. Patel

The paper reveals the structural mechanism of ATP-dependent DNA methylation by DNMT5, showing how hemimethylated DNA activates the SNF2 ATPase domain and remodels the catalytic pocket for specificity.

bioRxiv · Oct 1, 2021 · PreprintMolecular Biology