Author

Xueni Li

University of Colorado AnschutzORCID 0000-0002-3969-8480Unclaimed ORCID profile · follow to get notified of new preprints

Additional preprints under this name without ORCID

Xueni Li1 paper · Peking University

Biology Disciplines

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Biochemistry· 2 Molecular Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Research Focus:cell-cell communication· 1 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:differential expression· 1 Research Focus:gene regulatory network inference· 1 Approach:genetic perturbation / CRISPR· 1

Frequent Co-Authors

Rui ZhaoiD· 3 shared Shasha ShiiD· 3 shared Zhiling Kuang· 2 shared Aaron IssaianiD· 1 shared Angelo D’AlessandroiD· 1 shared Brian Kosmyna· 1 shared Christopher Alderman· 1 shared Christopher R. TrottaiD· 1 shared

Activity by Year

2025-2026 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 26 mutual co-author links

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3 shared papersBiochemistry

Rui ZhaoORCID

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

The U1 snRNP protein U1C and Helix H of U1 snRNA are critical for small molecule splicing modulator function

Zhiling Kuang, Brian Kosmyna, Xueni Li, Zhichao Tang, Shasha Shi, Karoline A. Lambert, Wenzheng Zhang, Joseph A. Giovinazzo, Kerstin A. Effenberger, Jairo Sierra, Lanqing Ying, Scott J. Barraza, Wencheng Li, Jingxin Wang, Christopher R. Trotta, Rui Zhao

This study shows that U1C and Helix H of U1 snRNA are essential for branaplam's effect on weak 5 splice site recognition, while risdiplam requires additional factors for activity.

Nature Communications · Jul 16, 2026Peer-reviewedBiochemistry

U1 snRNP and RNA polymerase II interaction is predominantly mediated by Prp40 rather than U1-70K in yeast

Xueni Li, Jiaqin Li, Shasha Shi, Zhiling Kuang, Pankaj K. Srivastava, Aaron Issaian, Shaun G. Bevers, Marisa Elise Wagley, Angelo D’Alessandro, Rui Zhao

The paper investigates the interaction between U1 snRNP and RNA polymerase II in yeast, finding that Prp40, not U1-70K, mediates this interaction, contrasting with the human system.

Nucleic Acids Research · Jun 8, 2026Peer-reviewedBiochemistry

Cryo-EM structures reveal the PP2A-B55α and Eya3 interaction that can be disrupted by a peptide inhibitor

Shasha Shi, Xueni Li, Christopher Alderman, Lars Wick, Wei Huang, North Foulon, Lingdi Zhang, John J. Rossi, Wenxin Hu, Shouqing Cui, Hongjin Zheng, Derek J. Taylor, Heide L. Ford, Rui Zhao

The paper determines cryo-EM structures of PP2A-B55 and Eya3 interaction, showing how a peptide inhibitor disrupts this interaction and affects Myc stability in TNBC.

Journal of Biological Chemistry · May 23, 2025Peer-reviewedMolecular Biology