Our long-term research goal is to elucidate the molecular mechanisms underlying the complex roles of chemical modifications in regulating the functions of biomacromolecules. By integrating chemical biology with structural, molecular, and cell biology, we develop potent chemical tools to manipulate chemical modifications and investigate how dysregulated modifications contribute to human diseases, particularly cancer and neurodegenerative disorders. Ultimately, our research seeks to advance a mechanistic understanding of human biology and facilitate the identification of novel therapeutic targets and the development of strategies for disease intervention.
Our current research focuses on the molecular mechanisms by which post-translational modifications regulate protein function, with a particular emphasis on the ubiquitin–proteasome system (UPS) and the control of protein stability. We are especially interested in understanding how E3 ubiquitin ligases recognize their substrates and catalyze their polyubiquitination, as well as how mechanistic insights from structural and chemical biology can be translated into chemical tools and therapeutic strategies, including targeted protein degraders (TPDs).
- Molecular basis for Eaf3-mediated assembly of Rpd3S and NuA4.Cell Discov.,2023,9(1):51.
- Molecular basis for C-degron recognition by CRL2APPBP2 ubiquitin ligase.Proc Natl Acad Sci U S A.,2023,120(43):e2308870120.
- Mechanism of Ψ-Pro/C-degron recognition by the CRL2FEM1B ubiquitin ligase.Nat Commun.,2024,15(1):3558.
- Molecular basis for METTL9-mediated N1-histidine methylation.Cell Discovery,2023,9(1):38.
- Structural basis for Gemin5 decamer-mediated mRNA binding.Nat. Commun.,2022,13(1):5166.
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