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We are exploring chemistry and biology of protein modifications

Ubiquitination in stress response and adaptation

In ever-changing environments, cells confront a myriad of stressors. While increased ubiquitination is known as a typical cellular stress response, the mechanisms by which ubiquitination tailors cellular response to each unique stress remain unclear. We will leverage a proteomics approach and chemical biology tools to delineate the stress-induced ubiquitination across the proteome and determine its interplay with other protein modifications and cellular pathways.

E3 ligase biology and protein aging

Despite the increasing significance of E3 ligases in drug discovery, many of these enzymes have yet to have their natural substrate recognition mechanisms uncovered. Drawing inspirations from the chemistry and biology of protein modifications, we will reveal the natural recognition motifs of E3 ligases, termed degrons, and delve into their biological implications in protein aging and other essential biological processes.

Non-enzymatic modifications in human biology 

Growing evidence implies as-yet-unknown modes of regulation by non-enzymatic post-translational modifications (PTMs) in broad cellular processes. We will develop approaches to characterize their sites and interactome, aiming to expand the landscape of the biology controlled by non-enzymatic PTMs and explore their potential as diagnostic tools, biomarkers, or treatment targets.

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