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Our laboratory investigates how molecular interactions regulate protein function and contribute to disease. Using mass spectrometry–based proteomics, chemoproteomics, and biochemical approaches, we identify protein–protein and protein–small-molecule interactions and determine how microbial and metabolic factors alter protein activity, stability, post-translational modifications, and signaling. We use these mechanistic insights to identify therapeutic targets and develop chemical probes and targeted protein degraders.
Molecular Interactions
Molecular Interactions
We identify the molecular interactions that regulate protein function. Using affinity enrichment, chemical pulldown, proximity labeling, and high resolution mass spectrometry, we determine which proteins and small molecules bind, where these interactions occur, and how they affect protein activity, stability, localization, or degradation.
Microbial and Metabolic Regulation
Microbial and Metabolic Regulation
We study how microbial proteins and metabolic signals alter host protein function. Our work examines changes in protein interactions, stability, and post-translational modifications, and investigates how these molecular changes contribute to inflammation, impaired proteostasis, and neurodegenerative disease.
Chemical Biology and Targeted Protein Degradation
Chemical Biology and Targeted Protein Degradation
We discover ligands for underexplored E3 ubiquitin ligases and develop them into chemical probes and targeted protein degraders. We validate direct target engagement, map binding sites, test E3 ligase-dependent degradation, and use quantitative proteomics to determine the mechanisms and selectivity of prioritized compounds.
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