My laboratory is focused on understanding the role that post-translational modifications, specifically glycosylation, play in increasing functional diversity of proteins. For the last 16 years, my lab has primarily focused on the biomedical significance of O-glycosylation, specifically the nutrient-sensing O-GlcNAc modification of nuclear and cytosolic proteins and the O-mannosylation pathway that is defective in many cases of congenital muscular dystrophy. The laboratory also has extensive experience in analytical mass spectrometry and the development/application of glycomic and glycoproteomic capture, identification, and quantification approaches. I serve as a Co-Director of the ThermoFisher Scientific appointed center of excellence in glycoproteomics that allows my laboratory to interact at both the software and hardware level with a leading instrument manufacturer to drive technology developments like those outlined in this proposal.

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