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He received a Ph.D. under the direction of Dr. Michael B. Goshe at North Carolina State University in September 2008. My Ph.D. thesis research focused on developing novel chemical reagents and associated methodologies to study protein structure and protein-protein interactions using mass spectrometry. Since joining the Proteomics and Metabolomics Shared Resource in 2008, I have been involved in a broad range of research efforts from small scale basic science research projects to large clinical scale proteomic studies.
His research One area that he particularly interested in is the use of mass spectrometry to characterize protein post-translational modifications such as phosphorylation. After joining the Proteomics and Metabolomics Shared Resource, He was tasked with developing a sensitive, reproducible, and quantitative LC-MS based phosphoproteomic platform capable of measuring global phosphorylation events from cultured cells, biological fluids and tissue. Those developments included TiO2 based phosphopeptide enrichment protocols, modified Waters NanoAcquity UPLC methods tailored to the analysis of phosphorylated peptides, and MS acquisition strategies capable of accurately sequencing phosphorylated peptides. To date, the platform has been applied to over eighteen large scale global quantitative phosphoproteomics studies.
Research Article: Adv Mol Diag 2016, 1: 109
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