More than 70% of all proteins have sugars attached in the form of glycans including many therapeutics and antibodies. The nature of the attached glycan can influence the structure, function and stability of the attached protein. Indeed, many of the most valuable biopharmaceutical proteins are secreted and include N-glycans that may affect their function or pharmacological activity. The process of modifying and processing these sugars is one of the most important post-translational events to occur in eukaryotic cells with potentially major impacts on both biotechnology activity and disease. Our lab groups focuses on understanding these intracellular processing events from an experimental and modeling framework and we use this information to characterize the role of glycosylation in cell. We are also interested in metabolically engineering cells to change their glycosylation patterns. Such an engineered line may produce higher value products for the biotechnology industry.
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