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- Lionel Pereira receives Faculty of Science Graduate Student Excellence in Teaching Award
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Vocadlo Lab
We create new chemical and biochemical probes of glycan processing enzymes and use these to evaluate the roles of interesting glycoconjugates in cellular processes and diseases.
Cells from all domains of life are coated in glycans that are composed of distinct carbohydrate building blocks. The interdisciplinary laboratory of chemical glycobiology works at this frontier area of molecular biology to explore the functional roles of glycans in cell and organismal physiology. As part of this effort we study; (i) carbohydrate processing enzymes that act on glycans, (ii) develop chemical and biochemical tools to both perturb the action of these enzymes as well as to monitor glycans, and (iii) the use of these chemical tools to gain new understanding of how these glycans regulate cellular and organismal physiology. Members of the laboratory work as a team to address new problems in the area of glycobiology and come from different backgrounds including, for example, chemistry, biochemistry, and cell biology.
For more details, visit our .
Selected Publications
- Zhu Y, Shan X, Safarpour F, Erro Go N, Li N, Shan A, Huang MC, Deen M, Holicek V, Ashmus R, Madden Z, Gorski S, Silverman MA, Vocadlo DJ*, Pharmacological inhibition of O-GlcNAcase (OGA) enhances autophagy in brain through an mTOR-independent pathway.
- Liu T-W, Myschyshyn M, Sinclair DA, Cecioni S, Beja K, Honda BM, Morin RD, Vocadlo DJ* Genome-wide chemical mapping of O-GlcNAcylated proteins in Drosophila.
- Cecioni S, Vocadlo DJ.* Carbohydrate bis-acetal-based substrates as tunable fluorescence-quenched probes for monitoring exo-glycosidase activity.
- Zhu, Y., Liu, T., Madden Z., Yuzwa, S.A., Murray, K., Cecioni, S., Zachara, N., Vocadlo, D.J.* Post-translational O-GlcNAcylation is essential for nuclear pore integrity and maintenance of the pore selectivity filter.
- Zhu Y, Liu TW, Cecioni S, Eskandari R, Zandberg WF, Vocadlo DJ.* O-GlcNAc occurs cotranslationally to stabilize nascent polypeptide chains.
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