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Aberrant protein glycosylation in human disease

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Losfeld, M. E., F. Soncin, et al. “ A Sensitive Green Fluorescent Protein Biomarker of N-glycosylation Site Occupancy.” FASEB Journal 26, no. 10 (2012): 4210–17.

Mir, A., N. Gao, et al. “ A Zebrafish Model of Congenital Disorders of Glycosylation with Phosphomannose Isomerase Deficiency Reveals an Early Opportunity for Corrective Mannose Supplementation.” Disease Models & Mechanisms 6, no. 1 (2013): 95–105.


Imaging glycan patterns in developing embryos

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Baskin, J. M.,  K. W. Dehnert, et al. “Visualizing Enveloping Layer Glycans during Zebrafish Early Embryogenesis.” Proceedings of the National Academy of Sciences 107, no. 23 (2010): 10360–65.

Beahm, B. J., K. W. Dehnert, et al. “ A Visualizable Chain-terminating Inhibitor of Glycosaminoglycan Biosynthesis in Developing Zebrafish.” Angewandte Chemie International Edition 53, no. 13 (2014): 3347–52.


The role of protein glycosylation in bacterial motility

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Ewing, C. P., E. Andreischcheva, et al. “ Functional Characterization of Flagellin Glycosylation in Campylobacter Jejuni 81–176.” Journal of Bacteriology 191, no. 22 (2009): 7086–93.

Liu, F., A. J. Aubry, et al. “ The Engineering of Bacteria Bearing Azido-pseudaminic Acid-modified Flagella.” Chembiochem 10, no. 8 (2009): 1317–20.


Engineering bacteria for glycoprotein production

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Wacker, M., D. Linton, et al. “ N-linked Glycosylation in Campylobacter Jejuni and its Functional Transfer into E. coli.” Science 298, no. 5599 (2002): 1790–93.

Valderrama-Rincon, J. D., A. C. Fisher, et al. “ An Engineered Eukaryotic Protein Glycosylation Pathway in Escherichia coli.” Nature Chemical Biology 8, no. 5 (2012): 434–6.


Chemical strategies for glycoprotein production

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Hang, Z., J. Gildersleeve, et al. “ A New Strategy for the Synthesis of Glycoproteins.” Science 303, no. 5656 (2004): 371–3.

Van Kasteren, Sander I, H. B. Kramer, et al. “ Expanding the Diversity of Chemical Protein Modification Allows Post-translational Mimicry.” Nature 446, no. 7139 (2007): 1105–9.


Development and application of glycan arrays

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Blixt, O., S. Head, et al. “ Printed Covalent Glycan Array for Ligand Profiling of Diverse Glycan Binding Proteins.” Proceedings of the National Academy of Sciences 101, no. 49 (2004): 17033–8.

Hung, T. -C., C.-W. Lin, et al. “ Investigation of SSEA-4 Binding Protein in Breast Cancer Cells.” Journal of the American Chemical Society 135, no. 16 (2013): 5934–7.


Metabolic glycan labeling in cancer

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Neves, A. A., H. Stöckmann, et al. “ Imaging Cell Surface Glycosylation in Vivo using “Double Click” Chemistry.” Bioconjugate Chemistry 24, no. 6 (2013): 934–41.

Furumoto, S., R. Shinbo, et al. “ In Vitro and in Vivo Characterization of 2-deoxy-2-18F-fluoro-D-mannose as a Tumor-imaging Agent for PET.” Journal Nuclear  Medicine 54, no. 8 (2013): 1354–61.


Glycan-based synthetic vaccines

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Broecker, F., J. Aretz, et al. “ Epitope Recognition of Antibodies against a Yersinia Pestis Lipopolysaccharide Trisaccharide Component.” ACS Chemical Biology 9, no. 4 (2014): 867–73.

Lakshminarayanan, V., P. Thompson, et al. “ Immune Recognition of Tumor-associated Mucin MUC1 is Achieved by a Fully Synthetic Aberrantly Glycosylated MUC1 Tripartite Vaccine.” Proceedings of the National Academy of Sciences 109, no.1 (2012): 261–6.


A close look at influenza–host interactions

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Zhang, W., Y. Shi, et al. “ An Airborne Transmissible Avian Influenza H5 Hemagglutinin seen at the Atomic Level.” Science 340, no. 6139 (2013): 1463–7.

Connaris, H., E. A. Govorkova, et al. “ Prevention of Influenza by Targeting Host Receptors using Engineered Proteins.” Proceedings of the National Academy of Sciences 111, no. 17 (2014): 6401–6.


Synthetic antigens to generate HIV vaccines

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Wang, S. -K., P. -H. Liang, et al. “ Targeting the Carbohydrates on HIV-1: Interaction of Oligomannose Dendrons with Human Monoclonal Antibody 2G12 and DC-SIGN.” Proceedings of the National Academy of Sciences 105, no. 10 (2007): 3690–95.

Doores, K. J., Z. Fulton, et al. “ A Nonself Sugar Mimic of the HIV Glycan Shield Shows Enhanced Antigenicity.” Proceedings of the National Academy of Sciences 107, no. 40 (2010): 17107–12.


The role of sugar metabolites in diabetes

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Clark, P. M., J. F. Dweck, et al. “ Direct In-gel Fluorescence Detection and Cellular Imaging of O-GlcNAc-modified Proteins.” Journal of the American Chemical Society 130_,_ no. 35 (2008): 11576–7.

Wang, Z., K. Park, et al. “ Site-specific GlcNAcylation of Human Erythrocyte Proteins – Potential Biomarker(s) for Diabetes.” Diabetes 58, no. 2 (2009): 309–17.



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