The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Hijacking a biosynthetic pathway yields a glycosyltransferase inhibitor within cells
Open accessAbstract
Glycosyltransferases (GTs) are ubiquitous enzymes that catalyze the assembly of glycoconjugates found throughout all kingdoms of nature. A longstanding problem is the rational design of probes that can be used to manipulate GT activity in cells and tissues. Here we describe the rational design and synthesis of a nucleotide sugar analogue that inhibits, with high potency both in vitro and in cells, the human GT responsible for the reversible post-translational modification of nucleocytoplasmic proteins with O-linked N-acetylglucosamine residues (O-GlcNAc). We show the enzymes of the hexosamine biosynthetic pathway can transform, both in vitro and in cells, a synthetic carbohydrate precursor into the nucleotide sugar analogue. Treatment of cells with the precursor decreases O-GlcNAc in a targeted manner with a single digit micromolar EC50. This approach to inhibition of GTs should be applicable to other members of this increasingly interesting superfamily of enzymes and enable their manipulation in a biological setting.
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Cites
Varki, A. (2017) · Glycobiology · doi:10.1093/glycob/cww086 · Cited by 2,635
Cycling of O-linked β-N-acetylglucosamine on nucleocytoplasmic proteins
Hart, G. W., Housley, M. P., & Slawson, C. (2007) · Nature · doi:10.1038/nature05815 · Cited by 1,418
O-GlcNAcylation regulates phosphorylation of tau: A mechanism involved in Alzheimer's disease
Liu, F., Iqbal, K., Grundke-Iqbal, I., Hart, G. W., & Gong, C.-X. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400348101 · Cited by 775
Suppression of tumor growth and metastasis in Mgat5-deficient mice
Granovsky, M., Fata, J., Pawling, J., Muller, W. J., Khokha, R., & Dennis, J. W. (2000) · Nature Medicine · doi:10.1038/73163 · Cited by 569
Cited by
A Small Molecule That Inhibits OGT Activity in Cells
Ortiz-Meoz, R. F., Jiang, J., Lazarus, M. B., Orman, M., Janetzko, J., Fan, C., Duveau, D. Y., Tan, Z.-W., Thomas, C. J., & Walker, S. (2015) · ACS Chemical Biology · doi:10.1021/acschembio.5b00004 · Cited by 294
Unmasking Fucosylation: from Cell Adhesion to Immune System Regulation and Diseases
Li, J., Hsu, H.-C., Mountz, J. D., & Allen, J. G. (2018) · Cell Chemical Biology · doi:10.1016/j.chembiol.2018.02.005 · Cited by 256
O-GlcNAc occurs cotranslationally to stabilize nascent polypeptide chains
Zhu, Y., Liu, T.-W., Cecioni, S., Eskandari, R., Zandberg, W. F., & Vocadlo, D. J. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1774 · Cited by 134
Self-citationSystemic Blockade of Sialylation in Mice with a Global Inhibitor of Sialyltransferases
Macauley, M. S., Arlian, B. M., Rillahan, C. D., Pang, P.-C., Bortell, N., Marcondes, M. C. G., Haslam, S. M., Dell, A., & Paulson, J. C. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.606517 · Cited by 129
O-GlcNAc regulates gene expression by controlling detained intron splicing
Tan, Z.-W., Fei, G., Paulo, J. A., Bellaousov, S., Martin, S. E. S., Duveau, D. Y., Thomas, C. J., Gygi, S. P., Boutz, P. L., & Walker, S. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa263 · Cited by 119
Metadata
- Authors
- Gloster, T. M., Zandberg, W. F., Heinonen, J. E., Shen, D. L., Deng, L., & Vocadlo, D. J.
- Venue
- Nature Chemical Biology
- Published
- 2011-01-23
- Volume
- 7
- Issue
- 3
- Pages
- 174-181
- ISSN
- 1552-4450 (ISSN-L)
- 1552-4469
- OpenAlex
- W1998906741
- Cited by
- 335
- References
- 4
- FWCI
- 11.82
- Type
- journal article
- Language
- en
- Open access
- green
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- Gloster, T. M., Zandberg, W. F., Heinonen, J. E., Shen, D. L., Deng, L., & Vocadlo, D. J. (2011). Hijacking a biosynthetic pathway yields a glycosyltransferase inhibitor within cells. Nature Chemical Biology. https://doi.org/10.1038/nchembio.520
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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