The DOI matches its Crossref record; 59 of the 59 references it cites were found in a registry or an index.
Global metabolic inhibitors of sialyl- and fucosyltransferases remodel the glycome
Open accessAbstract
Despite the fundamental roles of sialyl- and fucosyltransferases in mammalian physiology, there are few pharmacological tools to manipulate their function in a cellular setting. Although fluorinated analogs of the donor substrates are well-established transition state inhibitors of these enzymes, they are not membrane permeable. By exploiting promiscuous monosaccharide salvage pathways, we show that fluorinated analogs of sialic acid and fucose can be taken up and metabolized to the desired donor substrate-based inhibitors inside the cell. Due to the existence of metabolic feedback loops, they also act to prevent the de novo synthesis of the natural substrates, resulting in a global, family-wide shutdown of sialyl- and/or fucosyltransferases and remodeling of cell surface glycans. As an example of the functional consequences, the inhibitors drastically reduce expression of the sialylated and fucosylated ligand Sialyl Lewis X on myeloid cells, resulting in loss of binding to selectins and impaired leukocyte rolling.
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Glycosyltransferases: Structures, Functions, and Mechanisms
Lairson, L. L., Henrissat, B., Davies, G. J., & Withers, S. G. (2008) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.76.061005.092322 · Cited by 2,079
GlycoWorkbench: A Tool for the Computer-Assisted Annotation of Mass Spectra of Glycans
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Self-citationFucose: biosynthesis and biological function in mammals
Becker, D. J., & Lowe, J. B. (2003) · Glycobiology · doi:10.1093/glycob/cwg054 · Cited by 930
Glycan-based interactions involving vertebrate sialic-acid-recognizing proteins
Varki, A. (2007) · Nature · doi:10.1038/nature05816 · Cited by 853
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A Genetic Approach to Mammalian Glycan Function
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Monocyte-Endothelial Cell Interactions in the Development of Atherosclerosis
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Self-citationA Potent and Highly Selective Inhibitor of Human α-1,3-Fucosyltransferase via Click Chemistry
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Immune regulation by the ST6Gal sialyltransferase
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Sialic acids sweeten a tumor's life
Büll, C., Stoel, M. A., den Brok, M. H., & Adema, G. J. (2014) · Cancer Research · doi:10.1158/0008-5472.can-14-0728 · Cited by 496
CD22 blockade restores homeostatic microglial phagocytosis in ageing brains
Pluvinage, J. V., Haney, M. S., Smith, B. A. H., Sun, J., Iram, T., Bonanno, L., Li, L., Lee, D. P., Morgens, D. W., Yang, A. C., et al. (2019) · Nature · doi:10.1038/s41586-019-1088-4 · Cited by 459
Insights into the role of sialylation in cancer progression and metastasis
Dobie, C., & Skropeta, D. (2021) · British Journal of Cancer · doi:10.1038/s41416-020-01126-7 · Cited by 348
Sialic acid-containing glycolipids mediate binding and viral entry of SARS-CoV-2
Nguyen, L., McCord, K. A., Bui, D. T., Bouwman, K. M., Kitova, E. N., Elaish, M., Kumawat, D., Daskhan, G. C., Tomris, I., Han, L., et al. (2022) · Nature Chemical Biology · doi:10.1038/s41589-021-00924-1 · Cited by 259
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
Metadata
- Authors
- Rillahan, C. D., Antonopoulos, A., Lefort, C. T., Sonon, R., Azadi, P., Ley, K., Dell, A., Haslam, S. M., & Paulson, J. C.
- Venue
- Nature Chemical Biology
- Published
- 2012-06-10
- Volume
- 8
- Issue
- 7
- Pages
- 661-668
- ISSN
- 1552-4450 (ISSN-L)
- 1552-4469
- OpenAlex
- W1982056508
- Cited by
- 447
- References
- 59
- FWCI
- 9.99
- Type
- journal article
- Language
- en
- Open access
- green
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