The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Emerging Role of α2,6-Sialic Acid as a Negative Regulator of Galectin Binding and Function
Open accessAbstract
Galectins are β-galactoside-binding lectins that regulate diverse cell behaviors, including adhesion, migration, proliferation, and apoptosis. Galectins can be expressed both intracellularly and extracellularly, and extracellular galectins mediate their effects by associating with cell-surface oligosaccharides. Despite intensive current interest in galectins, strikingly few studies have focused on a key enzyme that acts to inhibit galectin signaling, namely β-galactoside α2,6-sialyltransferase (ST6Gal-I). ST6Gal-I adds an α2,6-linked sialic acid to the terminal galactose of N-linked glycans, and this modification blocks galectin binding to β-galactosides. This minireview summarizes the evidence suggesting that ST6Gal-I activity serves as an "off switch" for galectin function.
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Cites
Anti-Inflammatory Activity of Immunoglobulin G Resulting from Fc Sialylation
Kaneko, Y., Nimmerjahn, F., & Ravetch, J. V. (2006) · Science · doi:10.1126/science.1129594 · Cited by 1,754
Lau, K. S., Partridge, E. A., Grigorian, A., Silvescu, C. I., Reinhold, V. N., Demetriou, M., & Dennis, J. W. (2007) · Cell · doi:10.1016/j.cell.2007.01.049 · Cited by 914
Toscano, M. A., Bianco, G. A., Ilarregui, J. M., Croci, D. O., Correale, J., Hernandez, J. D., Zwirner, N. W., Poirier, F., Riley, E. M., Baum, L. G., et al. (2007) · Nature Immunology · doi:10.1038/ni1482 · Cited by 653
Galectin–glycan lattices regulate cell-surface glycoprotein organization and signalling
Garner, O. B., & Baum, L. G. (2008) · Biochemical Society Transactions · doi:10.1042/bst0361472 · Cited by 226
Cited by
Varki, A. (2017) · Glycobiology · doi:10.1093/glycob/cww086 · Cited by 2,635
“Complexity arises because capping of polylactosaminoglycans by sialic acids can modulate galectin recognition by its presence and or linkage type (618) (619) (620) (621) (622) .”
BackgroundGlycosylation: mechanisms, biological functions and clinical implications
He, M., Zhou, X., & Wang, X. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01886-1 · Cited by 499
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
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
Reiding, K. R., Blank, D., Kuijper, D. M., Deelder, A. M., & Wuhrer, M. (2014) · Analytical Chemistry · doi:10.1021/ac500335t · Cited by 334
Metadata
- Authors
- Zhuo, Y., & Bellis, S. L.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2011-02
- Volume
- 286
- Issue
- 8
- Pages
- 5935-5941
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2046555998
- Cited by
- 174
- References
- 4
- FWCI
- 3.86
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Zhuo, Y., & Bellis, S. L. (2011). Emerging Role of α2,6-Sialic Acid as a Negative Regulator of Galectin Binding and Function. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.r110.191429
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