The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Regulation of the metastatic cell phenotype by sialylated glycans
Open accessAbstract
Tumor cells exhibit striking changes in cell surface glycosylation as a consequence of dysregulated glycosyltransferases and glycosidases. In particular, an increase in the expression of certain sialylated glycans is a prominent feature of many transformed cells. Altered sialylation has long been associated with metastatic cell behaviors including invasion and enhanced cell survival; however, there is limited information regarding the molecular details of how distinct sialylated structures or sialylated carrier proteins regulate cell signaling to control responses such as adhesion/migration or resistance to specific apoptotic pathways. The goal of this review is to highlight selected examples of sialylated glycans for which there is some knowledge of molecular mechanisms linking aberrant sialylation to critical processes involved in metastasis.
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Liu, Y.-C., Yen, H.-Y., Chen, C.-Y., Chen, C.-H., Cheng, P.-F., Juan, Y.-H., Chen, C.-H., Khoo, K.-H., Yu, C.-J., Yang, P.-C., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1107385108 · Cited by 424
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
Cosmc is an essential chaperone for correct protein O-glycosylation
Wang, Y., Ju, T., Ding, X., Xia, B., Wang, W., Xia, L., He, M., & Cummings, R. D. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0914004107 · Cited by 212
Hinek, A., Pshezhetsky, A. V., von Itzstein, M., & Starcher, B. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m508736200 · Cited by 176
Cited by
Global view of human protein glycosylation pathways and functions
Schjoldager, K. T., Narimatsu, Y., Joshi, H. J., & Clausen, H. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-00294-x · Cited by 1,309
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
Emerging principles for the therapeutic exploitation of glycosylation
Dalziel, M., Crispin, M., Scanlan, C. N., Zitzmann, N., & Dwek, R. A. (2014) · Science · doi:10.1126/science.1235681 · Cited by 447
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
- Schultz, M. J., Swindall, A. F., & Bellis, S. L.
- Venue
- Cancer and Metastasis Reviews
- Published
- 2012-06-15
- Volume
- 31
- Issue
- 3-4
- Pages
- 501-518
- ISSN
- 0167-7659 (ISSN-L)
- 1573-7233
- OpenAlex
- W1967907911
- Cited by
- 303
- References
- 5
- FWCI
- 0.99
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Schultz, M. J., Swindall, A. F., & Bellis, S. L. (2012). Regulation of the metastatic cell phenotype by sialylated glycans. Cancer and Metastasis Reviews. https://doi.org/10.1007/s10555-012-9359-7
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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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