The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
O-GlcNAc signalling: implications for cancer cell biology
Open accessAbstract
O-GlcNAcylation is the covalent attachment of β-D-N-acetylglucosamine (GlcNAc) sugars to serine or threonine residues of nuclear and cytoplasmic proteins, and it is involved in extensive crosstalk with other post-translational modifications, such as phosphorylation. O-GlcNAcylation is becoming increasing realized as having important roles in cancer-relevant processes, such as cell signalling, transcription, cell division, metabolism and cytoskeletal regulation. However, currently little is known about the specific roles of aberrant O-GlcNAcylation in cancer. In this Opinion article, we summarize the current understanding of O-GlcNAcylation in cancer and its emerging functions in transcriptional regulation at the level of chromatin and transcription factors.
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Citations
Cites
Hallmarks of Cancer: The Next Generation
Hanahan, D., & Weinberg, R. A. (2011) · Cell · doi:10.1016/j.cell.2011.02.013 · Cited by 66,590
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
Self-citationRescue of embryonic lethality in Mdm2-deficient mice by absence of p53
Jones, S. N., Roe, A. E., Donehower, L. A., & Bradley, A. (1995) · Nature · doi:10.1038/378206a0 · Cited by 1,280 · cited 1×
“Owing to the pivotal role of p53 in maintaining genomic integrity, p53 is tightly regulated by proteolytic degradatio”
BackgroundChou, T.-Y., Hart, G. W., & Dang, C. V. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.32.18961 · Cited by 453
Self-citationBrady, C. A., & Attardi, L. D. (2010) · Journal of Cell Science · doi:10.1242/jcs.064501 · Cited by 403
O-GlcNAc signaling: a metabolic link between diabetes and cancer?
Slawson, C., Copeland, R. J., & Hart, G. W. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.04.005 · Cited by 346
Self-citationEssential Role of the Glycosyltransferase Sxc/Ogt in Polycomb Repression
Gambetta, M. C., Oktaba, K., & Müller, J. (2009) · Science · doi:10.1126/science.1169727 · Cited by 315
Cited by
Protein Glycosylation in Cancer
Stowell, S. R., Ju, T., & Cummings, R. D. (2015) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev-pathol-012414-040438 · Cited by 873
TET2 and TET3 regulate GlcNAcylation and H3K4 methylation through OGT and SET1/COMPASS
Deplus, R., Delatte, B., Schwinn, M. K., Defrance, M., Méndez, J., Murphy, N., Dawson, M. A., Volkmar, M., Putmans, P., Calonne, E., et al. (2013) · The EMBO Journal · doi:10.1038/emboj.2012.357 · Cited by 486
The role of the unfolded protein response in cancer progression: From oncogenesis to chemoresistance
Madden, E., Logue, S. E., Healy, S. J., Manie, S., & Samali, A. (2019) · Biology of the Cell · doi:10.1111/boc.201800050 · Cited by 359
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
Glutamine Links Obesity to Inflammation in Human White Adipose Tissue
Petrus, P., Lecoutre, S., Dollet, L., Wiel, C., Sulen, A., Gao, H., Tavira, B., Laurencikiene, J., Rooyackers, O., Checa, A., et al. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2019.11.019 · Cited by 254
Metadata
- Authors
- Slawson, C., & Hart, G. W.
- Venue
- Nature Reviews Cancer
- Published
- 2011-08-18
- Volume
- 11
- Issue
- 9
- Pages
- 678-684
- ISSN
- 1474-175X (ISSN-L)
- 1474-1768
- OpenAlex
- W2056173710
- Cited by
- 458
- References
- 7
- FWCI
- 1.56
- Type
- journal article
- Language
- en
- Open access
- green
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.