The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Protein O-GlcNAcylation: emerging mechanisms and functions
Open accessAbstract
O-GlcNAcylation — the attachment of O-linked N-acetylglucosamine (O-GlcNAc) moieties to cytoplasmic, nuclear and mitochondrial proteins — is a post-translational modification that regulates fundamental cellular processes in metazoans. A single pair of enzymes — O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) — controls the dynamic cycling of this protein modification in a nutrient- and stress-responsive manner. Recent years have seen remarkable advances in our understanding of O-GlcNAcylation at levels that range from structural and molecular biology to cell signalling and gene regulation to physiology and disease. New mechanisms and functions of O-GlcNAcylation that are emerging from these recent developments enable us to begin constructing a unified conceptual framework through which the significance of this modification in cellular and organismal physiology can be understood.
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Cites
Cycling of O-linked β-N-acetylglucosamine on nucleocytoplasmic proteins
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Role of TET enzymes in DNA methylation, development, and cancer
Rasmussen, K. D., & Helin, K. (2016) · Genes & Development · doi:10.1101/gad.276568.115 · Cited by 1,040
linking metabolism to epigenetics through O-GlcNAcylation
Hanover, J. A., Krause, M. W., & Love, D. C. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3334 · Cited by 414
Essential Role of the Glycosyltransferase Sxc/Ogt in Polycomb Repression
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O-GlcNAc Transferase Enables AgRP Neurons to Suppress Browning of White Fat
Ruan, H.-B., Dietrich, M. O., Liu, Z.-W., Zimmer, M. R., Li, M.-D., Singh, J. P., Zhang, K., Yin, R., Wu, J., Horvath, T. L., et al. (2014) · Cell · doi:10.1016/j.cell.2014.09.010 · Cited by 281
Self-citationO-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
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Self-citationMetabolic reprogramming and epigenetic modifications on the path to cancer
Sun, L., Zhang, H., & Gao, P. (2022) · Protein & Cell · doi:10.1007/s13238-021-00846-7 · Cited by 770
Click Chemistry in Proteomic Investigations
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Metadata
- Authors
- Yang, X., & Qian, K.
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2017-05-10
- Volume
- 18
- Issue
- 7
- Pages
- 452-465
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- OpenAlex
- W2613539552
- Cited by
- 1,194
- References
- 6
- FWCI
- 6.05
- Type
- journal article
- Language
- en
- Open access
- green
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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.
