ArticleJournal of the American Chemical Society2014
Changes in metabolic chemical reporter structure yield a selective probe of O-GlcNAc modification.
Article in Journal of the American Chemical Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 66 papers.
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Who cites it
66 citing papers in PubMed.
- Bioorthogonal Click Chemistry for Antibody-Free Profiling of Acetylation, Propionylation, and Butyrylation inACS infectious diseases · 2026Article
- Chemoenzymatic Synthesis and Purification of Bioorthogonally Tagged UDP-GlcNAc and UDP-GalNAc Analogues.Current protocols · 2025Article
- C-6-Modified 2-F-Fucose Derivatives as Inhibitors of Fucosyltransferases.Chembiochem : a European journal of chemical biology · 2025Article
- RENBP inhibition amplifies metabolic glycan labeling efficiency of antigen-presenting cells in vitro and in vivo.Cell chemical biology · 2025Article
- Selective bioorthogonal probe for N-glycan hybrid structures.Nature chemical biology · 2025Article
- Engineered Proteins and Chemical Tools to Probe the Cell Surface Proteome.Chemical reviews · 2025Review
- Comprehensive Multi-Omics Analysis Identifies FUT1 as a Prognostic and Therapeutic Biomarker Across Pan-Cancer.International journal of medical sciences · 2025Article
- Metabolic Tagging Technology of Exosomes-An Updated Review.Current pharmaceutical design · 2025Review
- GlycoID Proximity Labeling to Identify O-GlcNAcylated Protein Interactomes in Live Cells.Current protocols · 2024Article
- Full-length single-molecule protein fingerprinting.Nature nanotechnology · 2024Article
- A bioorthogonal chemistry approach to detect the K1 polysialic acid capsule inRSC chemical biology · 2023Article
- Chemical Biology Approaches to Understanding Neuronal O-GlcNAcylation.Israel journal of chemistry · 2023Article
- Recent development of analytical methods for disease-specific proteinRSC advances · 2022Review
- Synthesis and mammalian cell compatibility of light-released glycan precursors for controlled metabolic engineering.Bioorganic & medicinal chemistry · 2022Article
- Tools for mammalian glycoscience research.Cell · 2022Review
- 4-Deoxy-4-fluoro-GalNAz (4FGalNAz) Is a Metabolic Chemical Reporter of O-GlcNAc Modifications, Highlighting the Notable Substrate Flexibility of O-GlcNAc Transferase.ACS chemical biology · 2022Article
- Anomeric Fatty Acid Functionalization Prevents NonenzymaticACS chemical biology · 2021Article
- Advances in chemical probing of proteinChemical Society reviews · 2021Review
- Chemical reporters to study mammalian O-glycosylation.Biochemical Society transactions · 2021Review
- Design and Synthesis of Metabolic Chemical Reporters for the Visualization and Identification of Glycoproteins.RSC chemical biology · 2021Article
6 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issued
Authors and funding
5 authors.
Funding
Abstract
Metabolic chemical reporters (MCRs) of glycosylation are analogues of monosaccharides that contain bioorthogonal functionalities and enable the direct visualization and identification of glycoproteins from living cells. Each MCR was initially thought to report on specific types of glycosylation. We and others have demonstrated that several MCRs are metabolically transformed and enter multiple glycosylation pathways. Therefore, the development of selective MCRs remains a key unmet goal. We demonstrate here that 6-azido-6-deoxy-N-acetyl-glucosamine (6AzGlcNAc) is a specific MCR for O-GlcNAcylated proteins. Biochemical analysis and comparative proteomics with 6AzGlcNAc, N-azidoacetyl-glucosamine (GlcNAz), and N-azidoacetyl-galactosamine (GalNAz) revealed that 6AzGlcNAc exclusively labels intracellular proteins, while GlcNAz and GalNAz are incorporated into a combination of intracellular and extracellular/lumenal glycoproteins. Notably, 6AzGlcNAc cannot be biosynthetically transformed into the corresponding UDP sugar-donor by the canonical salvage-pathway that requires phosphorylation at the 6-hydroxyl. In vitro experiments showed that 6AzGlcNAc can bypass this roadblock through direct phosphorylation of its 1-hydroxyl by the enzyme phosphoacetylglucosamine mutase (AGM1). Taken together, 6AzGlcNAc enables the specific analysis of O-GlcNAcylated proteins, and these results suggest that specific MCRs for other types of glycosylation can be developed. Additionally, our data demonstrate that cells are equipped with a somewhat unappreciated metabolic flexibility with important implications for the biosynthesis of natural and unnatural carbohydrates.
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