ArticleAnalytical chemistry2020
A Chemoenzymatic Method Based on Easily Accessible Enzymes for Profiling Protein O-GlcNAcylation.
Article in Analytical chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Mass Spectrometry-Based Proteomics Methods for Systematic Identification and Quantification of Protein O-Glycosylation in Complex Biological Samples.Journal of the American Society for Mass Spectrometry · 2026Review
- Isotopic Labeling-Enabled Chemical Proteomics Analysis Revealed Structural and Functional Features of Allysine Modifications in Mammalian Cells and Tissues.Analytical chemistry · 2025Article
- Article
- Ultradeep O-GlcNAc proteomics reveals widespread O-GlcNAcylation on tyrosine residues of proteins.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Systematic Evaluation of Affinity Enrichment Methods for O-GlcNAc Proteomics.Journal of proteome research · 2024Article
- Combining Selective Enrichment and a Boosting Approach to Globally and Site-Specifically Characterize Protein Co-translationalAnalytical chemistry · 2023Article
- Systematic characterization of extracellular glycoproteins using mass spectrometry.Mass spectrometry reviews · 2023Review
- Recent development of analytical methods for disease-specific proteinRSC advances · 2022Review
- Design and Preparation of Novel Nitro-Oxide-Grafted Nanospheres with Enhanced Hydrogen Bonding Interaction forACS applied materials & interfaces · 2022Article
- Advances in chemical probing of proteinChemical Society reviews · 2021Review
- Increasing O-GlcNAcylation is neuroprotective in young and aged brains after ischemic stroke.Experimental neurology · 2021Article
- Towards structure-focused glycoproteomics.Biochemical Society transactions · 2021Review
- A Pragmatic Guide to Enrichment Strategies for Mass Spectrometry-Based Glycoproteomics.Molecular & cellular proteomics : MCP · 2021Review
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Authors and funding
3 authors.
Funding
Abstract
O-GlcNAcylation has gradually been recognized as a critically important protein post-translational modification in mammalian cells. Besides regulation of gene expression, its crosstalk with protein phosphorylation is vital for cell signaling. Despite its importance, comprehensive analysis of O-GlcNAcylation is extraordinarily challenging due to the low abundances of many O-GlcNAcylated proteins and the complexity of biological samples. Here, we developed a novel chemoenzymatic method based on a wild-type galactosyltransferase and uridine diphosphate galactose (UDP-Gal) for global and site-specific analysis of protein O-GlcNAcylation. This method integrates enzymatic reactions and hydrazide chemistry to enrich O-GlcNAcylated peptides. All reagents used are more easily accessible and cost-effective as compared to the engineered enzyme and click chemistry reagents. Biological triplicate experiments were performed to validate the effectiveness and the reproducibility of this method, and the results are comparable with the previous chemoenzymatic method using the engineered enzyme and click chemistry. Moreover, because of the promiscuity of the galactosyltransferase, 18 unique O-glucosylated peptides were identified on the EGF domain from nine proteins. Considering that effective and approachable methods are critical to advance glycoscience research, the current method without any sample restrictions can be widely applied for global analysis of protein O-GlcNAcylation in different samples.
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