ArticlePloS one2017
WGA-based lectin affinity gel electrophoresis: A novel method for the detection of O-GlcNAc-modified proteins.
Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 23 citations in OpenAlex.
- O-GlcNAcylation Stimulation Modulates Na+/K+ ATPase and Improves Outcomes in Hemorrhagic Shock.MedComm · 2026Article
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- Dynamic O-GlcNAcylation governs long-range chromatin interactions in V(D)J recombination during early B-cell development.Cellular & molecular immunology · 2025Article
- Enzymatic Modulation of the Pulmonary Glycocalyx Enhances Susceptibility toAmerican journal of respiratory cell and molecular biology · 2024Article
- Optimization of glycopeptide enrichment techniques for the identification of clinical biomarkers.Expert review of proteomics · 2024Review
- JiangShi(): a widely distributed Mucin-like protein essential for Drosophila development.G3 (Bethesda, Md.) · 2022Article
- Disaccharide-tag for highly sensitive identification of O-GlcNAc-modified proteins in mammalian cells.PloS one · 2022Article
- Lectin affinity-based glycoproteome analysis of the developing xylem in poplar.Forestry research · 2022Article
- A Pragmatic Guide to Enrichment Strategies for Mass Spectrometry-Based Glycoproteomics.Molecular & cellular proteomics : MCP · 2021Review
- Native detection of proteinThe Analyst · 2020Article
- Naja annulifera Snake: New insights into the venom components and pathogenesis of envenomation.PLoS neglected tropical diseases · 2019Article
- Lectin nanoparticle assays for detecting breast cancer-associated glycovariants of cancer antigen 15-3 (CA15-3) in human plasma.PloS one · 2019Article
- Wheat Germ Agglutinin (WGA)-SDS-PAGE: A Novel Method for the Detection of O-GlcNAc-modified Proteins by Lectin Affinity Gel Electrophoresis.Bio-protocol · 2018Article
- Interplay Between Phosphorylation and O-GlcNAcylation of Sarcomeric Proteins in Ischemic Heart Failure.Frontiers in endocrinology · 2018Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Post-translational modification with O-linked β-N-acetylglucosamine (O-GlcNAc) occurs selectively on serine and/or threonine residues of cytoplasmic and nuclear proteins, and dynamically regulates their molecular functions. Since conventional strategies to evaluate the O-GlcNAcylation level of a specific protein require time-consuming steps, the development of a rapid and easy method for the detection and quantification of an O-GlcNAcylated protein has been a challenging issue. Here, we describe a novel method in which O-GlcNAcylated and non-O-GlcNAcylated forms of proteins are separated by lectin affinity gel electrophoresis using wheat germ agglutinin (WGA), which primarily binds to N-acetylglucosamine residues. Electrophoresis of cell lysates through a gel containing copolymerized WGA selectively induced retardation of the mobility of O-GlcNAcylated proteins, thereby allowing the simultaneous visualization of both the O-GlcNAcylated and the unmodified forms of proteins. This method is therefore useful for the quantitative detection of O-GlcNAcylated proteins.
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