ArticleThe Journal of biological chemistry2014
Antibodies that detect O-linked β-D-N-acetylglucosamine on the extracellular domain of cell surface glycoproteins.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
36 citing papers in PubMed, 58 citations in OpenAlex.
- O-GlcNAcylation at the tumor-immune interface: a metabolic post-translational code driving immune evasion and therapy resistance in cancer.Frontiers in immunology · 2026Review
- EOGT enables residual Notch signaling in mouse intestinal cells lacking POFUT1.Scientific reports · 2023Article
- Differential Detection of O-GlcNAcylated proteins in the heart using antibodies.Analytical biochemistry · 2023Article
- Recent development of analytical methods for disease-specific proteinRSC advances · 2022Review
- Recent Advances in the Rheumatic Fever and Rheumatic Heart Disease Continuum.Pathogens (Basel, Switzerland) · 2022Review
- Deciphering the Structure and Formation of Amyloids in Neurodegenerative Diseases With Chemical Biology Tools.Frontiers in chemistry · 2022Review
- Variation of ewe olfactory secretome during a ram effect.Frontiers in veterinary science · 2022Article
- How Nanotechniques Could Vitalize the O-GlcNAcylation-Targeting Approach for Cancer Therapy.International journal of nanomedicine · 2022Review
- Laminar Flow on Endothelial Cells Suppresses eNOS O-GlcNAcylation to Promote eNOS Activity.Circulation research · 2021Article
- Advances in chemical probing of proteinChemical Society reviews · 2021Review
- O-GlcNAcylated peptides and proteins for structural and functional studies.Current opinion in structural biology · 2021Review
- Detection and Analysis of Proteins Modified by O-Linked N-Acetylglucosamine.Current protocols · 2021Article
- Bioinformatics and Functional Analyses Implicate Potential Roles for EOGT and L-fringe in Pancreatic Cancers.Molecules (Basel, Switzerland) · 2021Article
- O-GlcNAcylation in Chronic Lymphocytic Leukemia and Other Blood Cancers.Frontiers in immunology · 2021Review
- Chemistry-Assisted Proteomic Profiling of O-GlcNAcylation.Frontiers in chemistry · 2021Review
- LDL receptor-related protein LRP6 senses nutrient levels and regulates Hippo signaling.EMBO reports · 2020Article
- Tools for functional dissection of site-specific O-GlcNAcylation.RSC chemical biology · 2020Review
- Article
- Rheumatic Heart Valve Disease Pathophysiology and Underlying Mechanisms.Frontiers in cardiovascular medicine · 2020Review
- New Insights Into the Biology of Protein O-GlcNAcylation: Approaches and Observations.Frontiers in aging · 2020Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The transfer of N-acetylglucosamine (GlcNAc) to Ser or Thr in cytoplasmic and nuclear proteins is a well known post-translational modification that is catalyzed by the O-GlcNAc transferase OGT. A more recently identified O-GlcNAc transferase, EOGT, functions in the secretory pathway and transfers O-GlcNAc to proteins with epidermal growth factor-like (EGF) repeats. A number of antibodies that detect O-GlcNAc in cytosolic and nuclear extracts have been described previously. Here we compare seven of these antibodies (CTD110.6, 10D8, RL2, HGAC85, 18B10.C7(#3), 9D1.E4(#10), and 1F5.D6 (#14) for detection of the O-GlcNAc modification on extracellular domains of membrane or secreted glycoproteins that may also carry various N- and O-glycans. We found that CTD110.6 binds not only to O-GlcNAc on proteins but also to terminal β-GlcNAc on the complex N-glycans of Lec8 Chinese hamster ovary (CHO) cells that lack UDP-Gal transporter activity and express GlcNAc-terminating, complex N-glycans. We show that CTD110.6, #3, and #10 antibodies can be used to detect cell surface glycoproteins bearing O-GlcNAc. Cell surface glycoproteins recognized by CTD110.6 antibody included NOTCH1 that possesses many EGF repeats with a consensus site for EOGT. Knockdown of CHO Eogt reduced binding of CTD110.6 to Lec1 CHO cells, and expression of a human EOGT cDNA increased the O-GlcNAc signal on Lec1 cells and the extracellular domain of NOTCH1. Thus, with careful controls, antibodies CTD110.6 (IgM), #3 (IgG), and #10 (IgG) can be used to detect membrane and secreted proteins modified by O-GlcNAc on EGF repeats.
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