ArticleACS chemical biology2017
Direct Monitoring of Protein O-GlcNAcylation by High-Resolution Native Mass Spectrometry.
Article in ACS chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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Who cites it
12 citing papers in PubMed, 25 citations in OpenAlex.
- State-of-the-Art and Future Directions in Structural Proteomics.Molecular & cellular proteomics : MCP · 2025Review
- Quantifying the Impact of the Peptide Identification Framework on the Results of Fast Photochemical Oxidation of Protein Analysis.Journal of proteome research · 2024Article
- Writing and Erasing O-GlcNAc on Casein Kinase 2 Alpha Alters the Phosphoproteome.ACS chemical biology · 2022Article
- Structural O-Glycoform Heterogeneity of the SARS-CoV-2 Spike Protein Receptor-Binding Domain Revealed by Top-Down Mass Spectrometry.Journal of the American Chemical Society · 2021Article
- O-GlcNAcylation in Hyperglycemic Pregnancies: Impact on Placental Function.Frontiers in endocrinology · 2021Review
- A Pragmatic Guide to Enrichment Strategies for Mass Spectrometry-Based Glycoproteomics.Molecular & cellular proteomics : MCP · 2021Review
- Native detection of proteinThe Analyst · 2020Article
- New Insights Into the Biology of Protein O-GlcNAcylation: Approaches and Observations.Frontiers in aging · 2020Article
- Too sweet to resist: Control of immune cell function by O-GlcNAcylation.Cellular immunology · 2018Review
- Glycosylation profiling to evaluate glycoprotein immunogens against HIV-1.Expert review of proteomics · 2017Review
- Elucidating crosstalk mechanisms between phosphorylation and O-GlcNAcylation.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- The Role of Stress-Induced O-GlcNAc Protein Modification in the Regulation of Membrane Transport.Oxidative medicine and cellular longevity · 2017Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
O-GlcNAcylation is one of the most abundant metazoan nuclear-cytoplasmic post-translational modifications. Proteins modified by O-GlcNAc play key cellular roles in signaling, transcription, metabolism, and cell division. Mechanistic studies on protein O-GlcNAcylation are hampered by the lack of methods that can simultaneously quantify O-GlcNAcylation, determine its stoichiometry, and monitor O-GlcNAcylation kinetics. Here, we demonstrate that high-resolution native mass spectrometry can be employed to monitor the small mass shifts induced by modification by O-GlcNAc on two known protein substrates, CK2α and TAB1, without the need for radioactive labeling or chemoenzymatic tagging using large mass tags. Limited proteolysis enabled further localization of the O-GlcNAc sites. In peptide-centric MS analysis, the O-GlcNAc moiety is known to be easily lost. In contrast, we demonstrate that the O-GlcNAc is retained under native MS conditions, enabling precise quantitative analysis of stoichiometry and O-GlcNAcylation kinetics. Together, the data highlight that high resolution native MS may provide an alternative tool to monitor kinetics on one of the most labile of protein post-translational modifications, in an efficient, reliable, and quantitative manner.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.