ArticleJournal of the American Society for Mass Spectrometry2011
A novel two-stage tandem mass spectrometry approach and scoring scheme for the identification of O-GlcNAc modified peptides.
Article in Journal of the American Society for Mass Spectrometry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- O-GlcNAc informatics: advances and trends.Analytical and bioanalytical chemistry · 2025Review
- Methods for Enrichment and Assignment of N-Acetylglucosamine Modification Sites.Molecular & cellular proteomics : MCP · 2021Review
- A Tandem Mass Spectrometry Sequence Database Search Method for Identification of O-Fucosylated Proteins by Mass Spectrometry.Journal of proteome research · 2019Article
- O-GlcNAcylation of PERIOD regulates its interaction with CLOCK and timing of circadian transcriptional repression.PLoS genetics · 2019Article
- Combined Antibody/Lectin Enrichment Identifies Extensive Changes in the O-GlcNAc Sub-proteome upon Oxidative Stress.Journal of proteome research · 2016Article
- O-GlcNAc profiling: from proteins to proteomes.Clinical proteomics · 2014Article
- Proteome wide purification and identification of O-GlcNAc-modified proteins using click chemistry and mass spectrometry.Journal of proteome research · 2013Article
- Discovery of O-GlcNAc-modified proteins in published large-scale proteome data.Molecular & cellular proteomics : MCP · 2012Article
- Discovery of O-GlcNAc-6-phosphate modified proteins in large-scale phosphoproteomics data.Molecular & cellular proteomics : MCP · 2012Article
- Increasing the productivity of glycopeptides analysis by using higher-energy collision dissociation-accurate mass-product-dependent electron transfer dissociation.International journal of proteomics · 2012Article
Corrections and comments
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Authors and funding
2 authors.
Funding
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Abstract
The modification of serine and threonine residues in proteins by a single N-acetylglucosamine (O-GlcNAc) residue is an emerging post-translational modification (PTM) with broad biological implications. However, the systematic or large-scale analysis of this PTM is hampered by several factors, including low stoichiometry and the lability of the O-glycosidic bond during tandem mass spectrometry. Using a library of 72 synthetic glycopeptides, we developed a two-stage tandem MS approach consisting of pulsed Q dissociation (PQD) for O-GlcNAc peptide detection and electron transfer dissociation (ETD) for identification and site localization. Based on a set of O-GlcNAc specific fragment ions, we further developed a score (OScore) that discriminates O-GlcNAc peptide spectra from spectra of unmodified peptides with 95% sensitivity and >99% specificity. Integrating the OScore into the two-stage LC-MS/MS approach detected O-GlcNAc peptides in the low fmol range and at 10-fold better sensitivity than a single data-dependent ETD tandem MS experiment.
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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.