ArticleJournal of proteome research2011
Combining high-energy C-trap dissociation and electron transfer dissociation for protein O-GlcNAc modification site assignment.
Article in Journal of proteome research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.
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Who cites it
85 citing papers in PubMed, 159 citations in OpenAlex.
- Loss of O-GlcNAc transferase activity impairs the dynamic formation of protective stress granules in ischemic cardiomyocytes.The Biochemical journal · 2026Article
- Enhanced nuclear export caused by O-GlcNAcylation of nucleoporins is a potential therapeutic target in mesothelioma.British journal of cancer · 2026Article
- Improvements in Glycoproteomics through Architecture Changes to the Orbitrap Tribrid MS Platform.Analytical chemistry · 2025Article
- GATAD2B O-GlcNAcylation Regulates Breast Cancer Stem-like Potential and Drug Resistance.Cells · 2025Article
- O-GlcNAc informatics: advances and trends.Analytical and bioanalytical chemistry · 2025Review
- Pharmacologically increasing O-GlcNAcylation increases complexity of astrocytes in the dentate gyrus of TgF344-AD rats.Frontiers in aging neuroscience · 2025Article
- Autonomous Dissociation-type Selection for Glycoproteomics Using a Real-Time Library Search.Journal of proteome research · 2024Article
- 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
- Tissue-specificeLife · 2024Article
- OGT and OGA: Sweet guardians of the genome.The Journal of biological chemistry · 2024Review
- Molecular Mechanisms Linking Diabetes with Increased Risk of Thrombosis.International journal of molecular sciences · 2023Review
- Top/Middle-Down Characterization of α-Synuclein Glycoforms.Analytical chemistry · 2023Article
- Review
- Diagnostic utility of N-terminal TMPP labels for unambiguous identification of clipped sites in therapeutic proteins.Scientific reports · 2023Article
- Investigation of in vitro histone H3 glycosylation using H3 tail peptides.Scientific reports · 2022Article
- Design and Preparation of Novel Nitro-Oxide-Grafted Nanospheres with Enhanced Hydrogen Bonding Interaction forACS applied materials & interfaces · 2022Article
- Analysis of Viral Spike Protein N-Glycosylation Using Ultraviolet Photodissociation Mass Spectrometry.Analytical chemistry · 2022Article
- Mapping the O-GlcNAc Modified Proteome: Applications for Health and Disease.Frontiers in molecular biosciences · 2022Review
- The glycosylation in SARS-CoV-2 and its receptor ACE2.Signal transduction and targeted therapy · 2021Review
25 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Mass spectrometry-based studies of proteins that are post-translationally modified by O-linked β-N-acetylglucosamine (O-GlcNAc) are challenged in effectively identifying the sites of modification while simultaneously sequencing the peptides. Here we tested the hypothesis that a combination of high-energy C-trap dissociation (HCD) and electron transfer dissociation (ETD) could specifically target the O-GlcNAc modified peptides and elucidate the amino acid sequence while preserving the attached GlcNAc residue for accurate site assignment. By taking advantage of the recently characterized O-GlcNAc-specific IgG monoclonal antibodies and the combination of HCD and ETD fragmentation techniques, O-GlcNAc modified proteins were enriched from HEK293T cells and subsequently characterized using the LTQ Orbitrap Velos ETD (Thermo Fisher Scientific) mass spectrometer. In our data set, 83 sites of O-GlcNAc modification are reported with high confidence confirming that the HCD/ETD combined approach is amenable to the detection and site assignment of O-GlcNAc modified peptides. Realizing HCD triggered ETD fragmentation on a linear ion trap/Orbitrap platform for more in-depth analysis and application of this technique to other post-translationally modified proteins are currently underway. Furthermore, this report illustrates that the O-GlcNAc transferase appears to demonstrate promiscuity with regards to the hydroxyl-containing amino acid modified in short stretches of primary sequence of the glycosylated polypeptides.
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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.