ArticleJournal of the American Society for Mass Spectrometry2014
Absolute quantitation of glycosylation site occupancy using isotopically labeled standards and LC-MS.
Article in Journal of the American Society for Mass Spectrometry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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
16 citing papers in PubMed, 32 citations in OpenAlex.
- Development and Validation of a Lectin-independent Liquid Chromatography-Tandem Mass Spectrometry Method for Serum Glycosylated Alpha-fetoprotein Analysis and Comparison with a Liquid-phase Binding Assay.Annals of laboratory medicine · 2026Article
- Standards-Free Absolute Quantitation of Oxidizable Glycopeptides by Coulometric Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2024Article
- Innovative Metrics for Reporting and Comparing the Glycan Structural Profile in Biotherapeutics.Molecules (Basel, Switzerland) · 2023Article
- Recent Advances in Analytical Approaches for Glycan and Glycopeptide Quantitation.Molecular & cellular proteomics : MCP · 2021Review
- Overcoming Challenges in Structural Characterization of HIV-1 Envelope Glycoprotein by LC-MS/MS.Journal of the American Society for Mass Spectrometry · 2019Article
- Mass Spectrometry Approaches to Glycomic and Glycoproteomic Analyses.Chemical reviews · 2018Review
- Heterogeneity in glycan composition on the surface of HIV-1 envelope determines virus sensitivity to lectins.PloS one · 2018Article
- Global site-specific N-glycosylation analysis of HIV envelope glycoprotein.Nature communications · 2017Article
- Global N-Glycan Site Occupancy of HIV-1 gp120 by Metabolic Engineering and High-Resolution Intact Mass Spectrometry.ACS chemical biology · 2017Article
- Glycans and glycoproteins as specific biomarkers for cancer.Analytical and bioanalytical chemistry · 2017Review
- Recent advances in mass spectrometric analysis of glycoproteins.Electrophoresis · 2017Review
- A case for protein-level and site-level specificity in glycoproteomic studies of disease.Glycoconjugate journal · 2016Review
- N-glycoprotein macroheterogeneity: biological implications and proteomic characterization.Glycoconjugate journal · 2016Review
- Large-Scale Measurement of Absolute Protein Glycosylation Stoichiometry.Analytical chemistry · 2015Article
- Mass spectrometric analysis of the cell surface N-glycoproteome by combining metabolic labeling and click chemistry.Journal of the American Society for Mass Spectrometry · 2015Article
- New glycoproteomics software, GlycoPep Evaluator, generates decoy glycopeptides de novo and enables accurate false discovery rate analysis for small data sets.Analytical chemistry · 2014Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
N-linked glycans are required to maintain appropriate biological functions on proteins. Underglycosylation leads to many diseases in plants and animals; therefore, characterizing the extent of glycosylation on proteins is an important step in understanding, diagnosing, and treating diseases. To determine the glycosylation site occupancy, protein N-glycosidase F (PNGase F) is typically used to detach the glycan from the protein, during which the formerly glycosylated asparagine undergoes deamidation to become an aspartic acid. By comparing the abundance of the resulting peptide containing aspartic acid against the one containing non-glycosylated asparagine, the glycosylation site occupancy can be evaluated. However, this approach can give inaccurate results when spontaneous chemical deamidation of the non-glycosylated asparagine occurs. To overcome this limitation, we developed a new method to measure the glycosylation site occupancy that does not rely on converting glycosylated peptides to their deglycosylated forms. Specifically, the overall protein concentration and the non-glycosylated portion of the protein are quantified simultaneously by using heavy isotope-labeled internal standards coupled with LC-MS analysis, and the extent of site occupancy is accurately determined. The efficacy of the method was demonstrated by quantifying the occupancy of a glycosylation site on bovine fetuin. The developed method is the first work that measures the glycosylation site occupancy without using PNGase F, and it can be done in parallel with glycopeptide analysis because the glycan remains intact throughout the workflow.
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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.