ArticleAnalytical chemistry2013
Absolute quantitation of immunoglobulin G and its glycoforms using multiple reaction monitoring.
Article in Analytical chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT03394092 (Changes in Glycopeptides of Serum Immunoglobulin G in Patients With Acute Myocardial Infarction and the Relationships Between Its Change and Prognosis), which is not on this map. Cited by 57 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.
Changes in Glycopeptides of Serum Immunoglobulin G in Patients With Acute Myocardial Infarction and the Relationships Between Its Change and Prognosis
Who cites it
57 citing papers in PubMed.
- Trial
- Lipid-Based Nutrient Supplements During Pregnancy and Lactation Did Not Affect Human Milk Oligosaccharides and Bioactive Proteins in a Randomized Trial.The Journal of nutrition · 2017Trial
- Quantitative analysis of immunoglobulin subclasses and subclass specific glycosylation by LC-MS-MRM in liver disease.Journal of proteomics · 2015Trial
- Standards-Free Absolute Quantitation of Oxidizable Glycopeptides by Coulometric Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2024Article
- Decoding the glycoproteome: a new frontier for biomarker discovery in cancer.Journal of hematology & oncology · 2024Review
- Methods for quantification of glycopeptides by liquid separation and mass spectrometry.Mass spectrometry reviews · 2023Review
- Article
- Quantitative clinical glycomics strategies: A guide for selecting the best analysis approach.Mass spectrometry reviews · 2022Review
- Strategies for Proteome-Wide Quantification of Glycosylation Macro- and Micro-Heterogeneity.International journal of molecular sciences · 2022Review
- Glycosylation alterations in serum of Alzheimer's disease patients show widespread changes inAlzheimer's & dementia (Amsterdam, Netherlands) · 2022Article
- Streamlined Subclass-Specific Absolute Quantification of Serum IgG Glycopeptides Using Synthetic Isotope-Labeled Standards.Analytical chemistry · 2021Article
- Recent Advances in Analytical Approaches for Glycan and Glycopeptide Quantitation.Molecular & cellular proteomics : MCP · 2021Review
- Isomer-Specific Monitoring of SialylatedFrontiers in molecular biosciences · 2021Article
- Mass spectrometry in clinical glycomics: The path from biomarker identification to clinical implementation.Clinical mass spectrometry (Del Mar, Calif.) · 2020Review
- A site-specific map of the human plasma glycome and its age and gender-associated alterations.Scientific reports · 2020Article
- Review
- Relative Quantitation of Subclass-Specific Murine IgG FcACS omega · 2020Article
- N-glycopeptide Signatures of IgAMolecular & cellular proteomics : MCP · 2019Article
- Chemical labeling for fine mapping of IgG N-glycosylation by ETD-MS.Chemical science · 2019Article
- Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Studies aimed toward glycan biomarker discovery have focused on glycan characterization by the global profiling of released glycans. Site-specific glycosylation analysis is less developed but may provide new types of biomarkers with higher sensitivity and specificity. Quantitation of peptide-conjugated glycans directly facilitates the differential analysis of distinct glycoforms associated with specific proteins at distinct sites. We have developed a method using MRM to monitor protein glycosylation normalized to absolute protein concentrations to examine quantitative changes in glycosylation at a site-specific level. This new approach provides information regarding both the absolute amount of protein and the site-specific glycosylation profile and will thus be useful to determine if altered glycosylation profiles in serum/plasma are due to a change in protein glycosylation or a change in protein concentration. The remarkable sensitivity and selectivity of MRM enable the detection of low abundance IgG glycopeptides, even when IgG was digested directly in serum with no cleanup prior to the liquid chromatography. Our results show a low limit of detection of 60 amol and a wide dynamic range of 3 orders magnitude for IgG protein quantitation. The results show that IgG glycopeptides can be analyzed directly from serum (without enrichment) and yield more accurate abundances when normalized to the protein content. This report represents the most comprehensive study so far of the use of multiple reaction monitoring for the quantitation of glycoproteins and their glycosylation patterns in biofluids.
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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.