ArticleJournal of proteome research2018
Multiple Reaction Monitoring for the Quantitation of Serum Protein Glycosylation Profiles: Application to Ovarian Cancer.
Article in Journal of proteome research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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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.
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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
24 citing papers in PubMed, 43 citations in OpenAlex.
- Orosomucoid 2 (ORM2) in type 2 diabetes and coronary artery disease: a potential link between insulin resistance and vascular inflammation.Frontiers in cardiovascular medicine · 2026Review
- Serum N-Glycomics with Nano-LC-QToF LC-MS/MS Reveals N-Glycan Biomarkers for Glioblastoma, Meningioma, and High-Grade Meningioma.Journal of proteome research · 2025Article
- Proteomic landscape of epithelial ovarian cancer.Nature communications · 2024Article
- Diagnosing and staging epithelial ovarian cancer by serum glycoproteomic profiling.British journal of cancer · 2024Article
- Decoding the glycoproteome: a new frontier for biomarker discovery in cancer.Journal of hematology & oncology · 2024Review
- Water-stable hydrophilic metal organic framework composite for the recognition of N-glycopeptides during diabetes progression by mass spectrometry.Mikrochimica acta · 2023Article
- Discovery and validation of serum glycoprotein biomarkers for high grade serous ovarian cancer.Proteomics. Clinical applications · 2023Article
- Article
- Methods for quantification of glycopeptides by liquid separation and mass spectrometry.Mass spectrometry reviews · 2023Review
- Higher Temperature Porous Graphitic Carbon Separations Differentially Impact Distinct Glycopeptide Classes.Journal of the American Society for Mass Spectrometry · 2023Article
- Article
- Quantitative clinical glycomics strategies: A guide for selecting the best analysis approach.Mass spectrometry reviews · 2022Review
- Identification of Potential Predictor of Biochemical Recurrence in Prostate Cancer.International journal of general medicine · 2022Article
- Recent Advances in Analytical Approaches for Glycan and Glycopeptide Quantitation.Molecular & cellular proteomics : MCP · 2021Review
- Glycoproteomics-based signatures for tumor subtyping and clinical outcome prediction of high-grade serous ovarian cancer.Nature communications · 2020Article
- Glycoproteomic Analysis of Human Urinary Exosomes.Analytical chemistry · 2020Article
- 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
- Targeting Oligosaccharides and Glycoconjugates Using Superselective Binding Scaffolds.Advanced functional materials · 2020Article
- Distribution ofFrontiers in immunology · 2020Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
Protein glycosylation fingerprints are widely recognized as potential markers for disease states, and indeed differential glycosylation has been identified in multiple types of autoimmune diseases and several types of cancer. However, releasing the glycans leave the glycoproteins unknown; therefore, there exists a need for high-throughput methods that allow quantification of site- and protein-specific glycosylation patterns from complex biological mixtures. In this study, a targeted multiple reaction monitoring (MRM)-based method for the protein- and site-specific quantitation involving serum proteins immunoglobulins A, G and M, alpha-1-antitrypsin, transferrin, alpha-2-macroglobulin, haptoglobin, alpha-1-acid glycoprotein and complement C3 was developed. The method is based on tryptic digestion of serum glycoproteins, followed by immediate reverse phase UPLC-QQQ-MS analysis of glycopeptides. To quantitate protein glycosylation independent of the protein serum concentration, a nonglycosylated peptide was also monitored. Using this strategy, 178 glycopeptides and 18 peptides from serum glycoproteins are analyzed with good repeatability (interday CVs of 3.65-21-92%) in a single 17 min run. To assess the potential of the method, protein glycosylation was analyzed in serum samples from ovarian cancer patients and controls. A training set consisting of 40 cases and 40 controls was analyzed, and differential analyses were performed to identify aberrant glycopeptide levels. All findings were validated in an independent test set (n = 44 cases and n = 44 controls). In addition to the differential glycosylation on the immunoglobulins, which was reported previously, aberrant glycosylation was also observed on each of the glycoproteins, which could be corroborated in the test set. This report shows the development of a method for targeted protein- and site-specific glycosylation analysis and the potential of such methods in biomarker development.
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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.