ReviewBiochemistry2020
A Perspective on the Confident Comparison of Glycoprotein Site-Specific Glycosylation in Sample Cohorts.
Review in Biochemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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
6 citing papers in PubMed.
- Mass Spectrometry-Based Glycomics and Proteomics Profiling of On-Slide Digested Tissue from Complex Biological Samples.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Methods for quantification of glycopeptides by liquid separation and mass spectrometry.Mass spectrometry reviews · 2023Review
- Charting the Proteoform Landscape of Serum Proteins in Individual Donors by High-Resolution Native Mass Spectrometry.Analytical chemistry · 2022Article
- Comparative N-Glycoproteomics Analysis of Clinical Samples Via Different Mass Spectrometry Dissociation Methods.Frontiers in chemistry · 2022Article
- Comprehensive Plasma N-Glycoproteome Profiling Based on EThcD-sceHCD-MS/MS.Frontiers in chemistry · 2022Article
- Calculating Glycoprotein Similarities From Mass Spectrometric Data.Molecular & cellular proteomics : MCP · 2021Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
Protein glycosylation, resulting from glycosyl transferase reactions under complex control in the secretory pathway, consists of a distribution of related glycoforms at each glycosylation site. Because the biosynthetic substrate concentration and transport rates depend on architecture and other aspects of cellular phenotypes, site-specific glycosylation cannot be predicted accurately from genomic, transcriptomic, or proteomic information. Rather, it is necessary to quantify glycosylation at each protein site and how this changes among a sample cohort to provide information about disease mechanisms. At present, mature mass spectrometry-based methods allow for qualitative assignment of the glycan composition and glycosylation site of singly glycosylated proteolytic peptides. To make such quantitative comparisons, it is necessary to sample the glycosylation distribution with sufficient coverage and accuracy for confident assessment of the glycosylation changes that occur in the biological cohort. In this Perspective, we discuss the unmet needs for mass spectrometry acquisition methods and bioinformatics for the confident comparison of protein site-specific glycosylation among sample cohorts.
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Registered trials
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