ReviewMass spectrometry reviews2019
Global and site-specific analysis of protein glycosylation in complex biological systems with Mass Spectrometry.
Review in Mass spectrometry reviews, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
41 citing papers in PubMed.
- Surface Engineering of Magnetite Nanoparticles with Boronated Polysaccharides Enables Alpha-1-Acid Glycoprotein Binding.ACS omega · 2026Article
- Mass Spectrometry-Based Proteomics Methods for Systematic Identification and Quantification of Protein O-Glycosylation in Complex Biological Samples.Journal of the American Society for Mass Spectrometry · 2026Review
- Characterization of Cell Surface Glycoproteins Using Enzymatic Treatment and Mass Spectrometry.Analytical chemistry · 2024Article
- Veneer Is a Webtool for Rapid, Standardized, and Transparent Interpretation, Annotation, and Reporting of Mammalian Cell SurfaceJournal of proteome research · 2024Article
- Exposing the molecular heterogeneity of glycosylated biotherapeutics.Nature communications · 2024Article
- Mass Spectrometry Strategies forCells · 2024Review
- Can We BoostJournal of the American Society for Mass Spectrometry · 2024Article
- Mass spectrometry analysis of intact proteinJournal of Zhejiang University. Science. B · 2024Article
- Hydrophilic Interaction Liquid Chromatography (HILIC) Enrichment of Glycopeptides Using PolyHYDROXYETHYL A.Methods in molecular biology (Clifton, N.J.) · 2024Article
- A novel hydrophilic polymer-coated magnetic nanomaterial based on the HILIC strategy for fast separation of glycopeptides and glycosylated exosomes.Analytical and bioanalytical chemistry · 2023Article
- Deciphering the Properties and Functions of Glycoproteins Using Quantitative Proteomics.Journal of proteome research · 2023Review
- Methods for quantification of glycopeptides by liquid separation and mass spectrometry.Mass spectrometry reviews · 2023Review
- Systematic characterization of extracellular glycoproteins using mass spectrometry.Mass spectrometry reviews · 2023Review
- In-depth characterization of protein N-glycosylation for a COVID-19 variant-design vaccine spike protein.Analytical and bioanalytical chemistry · 2023Article
- Article
- High sensitivity glycomics in biomedicine.Mass spectrometry reviews · 2022Review
- Mass Spectrometry-Based Techniques to Elucidate the Sugar Code.Chemical reviews · 2022Review
- Comparison of Different Mass Spectrometry Workflows for the Proteomic Analysis of Tear Fluid.International journal of molecular sciences · 2022Article
- Potential Biomarkers for Liver Cancer Diagnosis Based on Multi-Omics Strategy.Frontiers in oncology · 2022Review
- Computational Prediction of N- and O-Linked Glycosylation Sites for Human and Mouse Proteins.Methods in molecular biology (Clifton, N.J.) · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
Protein glycosylation is ubiquitous in biological systems and plays essential roles in many cellular events. Global and site-specific analysis of glycoproteins in complex biological samples can advance our understanding of glycoprotein functions and cellular activities. However, it is extraordinarily challenging because of the low abundance of many glycoproteins and the heterogeneity of glycan structures. The emergence of mass spectrometry (MS)-based proteomics has provided us an excellent opportunity to comprehensively study proteins and their modifications, including glycosylation. In this review, we first summarize major methods for glycopeptide/glycoprotein enrichment, followed by the chemical and enzymatic methods to generate a mass tag for glycosylation site identification. We next discuss the systematic and quantitative analysis of glycoprotein dynamics. Reversible protein glycosylation is dynamic, and systematic study of glycoprotein dynamics helps us gain insight into glycoprotein functions. The last part of this review focuses on the applications of MS-based proteomics to study glycoproteins in different biological systems, including yeasts, plants, mice, human cells, and clinical samples. Intact glycopeptide analysis is also included in this section. Because of the importance of glycoproteins in complex biological systems, the field of glycoproteomics will continue to grow in the next decade. Innovative and effective MS-based methods will exponentially advance glycoscience, and enable us to identify glycoproteins as effective biomarkers for disease detection and drug targets for disease treatment. © 2019 Wiley Periodicals, Inc. Mass Spec Rev 9999: XX-XX, 2019.
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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 Socratic graph.