ArticleAnalytical chemistry2013
Characterizing O-linked glycopeptides by electron transfer dissociation: fragmentation rules and applications in data analysis.
Article in Analytical chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 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
23 citing papers in PubMed, 56 citations in OpenAlex.
- Studying Mucin-Derived O-Glycopeptides with Gas-Phase FRET.Analytical chemistry · 2026Article
- Evaluating the Performance of Photon- and Electron-Based Fragmentation Methods in Omnitrap-LCMS Analysis ofAnalytical chemistry · 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
- Integration of alternative fragmentation techniques into standard LC-MS workflows using a single deep learning model enhances proteome coverage.Nature methods · 2026Article
- Intact mass analysis reveals the novel O-linked glycosylation on the stalk region of PD-1 protein.Scientific reports · 2023Article
- The next "sweet" spot for pancreatic ductal adenocarcinoma: Glycoprotein for early detection.Mass spectrometry reviews · 2023Review
- HIV and Proteomics: What We Have Learned from High Throughput Studies.Proteomics. Clinical applications · 2021Review
- Optimal Dissociation Methods Differ forJournal of proteome research · 2020Article
- Large-scale site-specific mapping of the O-GalNAc glycoproteome.Nature protocols · 2020Article
- Recent Advances in Glycoproteomic Analysis by Mass Spectrometry.Analytical chemistry · 2020Review
- DecoyDeveloper: An On-Demand, De Novo Decoy Glycopeptide Generator.Journal of proteome research · 2019Article
- Mapping the O-glycoproteome using site-specific extraction of O-linked glycopeptides (EXoO).Molecular systems biology · 2018Article
- Comparison of Collisional and Electron-Based Dissociation Modes for Middle-Down Analysis of Multiply Glycosylated Peptides.Journal of the American Society for Mass Spectrometry · 2018Article
- Ultraviolet, Infrared, and High-Low Energy Photodissociation of Post-Translationally Modified Peptides.Journal of the American Society for Mass Spectrometry · 2018Article
- The Role of Electron Transfer Dissociation in Modern Proteomics.Analytical chemistry · 2018Review
- Electron-Transfer/Higher-Energy Collision Dissociation (EThcD)-Enabled Intact Glycopeptide/Glycoproteome Characterization.Journal of the American Society for Mass Spectrometry · 2017Article
- Travelling-wave ion mobility and negative ion fragmentation of high-mannose N-glycans.Journal of mass spectrometry : JMS · 2016Article
- Proteomics, biomarkers, and HIV-1: A current perspective.Proteomics. Clinical applications · 2016Review
- Site-specific O-Glycosylation Analysis of Human Blood Plasma Proteins.Molecular & cellular proteomics : MCP · 2016Article
- Comparison of Glycopeptide Fragmentation by Collision Induced Dissociation and Ultraviolet Photodissociation.International journal of mass spectrometry · 2015Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Studying protein O-glycosylation remains an analytical challenge. Different from N-linked glycans, the O-glycosylation site is not within a known consensus sequence. Additionally, O-glycans are heterogeneous with numerous potential modification sites. Electron transfer dissociation (ETD) is the method of choice in analyzing these glycopeptides since the glycan side chain remains intact in ETD, and the glycosylation site can be localized on the basis of the c and z fragment ions. Nonetheless, new software is necessary for interpreting O-glycopeptide ETD spectra in order to expedite the analysis workflow. To address the urgent need, we studied the fragmentation of O-glycopeptides in ETD and found useful rules that facilitate their identification. By implementing the rules into an algorithm to score potential assignments against ETD-MS/MS data, we applied the method to glycopeptides generated from various O-glycosylated proteins including mucin, erythropoietin, fetuin, and an HIV envelope protein, 1086.C gp120. The site-specific O-glycopeptide composition was correctly assigned in every case, proving the merits of our method in analyzing glycopeptide ETD data. The algorithm described herein can be easily incorporated into other automated glycomics tools.
Indexed as
Identifiers
What OpenQuestion holds
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.