Evidence map›Paper›PMID 29603058›Full record

ArticleJournal of the American Society for Mass Spectrometry2018

Discrimination of Isomers of Released N- and O-Glycans Using Diagnostic Product Ions in Negative Ion PGC-LC-ESI-MS/MS.

Christopher Ashwood, Chi-Hung Lin, Morten Thaysen-Andersen, Nicolle H Packer

Abstract read
PubMed Publisher
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
5.4field-weighted citation impact, top 3% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

58 citing papers in PubMed, 116 citations in OpenAlex.

  1. Review
  2. Article
  3. Isomeric diversity of GlcNAc(ManScientific reports · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Exploring the O-glycomic Degradome Using Natural Mucin Libraries.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  10. Article
  11. Review
  12. Article
  13. ComprehensiveAnalytical chemistry · 2024
    Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Glycoproteome remodeling and organelle-specificProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 4 institutions in 1 country.

Christopher AshwoodDepartment of Molecular Sciences, Macquarie University, Sydney, Australia.
Chi-Hung LinDepartment of Molecular Sciences, Macquarie University, Sydney, Australia.
Morten Thaysen-AndersenDepartment of Molecular Sciences, Macquarie University, Sydney, Australia.
Nicolle H PackerDepartment of Molecular Sciences, Macquarie University, Sydney, Australia. nicki.packer@mq.edu.au.ORCID http://orcid.org/0000-0002-7532-4021
Australian Genome Research Facility · AUAustralian Research Council · AUGriffith University · AUMacquarie University · AU

Funding

Centre of Excellence in Nanoscale Biophotonics, Australian Research Council (AU) CE140100003
6 · The paper itself

Abstract

Profiling cellular protein glycosylation is challenging due to the presence of highly similar glycan structures that play diverse roles in cellular physiology. As the anomericity and the exact linkage type of a single glycosidic bond can influence glycan function, there is a demand for improved and automated methods to confirm detailed structural features and to discriminate between structurally similar isomers, overcoming a significant bottleneck in the analysis of data generated by glycomics experiments. We used porous graphitized carbon-LC-ESI-MS/MS to separate and detect released N- and O-glycan isomers from mammalian model glycoproteins using negative mode resonance activation CID-MS/MS. By interrogating similar fragment spectra from closely related glycan isomers that differ only in arm position and sialyl linkage, product fragment ions for discrimination between these features were discovered. Using the Skyline software, at least two diagnostic fragment ions of high specificity were validated for automated discrimination of sialylation and arm position in N-glycan structures, and sialylation in O-glycan structures, complementing existing structural diagnostic ions. These diagnostic ions were shown to be useful for isomer discrimination using both linear and 3D ion trap mass spectrometers when analyzing complex glycan mixtures from cell lysates. Skyline was found to serve as a useful tool for automated assessment of glycan isomer discrimination. This platform-independent workflow can potentially be extended to automate the characterization and quantitation of other challenging glycan isomers. Graphical Abstract ᅟ.

Indexed as

AnimalsCell LineChromatography, LiquidGlycomicsGlycoproteinsGraphiteIonsIsomerismMicePolysaccharidesPorositySialic AcidsSpectrometry, Mass, Electrospray IonizationTandem Mass SpectrometryGlycoproteinsGraphiteIonsPolysaccharidesSialic AcidsDiagnostic ionsGlycomicsMS/MSSkyline

Identifiers

PMID29603058
OpenAlexW2794525690

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.