Evidence map›Paper›PMID 29730764›Full record

ArticleJournal of the American Society for Mass Spectrometry2018

Status Report on the High-Throughput Characterization of Complex Intact O-Glycopeptide Mixtures.

Adam Pap, Eva Klement, Eva Hunyadi-Gulyas, Zsuzsanna Darula, Katalin F Medzihradszky

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 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

26 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Quantitative proteome-wide O-glycoproteomics analysis with FragPipe.Analytical and bioanalytical chemistry · 2025
    Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Review
  11. DecipheringMolecular omics · 2022
    Article
  12. Revealing the human mucinome.Nature communications · 2022
    Article
  13. Review
  14. Article
  15. Article
  16. Towards structure-focused glycoproteomics.Biochemical Society transactions · 2021
    Review
  17. Linkage Memory in Underivatized Protonated Carbohydrates.Journal of the American Society for Mass Spectrometry · 2021
    Article
  18. Review
  19. Article
  20. 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

5 authors at 1 institution in 1 country.

Adam PapBiological Research Centre of the Hungarian Academy of Sciences, Szeged, Hungary.
Eva KlementBiological Research Centre of the Hungarian Academy of Sciences, Szeged, Hungary.
Eva Hunyadi-GulyasBiological Research Centre of the Hungarian Academy of Sciences, Szeged, Hungary.
Zsuzsanna DarulaBiological Research Centre of the Hungarian Academy of Sciences, Szeged, Hungary. darula.zsuzsanna@brc.mta.hu.ORCID http://orcid.org/0000-0003-1692-7591
Katalin F MedzihradszkyBiological Research Centre of the Hungarian Academy of Sciences, Szeged, Hungary.
Hungarian Academy of Sciences · HU

Funding

Economic Development and Innovation Operative Programmes GINOP-2.3.2-15-2016- 00001Economic Development and Innovation Operative Programmes GINOP-2.3.2-15-2016-00020Országos Tudományos Kutatási Alapprogramok 105611
6 · The paper itself

Abstract

A very complex mixture of intact, human N- and O-glycopeptides, enriched from the tryptic digest of urinary proteins of three healthy donors using a two-step lectin affinity enrichment, was analyzed by LC-MS/MS, leading to approximately 45,000 glycopeptide EThcD spectra. Two search engines, Byonic and Protein Prospector, were used for the interpretation of the data, and N- and O-linked glycopeptides were assigned from separate searches. The identification rate was very low in all searches, even when results were combined. Thus, we investigated the reasons why was it so, to help to improve the identification success rate. Focusing on O-linked glycopeptides, we noticed that in EThcD, larger glycan oxonium ions better survive the activation than those in HCD. These fragments, combined with reducing terminal Y ions, provide important information about the glycan(s) present, so we investigated whether filtering the peaklists for glycan oxonium ions indicating the presence of a tetra- or hexasaccharide structure would help to reveal all molecules containing such glycans. Our study showed that intact glycans frequently do not survive even mild supplemental activation, meaning one cannot rely on these oxonium ions exclusively. We found that ETD efficiency is still a limiting factor, and for highly glycosylated peptides, the only information revealed in EThcD was related to the glycan structures. The limited overlap of results delivered by the two search engines draws attention to the fact that automated data interpretation of O-linked glycopeptides is not even close to being solved. Graphical abstract ᅟ.

Indexed as

AdultCarbohydrate SequenceChromatography, LiquidFemaleGlycopeptidesHumansMaleMiddle AgedSearch EngineTandem Mass SpectrometryGlycopeptidesEThcDFragmentationGlycanMS/MSO-Glycopeptide

Identifiers

PMID29730764
OpenAlexW2802194796

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.