Evidence map›Paper›PMID 28623326›Full record

ArticleScientific reports2017

Sialic acid linkage differentiation of glycopeptides using capillary electrophoresis - electrospray ionization - mass spectrometry.

Guinevere S M Kammeijer, Bas C Jansen, Isabelle Kohler, Anthonius A M Heemskerk, Oleg A Mayboroda, Paul J Hensbergen, Julie Schappler, Manfred Wuhrer

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
4.6field-weighted citation impact, top 4% 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

24 citing papers in PubMed, 101 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. High-Sensitivity Glycoproteomic Analysis of Biological Samples by CZE-ESI-MS.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  12. The Hitchhiker's guide to glycoproteomics.Biochemical Society transactions · 2021
    Review
  13. Mass Spectrometry-Based Glycoproteomics and Prostate Cancer.International journal of molecular sciences · 2021
    Review
  14. Towards structure-focused glycoproteomics.Biochemical Society transactions · 2021
    Review
  15. Glycoproteomics Technologies in Glycobiotechnology.Advances in biochemical engineering/biotechnology · 2021
    Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. Review
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

8 authors at 3 institutions in 2 countries.

Guinevere S M KammeijerLeiden University Medical Center, Center for Proteomics and Metabolomics, Leiden, The Netherlands. g.s.m.kammeijer@lumc.nl.
Bas C JansenLeiden University Medical Center, Center for Proteomics and Metabolomics, Leiden, The Netherlands.
Isabelle KohlerLeiden University Medical Center, Center for Proteomics and Metabolomics, Leiden, The Netherlands.
Anthonius A M HeemskerkLeiden University Medical Center, Center for Proteomics and Metabolomics, Leiden, The Netherlands.
Oleg A MayborodaLeiden University Medical Center, Center for Proteomics and Metabolomics, Leiden, The Netherlands.
Paul J HensbergenLeiden University Medical Center, Center for Proteomics and Metabolomics, Leiden, The Netherlands.
Julie SchapplerUniversity of Geneva, University of Lausanne, School of Pharmaceutical Sciences, Geneva, Switzerland.
Manfred WuhrerLeiden University Medical Center, Center for Proteomics and Metabolomics, Leiden, The Netherlands.
Leiden University Medical Center · NLNetherlands Metabolomics Centre · NLUniversity of Lausanne · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sialylation is a glycosylation feature that occurs in different linkages at the non-reducing end of a glycan moiety, the linkage isomers are often differentially associated with various biological processes. Due to very similar physico-chemical properties, the separation of isomeric sialylated glycopeptides remains challenging but of utmost importance in the biomedicine and biotechnology, including biomarker discovery, glyco-engineering and biopharmaceutical characterization. This study presents the implementation of a high-resolution separation platform based on capillary electrophoresis - mass spectrometry (CE-MS) allowing for the selective analysis of α2,3- and α2,6-sialylated glycopeptides. These differentially linked glycopeptides showed an identical fragmentation pattern (collision induced dissociation) but different electrophoretic mobilities, allowing for baseline separation of the different linkages without the need for an extensive sample preparation. The different migration behavior between the two moieties was found to correlate with differences in pK

Indexed as

Spectrometry, Mass, Electrospray IonizationCarbohydrate ConformationElectrophoresis, CapillaryGlycopeptidesN-Acetylneuraminic AcidGlycopeptidesN-Acetylneuraminic Acid

Identifiers

PMID28623326
PMCPMC5473812
OpenAlexW2626957826

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.