Evidence map›Paper›PMID 37880209›Full record

ArticleNature communications2023

Sialic acid O-acetylation patterns and glycosidic linkage type determination by ion mobility-mass spectrometry.

Gaёl M Vos, Kevin C Hooijschuur, Zeshi Li, John Fjeldsted, Christian Klein, Robert P de Vries, Javier Sastre Toraño, Geert-Jan Boons

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
6.8field-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

29 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Article
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  4. Degradation of mucinbioRxiv : the preprint server for biology · 2026
    Article
  5. Article
  6. FUT1- and GAL3ST2-mediated cellular glycan remodeling broadly restricts sialic acid-dependent viral infections.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  7. Article
  8. Article
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  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Immune Camouflage inClinical ophthalmology (Auckland, N.Z.) · 2025
    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

8 authors at 3 institutions in 2 countries.

Gaёl M Vos *Department of Chemical Biology and Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Universiteitsweg 99, 3584 CG, Utrecht, The Netherlands.ORCID http://orcid.org/0000-0002-4989-2367
Kevin C Hooijschuur *Department of Chemical Biology and Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Universiteitsweg 99, 3584 CG, Utrecht, The Netherlands.
Zeshi LiDepartment of Chemical Biology and Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Universiteitsweg 99, 3584 CG, Utrecht, The Netherlands.ORCID http://orcid.org/0000-0002-8358-3162
John FjeldstedAgilent Technologies, Santa Clara, CA, 95051, USA.
Christian KleinAgilent Technologies, Santa Clara, CA, 95051, USA.
Robert P de VriesDepartment of Chemical Biology and Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Universiteitsweg 99, 3584 CG, Utrecht, The Netherlands.
Javier Sastre TorañoDepartment of Chemical Biology and Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Universiteitsweg 99, 3584 CG, Utrecht, The Netherlands. j.sastretorano@uu.nl.
Geert-Jan BoonsDepartment of Chemical Biology and Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Universiteitsweg 99, 3584 CG, Utrecht, The Netherlands. g.j.p.h.boons@uu.nl.ORCID http://orcid.org/0000-0003-3111-5954
Utrecht University · NLAgilent Technologies (United States) · USUniversity of Georgia · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

O-acetylation is a common modification of sialic acids that has been implicated in a multitude of biological and disease processes. A lack of analytical methods that can determine exact structures of sialic acid variants is a hurdle to determine roles of distinct O-acetylated sialosides. Here, we describe a drift tube ion mobility-mass spectrometry approach that can elucidate exact O-acetylation patterns as well as glycosidic linkage types of sialosides isolated from complex biological samples. It is based on the use of a library of synthetic O-acetylated sialosides to establish intrinsic collision cross section (CCS) values of diagnostic fragment ions. The CCS values were used to characterize O-acetylated sialosides from mucins and N-linked glycans from biologicals as well as equine tracheal and nasal tissues. It uncovered contrasting sialic acid linkage types of acetylated and non-acetylated sialic acids and provided a rationale for sialic acid binding preferences of equine H7 influenza A viruses.

Indexed as

Cardiac GlycosidesN-Acetylneuraminic AcidAcetylationAnimalsGlycosidesHorsesMass SpectrometrySialic AcidsCardiac GlycosidesGlycosidesN-Acetylneuraminic AcidSialic Acids

Identifiers

PMID37880209
PMCPMC10600165
OpenAlexW4387934278

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.