Evidence map›Paper›PMID 23320427›Full record

ArticleJournal of proteome research2013

Mass spectrometric analysis of neutral and anionic N-glycans from a Dictyostelium discoideum model for human congenital disorder of glycosylation CDG IL.

Alba Hykollari, Crina I A Balog, Dubravko Rendić, Thomas Braulke, Iain B H Wilson, Katharina Paschinger

Open access · bronzeAbstract read
In one paragraph

Article in Journal of proteome research, 2013. 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
2.2field-weighted citation impact, top 12% 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, 36 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Towards understanding the extensive diversity of protein N-glycan structures in eukaryotes.Biological reviews of the Cambridge Philosophical Society · 2022
    Review
  5. Article
  6. Review
  7. Glycosylation at an evolutionary nexus: the brittle starThe Journal of biological chemistry · 2020
    Article
  8. Sulfated and sialylatedThe Journal of biological chemistry · 2020
    Article
  9. Review
  10. Article
  11. N-glycomic Complexity in Anatomical Simplicity:Frontiers in molecular biosciences · 2019
    Review
  12. Article
  13. Article
  14. Article
  15. Asparagine-Linked Glycans ofMolecular & cellular proteomics : MCP · 2017
    Article
  16. The underestimated N-glycomes of lepidopteran species.Biochimica et biophysica acta. General subjects · 2017
    Article
  17. Analysis of Invertebrate and Protist N-Glycans.Methods in molecular biology (Clifton, N.J.) · 2017
    Article
  18. Article
  19. Review
  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

6 authors at 3 institutions in 3 countries.

Alba HykollariDepartment für Chemie, Universität für Bodenkultur, A-1190 Wien, Austria.
Crina I A Balog
Dubravko Rendić
Thomas Braulke
Iain B H Wilson
Katharina Paschinger
BOKU University · ATLeiden University Medical Center · NLUniversity Medical Center Hamburg-Eppendorf · DE

Funding

Austrian Science Fund FWF P 19615Austrian Science Fund FWF P 21946
6 · The paper itself

Abstract

The HL241 mutant strain of the cellular slime mold Dictyostelium discoideum is a potential model for human congenital disorder of glycosylation type IL (ALG9-CDG) and has been previously predicted to possess a lower degree of modification of its N-glycans with anionic moieties than the parental wild-type. In this study, we first showed that this strain has a premature stop codon in its alg9 mannosyltransferase gene compatible with the occurrence of truncated N-glycans. These were subject to an optimized analytical workflow, considering that the mass spectrometry of acidic glycans often presents challenges due to neutral loss and suppression effects. Therefore, the protein-bound N-glycans were first fractionated, after serial enzymatic release, by solid phase extraction. Then primarily single glycan species were isolated by mixed hydrophilic-interaction/anion-exchange or reversed-phase HPLC and analyzed using chemical and enzymatic treatments and MS/MS. We show that protein-linked N-glycans of the mutant are of reduced size as compared to those of wild-type AX3, but still contain core α1,3-fucose, intersecting N-acetylglucosamine, bisecting N-acetylglucosamine, methylphosphate, phosphate, and sulfate residues. We observe that a single N-glycan can carry up to four of these six possible modifications. Due to the improved analytical procedures, we reveal fuller details regarding the N-glycomic potential of this fascinating model organism.

Indexed as

Models, BiologicalBase SequenceBlotting, WesternChromatography, High Pressure LiquidCongenital Disorders of GlycosylationDictyosteliumDNA PrimersHumansPolysaccharidesSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationTandem Mass SpectrometryDNA PrimersPolysaccharides

Identifiers

PMID23320427
PMCPMC3588589
OpenAlexW2054618993

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.