Evidence map›Paper›PMID 27743366›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2017

Analysis of Invertebrate and Protist N-Glycans.

Alba Hykollari, Katharina Paschinger, Barbara Eckmair, Iain B H Wilson

Abstract read
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
6.5field-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

17 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Analysis of Caenorhabditis Protein Glycosylation.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  3. Article
  4. Review
  5. Sulfated and sialylatedThe Journal of biological chemistry · 2020
    Article
  6. Glycosylation at an evolutionary nexus: the brittle starThe Journal of biological chemistry · 2020
    Article
  7. Review
  8. Article
  9. Article
  10. N-glycomic Complexity in Anatomical Simplicity:Frontiers in molecular biosciences · 2019
    Review
  11. Protein-Specific Analysis of Invertebrate Glycoproteins.Methods in molecular biology (Clifton, N.J.) · 2019
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. The underestimated N-glycomes of lepidopteran species.Biochimica et biophysica acta. General subjects · 2017
    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 1 institution in 1 country.

Alba HykollariDepartment für Chemie, Universität für Bodenkultur, Muthgasse 18, 1190, Vienna, Austria.
Katharina PaschingerDepartment für Chemie, Universität für Bodenkultur, Muthgasse 18, 1190, Vienna, Austria.
Barbara EckmairDepartment für Chemie, Universität für Bodenkultur, Muthgasse 18, 1190, Vienna, Austria.
Iain B H WilsonDepartment für Chemie, Universität für Bodenkultur, Muthgasse 18, 1190, Vienna, Austria. iain.wilson@boku.ac.at.
BOKU University · AT

Funding

Austrian Science Fund FWF P 23922Austrian Science Fund FWF P 25058Austrian Science Fund FWF P 26662Austrian Science Fund FWF W 1224
6 · The paper itself

Abstract

N-glycans from invertebrates and protists have often unusual structures which present analytical challenges. Both core and antennal modifications can be quite different from the more familiar vertebrate glycan motifs; thereby, contrary to the concept that "simple" organisms have "simple" N-glycans, rather complex oligosaccharides structures, including zwitterionic and anionic ones, have been found in a range of species. Thus, to facilitate the optimized elucidation of the maximal possible range of structures, the analytical workflow for glycomics of these organisms should include sequential release and fractionation steps. Peptide:N-glycosidase F is sufficient to isolate N-glycans from fungi and some protists, but in most invertebrates core α1,3-fucose is present, so release of the glycans from glycopeptides with peptide:N-glycosidases A is required. Subsequent solid-phase extraction with graphitized carbon and reversed phase resins enables different classes of N-glycans to be separated prior to high-pressure liquid chromatography (HPLC) and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS). Depending on the types and numbers of glycans present, either reversed- or normal-phase HPLC (or both in series) enable even single isomeric or isobaric structures to be separated prior to MALDI-TOF MS and MS/MS. The use of enzymatic or chemical treatments allows further insights to be gained, although some glycan modifications (especially methylation) are resistant. Using a battery of methods, sometimes up to 100 structures from a single organism can be assigned, a complexity which raises evolutionary questions regarding the function of these glycans.

Indexed as

AnimalsBlotting, WesternChromatography, High Pressure LiquidGlycomicsGlycopeptidesInvertebratesPolysaccharidesSolid Phase ExtractionSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationGlycopeptidesPolysaccharidesGlycomeGlycosylationMass spectrometryPhosphorylated glycansSulphated glycans

Identifiers

PMID27743366
PMCPMC5156297
OpenAlexW2530113137

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Registered trials

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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.