Evidence map›Paper›PMID 31046847›Full record

ReviewParasitology2019

Comparisons of N-glycans across invertebrate phyla.

Katharina Paschinger, Iain B H Wilson

Open access · hybridAbstract readComparative StudyReview
In one paragraph

Review in Parasitology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

19 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. The Historiography of Galactose and Its Recognition by Galectins.Advances in experimental medicine and biology · 2026
    Review
  6. Introduction of a human- and keyboard-friendly N-glycan nomenclature.Beilstein journal of organic chemistry · 2024
    Article
  7. Article
  8. Species-SpecificMarine drugs · 2023
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. OligomannoseThe journal of physical chemistry. B · 2021
    Article
  15. Article
  16. Review
  17. Glycosylation at an evolutionary nexus: the brittle starThe Journal of biological chemistry · 2020
    Article
  18. Sulfated and sialylatedThe Journal of biological chemistry · 2020
    Article
  19. 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

2 authors at 1 institution in 1 country.

Katharina PaschingerDepartment für Chemie, Universität für Bodenkultur, 1190 Wien, Austria.ORCID 0000-0002-3594-7136
Iain B H WilsonDepartment für Chemie, Universität für Bodenkultur, 1190 Wien, Austria.ORCID 0000-0001-8996-1518
BOKU University · AT

Funding

Austrian Science Fund FWF P 21946Austrian Science Fund FWF P 23922Austrian Science Fund FWF P 25058Austrian Science Fund FWF P 29466
6 · The paper itself

Abstract

Many invertebrates are either parasites themselves or vectors involved in parasite transmission; thereby, the interactions of parasites with final or intermediate hosts are often mediated by glycans. Therefore, it is of interest to compare the glycan structures or motifs present across invertebrate species. While a typical vertebrate modification such as sialic acid is rare in lower animals, antennal and core modifications of N-glycans are highly varied and range from core fucose, galactosylated fucose, fucosylated galactose, methyl groups, glucuronic acid and sulphate through to addition of zwitterionic moieties (phosphorylcholine, phosphoethanolamine and aminoethylphosphonate). Only in some cases are the enzymatic bases and the biological function of these modifications known. We are indeed still in the phase of discovering invertebrate glycomes primarily using mass spectrometry, but molecular biology and microarraying techniques are complementary to the determination of novel glycan structures and their functions.

Indexed as

Host-Parasite InteractionsAnimalsFucoseGlycosylationInvertebratesPolysaccharidesSialic AcidsSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationFucosePolysaccharidesSialic AcidsGlycomicsglycosyltransferaseN-glycan

Identifiers

PMID31046847
PMCPMC6935376
OpenAlexW2943738097

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.