Evidence map›Paper›PMID 26538210›Full record

ArticleJournal of proteome research2015

Comparisons of Caenorhabditis Fucosyltransferase Mutants Reveal a Multiplicity of Isomeric N-Glycan Structures.

Shi Yan, Chunsheng Jin, Iain B H Wilson, Katharina Paschinger

Open access · hybridAbstract readComparative Study
In one paragraph

Article in Journal of proteome research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed, 1 pooled it
2.2field-weighted citation impact, top 13% 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

23 citing papers in PubMed, 1 synthesis or guideline pooled it, 38 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. N-glycomic Complexity in Anatomical Simplicity:Frontiers in molecular biosciences · 2019
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. The Journal of biological chemistry · 2017
    Article
  18. Article
  19. The underestimated N-glycomes of lepidopteran species.Biochimica et biophysica acta. General subjects · 2017
    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

4 authors at 1 institution in 1 country.

Shi YanDepartment für Chemie, Universität für Bodenkultur , 1190 Wien, Austria.
Chunsheng JinInstitutionen för Biomedicin, Göteborgs Universitet , 405 30 Göteborg, Sweden.
Iain B H WilsonDepartment für Chemie, Universität für Bodenkultur , 1190 Wien, Austria.
Katharina PaschingerDepartment für Chemie, Universität für Bodenkultur , 1190 Wien, Austria.
BOKU University · AT

Funding

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

Abstract

Recent studies have shown a remarkable degree of plasticity in the N-glycome of the model nematode Caenorhabditis elegans; ablation of glycosylation-relevant genes can result in radically altered N-glycan profiles despite only minor biological phenotypic effects. Up to four fucose residues and five different linkages of fucose are known on the N-glycans of C. elegans. Due to the complexity in the wild type, we established three mutant strains defective in two core fucosyltransferases each (fut-1;fut-6, fut-1;fut-8, and fut-6;fut-8). Enzymatically released N-glycans were subject to HPLC and MALDI-TOF MS/MS, in combination with various treatments, to verify structural details. The N-glycome of the fut-1;fut-6 mutant was the most complex of the three double-mutant strains due to the extension of the core α1,6-fucose as well as the presence of fucose on the bisecting galactose. In contrast, maximally two fucoses were found on N-glycans of the fut-1;fut-8 and fut-6;fut-8 strains. The different locations and capping of fucose meant that up to 13 isomeric structures, many highly galactosylated, were determined for some single masses. These data not only show the high variability of the N-glycomic capacity of a "simple" nematode but also exemplify the need for multiple approaches to reveal individual glycan structures within complex invertebrate glycomes.

Indexed as

AnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsCarbohydrate SequenceChromatography, High Pressure LiquidFucoseFucosyltransferasesGenes, HelminthGlycomicsGlycosylationMolecular Sequence DataMutant ProteinsMutationPolysaccharidesSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationCaenorhabditis elegans ProteinsFucoseFucosyltransferasesFUT-6 protein, C elegansgalactoside 3-fucosyltransferaseGlycoprotein 6-alpha-L-fucosyltransferaseMutant ProteinsPolysaccharidesbisectfucosyltransferase mutantglycomicsnematode

Identifiers

PMID26538210
PMCPMC4673604
OpenAlexW2193935687

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.