Evidence map›Paper›PMID 26911286›Full record

ReviewGlycobiology2016

Plant protein glycosylation.

Richard Strasser

Abstract readReview
In one paragraph

Review in Glycobiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 211 papers.

0numbers the graph read from it
0cells of the map it votes in
211citing papers in PubMed
–field-weighted citation impact
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

211 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Substrate Versatility of a Recombinant Bifidobacterial Endoglycosidase:International journal of molecular sciences · 2026
    Article
  6. Mass Spectrometric Analysis ofMolecules (Basel, Switzerland) · 2026
    Article
  7. Article
  8. Article
  9. Article
  10. Chemical reviews · 2026
    Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Studying Glycan-Dependent ERAD of Misfolded Glycoproteins in Plants.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  18. Article
  19. Article
  20. Article

151 more citing papers are in PubMed but not listed here.

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

1 author.

Richard StrasserDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, Muthgasse 18, 1190 Vienna, Austria richard.strasser@boku.ac.at.

Funding

Austrian Science Fund FWF P 23906
6 · The paper itself

Abstract

Protein glycosylation is an essential co- and post-translational modification of secretory and membrane proteins in all eukaryotes. The initial steps of N-glycosylation and N-glycan processing are highly conserved between plants, mammals and yeast. In contrast, late N-glycan maturation steps in the Golgi differ significantly in plants giving rise to complex N-glycans with β1,2-linked xylose, core α1,3-linked fucose and Lewis A-type structures. While the essential role of N-glycan modifications on distinct mammalian glycoproteins is already well documented, we have only begun to decipher the biological function of this ubiquitous protein modification in different plant species. In this review, I focus on the biosynthesis and function of different protein N-linked glycans in plants. Special emphasis is given on glycan-mediated quality control processes in the ER and on the biological role of characteristic complex N-glycan structures.

Indexed as

AnimalsArabidopsisGlycoproteinsGlycosylationGolgi ApparatusMammalsPlant ProteinsPolysaccharidesProtein Processing, Post-TranslationalXyloseYeastsGlycoproteinsPlant ProteinsPolysaccharidesXyloseendoplasmic reticulumglycosyltransferaseGolgi apparatusN-glycan processingN-glycosylation

Identifiers

PMID26911286
PMCPMC5045529

What OpenQuestion holds

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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.