Evidence map›Paper›PMID 21307368›Full record

ReviewMolecular plant2011

Sub-compartmental organization of Golgi-resident N-glycan processing enzymes in plants.

Jennifer Schoberer, Richard Strasser

Open access · bronzeAbstract readReview
In one paragraph

Review in Molecular plant, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
4.6field-weighted citation impact, top 5% 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

48 citing papers in PubMed, 86 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. An overview of proteinFrontiers in plant science · 2025
    Review
  6. Trafficking and localization of Golgi-residentFrontiers in plant science · 2025
    Review
  7. Article
  8. Article
  9. Article
  10. Unexpected Arabinosylation after Humanization of Plant ProteinFrontiers in bioengineering and biotechnology · 2022
    Article
  11. Article
  12. Frontiers in plant science · 2021
    Article
  13. Article
  14. Article
  15. Article
  16. Separating Golgi Proteins fromThe Plant cell · 2019
    Article
  17. Article
  18. Article
  19. Review
  20. The glycan-dependent ERAD machinery degrades topologically diverse misfolded proteins.The Plant journal : for cell and molecular biology · 2018
    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 2 institutions in 2 countries.

Jennifer SchobererSchool of Life Sciences, Oxford Brookes University, Headington Campus, Gipsy Lane, Oxford OX30BP, UK.
Richard Strasser
BOKU University · ATOxford Brookes University · GB

Funding

Austrian Science Fund FWF P 19494Austrian Science Fund FWF P 20817
6 · The paper itself

Abstract

In all eukaryotes, the Golgi apparatus is the main site of protein glycosylation. It is widely accepted that the glycosidases and glycosyltransferases involved in N-glycan processing are found concentrated within the Golgi stack where they provide their function. This means that enzymes catalyzing early steps in the processing pathway are located mainly at the cis-side, whereas late-acting enzymes mostly locate to the trans-side of the stacks, creating a non-uniform distribution along the cis-trans axis of the Golgi. There is compelling evidence that the information for their sorting to specific Golgi cisternae depends on signals encoded in the proteins themselves as well as on the trafficking machinery that recognizes these signals and it is believed that cisternal sub-compartmentalization is achieved and maintained by a combination of retention and retrieval mechanisms. Yet, the signals, mechanism(s), and molecular factors involved are still unknown. Here, we address recent findings and summarize the current understanding of this fundamental process in plant cell biology.

Indexed as

GlycosylationGlycosyltransferasesGolgi ApparatusPlantsPolysaccharidesGlycosyltransferasesPolysaccharides

Identifiers

PMID21307368
PMCPMC3063520
OpenAlexW2035630169

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.