Evidence map›Paper›PMID 33679857›Full record

ReviewFrontiers in plant science2021

Cracking the "Sugar Code": A Snapshot of

Richard Strasser, Georg Seifert, Monika S Doblin, Kim L Johnson, Colin Ruprecht, Fabian Pfrengle, Antony Bacic, José M Estevez

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in plant science, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
3.9field-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

43 citing papers in PubMed, 69 citations in OpenAlex.

  1. Substrate Versatility of a Recombinant Bifidobacterial Endoglycosidase:International journal of molecular sciences · 2026
    Article
  2. Mass Spectrometric Analysis ofMolecules (Basel, Switzerland) · 2026
    Article
  3. Article
  4. Review
  5. Advances and opportunities for computational interrogation of plant proteins.The Plant journal : for cell and molecular biology · 2026
    Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Toxins · 2025
    Article
  14. Review
  15. Trafficking and localization of Golgi-residentFrontiers in plant science · 2025
    Review
  16. Review
  17. Article
  18. Article
  19. 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

8 authors at 4 institutions in 5 countries.

Richard StrasserDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, Austria.
Georg SeifertDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, Austria.
Monika S DoblinLa Trobe Institute for Agriculture & Food, Department of Animal, Plant & Soil Sciences, La Trobe University, Bundoora, VIC, Australia.
Kim L JohnsonLa Trobe Institute for Agriculture & Food, Department of Animal, Plant & Soil Sciences, La Trobe University, Bundoora, VIC, Australia.
Colin RuprechtDepartment of Chemistry, University of Natural Resources and Life Sciences, Vienna, Austria.
Fabian PfrengleDepartment of Chemistry, University of Natural Resources and Life Sciences, Vienna, Austria.
Antony BacicLa Trobe Institute for Agriculture & Food, Department of Animal, Plant & Soil Sciences, La Trobe University, Bundoora, VIC, Australia.
José M EstevezFundación Instituto Leloir and Instituto de Investigaciones Bioquímicas de Buenos Aires (IIBBA-CONICET), Buenos Aires, Argentina.
BOKU University · ATAgriculture and Food · AUUniversidad Andrés Bello · CLZhejiang A & F University · CN

Funding

Austrian Science Fund FWF P 31920Austrian Science Fund FWF P 32332
6 · The paper itself

Abstract

Glycosylation is a fundamental co-translational and/or post-translational modification process where an attachment of sugars onto either proteins or lipids can alter their biological function, subcellular location and modulate the development and physiology of an organism. Glycosylation is not a template driven process and as such produces a vastly larger array of glycan structures through combinatorial use of enzymes and of repeated common scaffolds and as a consequence it provides a huge expansion of both the proteome and lipidome. While the essential role of

Indexed as

Arabidopsisglycan arraysglycan functionsglycosyl hydrolasesglycosyltransferasesN-glycosylationO-glycosylationplant protein glycosylation

Identifiers

PMID33679857
PMCPMC7933510
OpenAlexW3131613439

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.