Evidence map›Paper›PMID 31235546›Full record

ReviewCold Spring Harbor perspectives in biology2019

The Sweet Side of Plant-Specialized Metabolism.

Thomas Louveau, Anne Osbourn

Open access · bronzeAbstract readReview
In one paragraph

Review in Cold Spring Harbor perspectives in biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing 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

44 citing papers in PubMed, 108 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Glycosylated cannabinoids meet computational enzyme design.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  10. Article
  11. Glycosylated cannabinoids inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Unlocking saponin biosynthesis in soapwort.Nature chemical biology · 2025
    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

2 authors at 2 institutions in 1 country.

Thomas LouveauDepartment of Metabolic Biology, John Innes Centre, Norwich Research Park, Norwich NR4 7UH, United Kingdom.
Anne OsbournDepartment of Metabolic Biology, John Innes Centre, Norwich Research Park, Norwich NR4 7UH, United Kingdom.
John Innes Centre · GBNorwich Research Park · GB

Funding

Biotechnology and Biological Sciences Research Council BB/L014130/1Biotechnology and Biological Sciences Research Council BB/P012523/1Biotechnology and Biological Sciences Research Council BBS/E/J/00000614Biotechnology and Biological Sciences Research Council BBS/E/J/000PR9790
6 · The paper itself

Abstract

Glycosylation plays a major role in the structural diversification of plant natural products. It influences the properties of molecules by modifying the reactivity and solubility of the corresponding aglycones, so influencing cellular localization and bioactivity. Glycosylation of plant natural products is usually carried out by uridine diphosphate(UDP)-dependent glycosyltransferases (UGTs) belonging to the carbohydrate-active enzyme glycosyltransferase 1 (GT1) family. These enzymes transfer sugars from UDP-activated sugar moieties to small hydrophobic acceptor molecules. Plant GT1s generally show high specificity for their sugar donors and recognize a single UDP sugar as their substrate. In contrast, they are generally promiscuous with regard to acceptors, making them attractive biotechnological tools for small molecule glycodiversification. Although microbial hosts have traditionally been used for heterologous engineering of plant-derived glycosides, transient plant expression technology offers a potentially disruptive platform for rapid characterization of new plant glycosyltransferases and biosynthesis of complex glycosides.

Indexed as

BiocatalysisBiological ProductsGlycosylationGlycosyltransferasesPhylogenyPlantsProtein ConformationUridine DiphosphateBiological ProductsGlycosyltransferasesUridine Diphosphate

Identifiers

PMID31235546
PMCPMC6886449
OpenAlexW2951216493

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.