Evidence map›Paper›PMID 31679023›Full record

ReviewGlycobiology2019

Molecular characteristics of plant UDP-arabinopyranose mutases.

Anam Saqib, Henrik Vibe Scheller, Folmer Fredslund, Ditte Hededam Welner

Open access · bronzeAbstract readReview
In one paragraph

Review in Glycobiology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.7field-weighted citation impact, top 12% 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

19 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Cellular Partners of Tobamoviral Movement Proteins.International journal of molecular sciences · 2025
    Review
  6. An overview of proteinFrontiers in plant science · 2025
    Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. International journal of molecular sciences · 2023
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Plant ProteinFrontiers in plant science · 2021
    Review
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 3 institutions in 3 countries.

Anam SaqibNovo Nordisk Foundation Center for Biosustainability, Technical University of Denmark, Kemitorvet 220, Kongens Lyngby, DK-2800, Denmark.
Henrik Vibe SchellerFeedstocks Division, Joint BioEnergy Institute, 5885 Hollis Street, Emeryville, CA 94608, USA; Environmental Engineering and Systems Biology Division, Lawrence Berkeley National Laboratory, 1 Cyclotron Road, Berkeley, CA 94720, USA; Department of Plant & Microbial Biology, University of California, Berkeley, CA 94720, USA.
Folmer FredslundNovo Nordisk Foundation Center for Biosustainability, Technical University of Denmark, Kemitorvet 220, Kongens Lyngby, DK-2800, Denmark.
Ditte Hededam WelnerNovo Nordisk Foundation Center for Biosustainability, Technical University of Denmark, Kemitorvet 220, Kongens Lyngby, DK-2800, Denmark.
Novo Nordisk Foundation · DKLawrence Berkeley National Laboratory · USNational Institute for Biotechnology and Genetic Engineering · PK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

l-arabinofuranose is a ubiquitous component of the cell wall and various natural products in plants, where it is synthesized from cytosolic UDP-arabinopyranose (UDP-Arap). The biosynthetic machinery long remained enigmatic in terms of responsible enzymes and subcellular localization. With the discovery of UDP-Arap mutase in plant cytosol, the demonstration of its role in cell-wall arabinose incorporation and the identification of UDP-arabinofuranose transporters in the Golgi membrane, it is clear that the cytosolic UDP-Arap mutases are the key enzymes converting UDP-Arap to UDP-arabinofuranose for cell wall and natural product biosynthesis. This has recently been confirmed by several genotype/phenotype studies. In contrast to the solid evidence pertaining to UDP-Arap mutase function in vivo, the molecular features, including enzymatic mechanism and oligomeric state, remain unknown. However, these enzymes belong to the small family of proteins originally identified as reversibly glycosylated polypeptides (RGPs), which has been studied for >20 years. Here, we review the UDP-Arap mutase and RGP literature together, to summarize and systemize reported molecular characteristics and relations to other proteins.

Indexed as

Biological ProductsCell WallIntramolecular TransferasesOryzaUridine Diphosphate SugarsBiological ProductsIntramolecular Transferasesuridine diphosphate arabinoseUridine Diphosphate Sugarsarabinofuranosearabinosereversibly glycosylated polypeptideUDP-arabinopyranose mutaseUDP-arabinose

Identifiers

PMID31679023
PMCPMC6861824
OpenAlexW2972101961

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.