Evidence map›Paper›PMID 29317507›Full record

ArticleThe Journal of biological chemistry2018

Identification of

Sakonwan Kuhaudomlarp, Nicola J Patron, Bernard Henrissat, Martin Rejzek, Gerhard Saalbach, Robert A Field

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
5.4field-weighted citation impact, top 4% 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

21 citing papers in PubMed, 40 citations in OpenAlex.

  1. Characterization of a GH17 laminarinase,Applied and environmental microbiology · 2026
    Article
  2. Frontiers in microbiology · 2026
    Article
  3. New glycoside hydrolase families of β-1,2-glucanases.Protein science : a publication of the Protein Society · 2025
    Article
  4. Article
  5. Article
  6. Discovery and Biotechnological Exploitation of Glycoside-Phosphorylases.International journal of molecular sciences · 2022
    Review
  7. Article
  8. Review
  9. Article
  10. Genes · 2021
    Article
  11. β-Glucan phosphorylases in carbohydrate synthesis.Applied microbiology and biotechnology · 2021
    Review
  12. Unravelling Regioselectivity ofInternational journal of molecular sciences · 2021
    Article
  13. Article
  14. Article
  15. Article
  16. Metabolites · 2019
    Article
  17. Article
  18. Article
  19. Review
  20. Bioproducts FromFrontiers in bioengineering and biotechnology · 2019
    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

6 authors at 4 institutions in 2 countries.

Sakonwan KuhaudomlarpDepartment of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich NR4 7UH, United Kingdom.
Nicola J PatronEarlham Institute, Norwich Research Park, Norwich NR4 7UZ, United Kingdom.
Bernard HenrissatArchitecture et Fonction des Macromolécules Biologiques, Aix-Marseille University, 163 Avenue de Luminy, 13288 Marseille, France; CNRS, UMR 7257, 163 Avenue de Luminy, 13288 Marseille, France; Department of Biological Sciences, King Abdulaziz University, Jeddah 23218, Saudi Arabia.
Martin RejzekDepartment of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich NR4 7UH, United Kingdom.
Gerhard SaalbachDepartment of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich NR4 7UH, United Kingdom.
Robert A FieldDepartment of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich NR4 7UH, United Kingdom. Electronic address: rob.field@jic.ac.uk.
John Innes Centre · GBNorwich Research Park · GBArchitecture et Fonction des Macromolécules Biologiques · FRUniversity of Oxford · GB

Funding

Biotechnology and Biological Sciences Research Council BB/J004561/1Biotechnology and Biological Sciences Research Council BB/L014130/1Biotechnology and Biological Sciences Research Council BB/M02903411Biotechnology and Biological Sciences Research Council BBS/E/J/000C0618Biotechnology and Biological Sciences Research Council BBS/E/J/000PR9790
6 · The paper itself

Abstract

Glycoside phosphorylases (EC 2.4.x.x) carry out the reversible phosphorolysis of glucan polymers, producing the corresponding sugar 1-phosphate and a shortened glycan chain. β-1,3-Glucan phosphorylase activities have been reported in the photosynthetic euglenozoan

Indexed as

Amino Acid Sequencebeta-GlucansComputational BiologyConserved SequenceEuglena gracilisGenes, ProtozoanGlycoside HydrolasesGlycosidesHydrolysisKineticsMolecular WeightMultigene FamilyPhosphorylasesPhosphorylationPhylogenyProteoglycans(1-3)-beta-D-glucan phosphatebeta-GlucansGlycoside HydrolasesGlycosidesPhosphorylasespolysaccharide-KProteoglycansProtozoan ProteinsRecombinant Fusion Proteinsalgaebeta-1,3-glucanEuglena gracilisgene transferglycobiologyglycoside hydrolasegram-negative bacteriamolecular evolutionorthologsphosphorylasephylogeneticspolysaccharidepolysaccharide utilization loci

Identifiers

PMID29317507
PMCPMC5827456
OpenAlexW2783165892

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.