Evidence map›Paper›PMID 30819804›Full record

ArticleThe Journal of biological chemistry2019

Unraveling the subtleties of β-(1→3)-glucan phosphorylase specificity in the GH94, GH149, and GH161 glycoside hydrolase families.

Sakonwan Kuhaudomlarp, Giulia Pergolizzi, Nicola J Patron, Bernard Henrissat, Robert A Field

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.2field-weighted citation impact, top 14% 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

12 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
  2. New glycoside hydrolase families of β-1,2-glucanases.Protein science : a publication of the Protein Society · 2025
    Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Discovery and Biotechnological Exploitation of Glycoside-Phosphorylases.International journal of molecular sciences · 2022
    Review
  8. Review
  9. β-Glucan phosphorylases in carbohydrate synthesis.Applied microbiology and biotechnology · 2021
    Review
  10. Article
  11. Article
  12. 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

5 authors at 3 institutions in 3 countries.

Sakonwan KuhaudomlarpFrom the Department of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich NR4 7UH, United Kingdom.ORCID 0000-0003-4415-3781
Giulia PergolizziFrom the Department of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich NR4 7UH, United Kingdom.
Nicola J Patronthe Earlham 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.
Robert A FieldFrom the Department of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich NR4 7UH, United Kingdom, rob.field@jic.ac.uk.
John Innes Centre · GBCentre National de la Recherche Scientifique · FRNorwich Research Park · GB

Funding

Biotechnology and Biological Sciences Research Council BB/L014130/1Biotechnology and Biological Sciences Research Council BB/PO12523/1Biotechnology and Biological Sciences Research Council BBS/E/J/000C0618
6 · The paper itself

Abstract

Glycoside phosphorylases (GPs) catalyze the phosphorolysis of glycans into the corresponding sugar 1-phosphates and shortened glycan chains. Given the diversity of natural β-(1→3)-glucans and their wide range of biotechnological applications, the identification of enzymatic tools that can act on β-(1→3)-glucooligosaccharides is an attractive area of research. GP activities acting on β-(1→3)-glucooligosaccharides have been described in bacteria, the photosynthetic excavate

Indexed as

Bacterial Proteinsbeta-GlucansEuglena gracilisGlycoside HydrolasesOchromonasOligosaccharidesPaenibacillus polymyxaBacterial Proteinsbeta-GlucansGlycoside HydrolasesOligosaccharidescarbohydrate metabolismcarbohydrate utilization locienzyme evolutionglycobiologyglycoside hydrolaseGram-positive bacteriaheterokontorthologsphosphorylaseβ-1,3-glucan

Identifiers

PMID30819804
PMCPMC6484121
OpenAlexW2920414537

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.