Evidence map›Paper›PMID 28754708›Full record

ArticleApplied and environmental microbiology2017

Glucosylglycerate Phosphorylase, an Enzyme with Novel Specificity Involved in Compatible Solute Metabolism.

Jorick Franceus, Denise Pinel, Tom Desmet

Open access · bronzeAbstract read
In one paragraph

Article in Applied and environmental microbiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.8field-weighted citation impact, top 11% 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

16 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Microorganisms · 2023
    Article
  6. Review
  7. Article
  8. Discovery and Biotechnological Exploitation of Glycoside-Phosphorylases.International journal of molecular sciences · 2022
    Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Structural Comparison of a Promiscuous and a Highly Specific Sucrose 6International journal of molecular sciences · 2019
    Article
  14. Article
  15. Sucrose 6Microbial genomics · 2019
    Article
  16. 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

3 authors at 1 institution in 1 country.

Jorick FranceusCentre for Synthetic Biology, Department of Biochemical and Microbial Technology, Ghent University, Ghent, Belgium.
Denise PinelCentre for Synthetic Biology, Department of Biochemical and Microbial Technology, Ghent University, Ghent, Belgium.
Tom DesmetCentre for Synthetic Biology, Department of Biochemical and Microbial Technology, Ghent University, Ghent, Belgium tom.desmet@ugent.be.
Ghent University · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Family GH13_18 of the carbohydrate-active enzyme database consists of retaining glycoside phosphorylases that have attracted interest with their potential for synthesizing valuable α-sugars and glucosides. Sucrose phosphorylase was believed to be the only enzyme with specificity in this subfamily for many years, but recent work revealed an enzyme with a different function and hinted at an even broader diversity that is left to discover. In this study, a putative sucrose phosphorylase from

Indexed as

BacteriaBacterial ProteinsGlucosidesGlucosyltransferasesGlyceric AcidsKineticsPhylogenySubstrate SpecificityBacterial ProteinsGlucosidesGlucosyltransferasesglyceric acidGlyceric Acidssucrose phosphorylaseglucosylglycerate phosphorylaseglycoside hydrolase family GH13glycoside phosphorylasesucrose phosphorylase

Identifiers

PMID28754708
PMCPMC5601347
OpenAlexW2741669086

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.