Evidence map›Paper›PMID 28057757›Full record

ArticleThe Journal of biological chemistry2017

Oxidative Maturation and Structural Characterization of Prenylated FMN Binding by UbiD, a Decarboxylase Involved in Bacterial Ubiquinone Biosynthesis.

Stephen A Marshall, Karl Fisher, Aisling Ní Cheallaigh, Mark D White, Karl A P Payne, D A Parker, Stephen E J Rigby, David Leys

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
6.1field-weighted citation impact, top 3% 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

20 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Anaerobic degradation of polycyclic aromatic hydrocarbons.Applied and environmental microbiology · 2025
    Review
  5. Article
  6. Article
  7. Enzymatic Conversion of COChemical reviews · 2023
    Review
  8. Review
  9. Article
  10. Review
  11. Article
  12. Structure and Mechanism ofACS catalysis · 2021
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

8 authors at 2 institutions in 2 countries.

Stephen A MarshallFrom the Manchester Institute of Biotechnology, University of Manchester, 131 Princess Street Manchester, M1 7DN, United Kingdom and.
Karl FisherFrom the Manchester Institute of Biotechnology, University of Manchester, 131 Princess Street Manchester, M1 7DN, United Kingdom and.
Aisling Ní CheallaighFrom the Manchester Institute of Biotechnology, University of Manchester, 131 Princess Street Manchester, M1 7DN, United Kingdom and.
Mark D WhiteFrom the Manchester Institute of Biotechnology, University of Manchester, 131 Princess Street Manchester, M1 7DN, United Kingdom and.
Karl A P PayneFrom the Manchester Institute of Biotechnology, University of Manchester, 131 Princess Street Manchester, M1 7DN, United Kingdom and.
D A ParkerInnovation/Biodomain, Shell International Exploration and Production, Westhollow Technology Center, Houston, Texas 77082-3101.
Stephen E J RigbyFrom the Manchester Institute of Biotechnology, University of Manchester, 131 Princess Street Manchester, M1 7DN, United Kingdom and.
David LeysFrom the Manchester Institute of Biotechnology, University of Manchester, 131 Princess Street Manchester, M1 7DN, United Kingdom and david.leys@manchester.ac.uk.
University of Manchester · GBShell (United States) · US

Funding

Biotechnology and Biological Sciences Research Council BB/E013007/1Biotechnology and Biological Sciences Research Council BB/K017802/1Biotechnology and Biological Sciences Research Council BB/P000622/1
6 · The paper itself

Abstract

The activity of the reversible decarboxylase enzyme Fdc1 is dependent on prenylated FMN (prFMN), a recently discovered cofactor. The oxidized prFMN supports a 1,3-dipolar cycloaddition mechanism that underpins reversible decarboxylation. Fdc1 is a distinct member of the UbiD family of enzymes, with the canonical UbiD catalyzing the (de)carboxylation of

Indexed as

Binding SitesCarboxy-LyasesCrystallography, X-RayElectron Spin Resonance SpectroscopyElectron TransportEscherichia coliFlavin MononucleotideModels, MolecularOxidation-ReductionPrenylationProtein DomainsUbiquinone3-octaprenyl-4-hydroxybenzoate carboxy-lyaseCarboxy-LyasesFlavin MononucleotideUbiquinonecrystal structuredecarboxylaseelectron paramagnetic resonance (EPR)enzyme catalysisflavinubiquinone

Identifiers

PMID28057757
PMCPMC5377778
OpenAlexW2568201064

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.