Evidence map›Paper›PMID 29208656›Full record

ArticleThe Journal of biological chemistry2018

PvdO is required for the oxidation of dihydropyoverdine as the last step of fluorophore formation in

Michael T Ringel, Gerald Dräger, Thomas Brüser

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 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.1field-weighted citation impact, top 18% 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

13 citing papers in PubMed, 28 citations in OpenAlex.

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  12. The Journal of biological chemistry · 2018
    Article
  13. The biosynthesis of pyoverdines.Microbial cell (Graz, Austria) · 2018
    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

3 authors at 1 institution in 1 country.

Michael T RingelFrom the Institute of Microbiology, Leibniz Universität Hannover, Herrenhäuser Strasse 2, 30419 Hannover, Germany and.
Gerald Drägerthe Institute of Organic Chemistry, Leibniz Universität Hannover, Schneiderberg 1 B, 30167 Hannover, Germany.
Thomas BrüserFrom the Institute of Microbiology, Leibniz Universität Hannover, Herrenhäuser Strasse 2, 30419 Hannover, Germany and brueser@ifmb.uni-hannover.de.
Leibniz University Hannover · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pyoverdines are important siderophores that guarantee iron supply to important pathogenic and non-pathogenic pseudomonads in host habitats. A key characteristic of all pyoverdines is the fluorescent dihydroxyquinoline group that contributes two ligands to the iron complexes. Pyoverdines are derived from the non-ribosomally synthesized peptide ferribactin, and their fluorophore is generated by periplasmic oxidation and cyclization reactions of d-tyrosine and l-diaminobutyric acid. The formation of the fluorophore is known to be driven by the periplasmic tyrosinase PvdP. Here we report that the putative periplasmic oxidoreductase PvdO of

Indexed as

Amino Acid MotifsBacterial ProteinsCatalytic DomainCrystallography, X-RayOligopeptidesOxidation-ReductionOxidoreductasesPeriplasmPseudomonas fluorescensBacterial ProteinsOligopeptidesOxidoreductasespyoverdinbiosynthesisfluorophore formationironoxidation-reduction (redox)periplasmic maturationPseudomonasPseudomonas fluorescenspyoverdinessiderophore

Identifiers

PMID29208656
PMCPMC5818194
OpenAlexW2771303901

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.