Evidence map›Paper›PMID 16321958›Full record

ArticleJournal of bacteriology2005

FpvA-mediated ferric pyoverdine uptake in Pseudomonas aeruginosa: identification of aromatic residues in FpvA implicated in ferric pyoverdine binding and transport.

Jiang-Sheng Shen, Valérie Geoffroy, Shadi Neshat, Zongchao Jia, Allison Meldrum, Jean-Marie Meyer, Keith Poole

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.9field-weighted citation impact, top 24% 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

7 citing papers in PubMed, 19 citations in OpenAlex.

  1. The biosynthesis of pyoverdines.Microbial cell (Graz, Austria) · 2018
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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

7 authors at 3 institutions in 2 countries.

Jiang-Sheng ShenDepartment of Microbiology and Immunology, Queen's University, Kingston, Ontario K7L 3N6, Canada.
Valérie Geoffroy
Shadi Neshat
Zongchao Jia
Allison Meldrum
Jean-Marie Meyer
Keith Poole
Queen's University · CACentre National de la Recherche Scientifique · FRGénétique Moléculaire Génomique Microbiologie · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A number of aromatic residues were seen to cluster in the upper portion of the three-dimensional structure of the FpvA ferric pyoverdine receptor of Pseudomonas aeruginosa, reminiscent of the aromatic binding pocket for ferrichrome in the FhuA receptor of Escherichia coli. Alanine substitutions in three of these, W362, W391, and F795, markedly compromised ferric pyoverdine binding and transport, consistent with a role of FpvA in ferric pyoverdine recognition.

Indexed as

DNA Mutational AnalysisAmino Acid SubstitutionBacterial Outer Membrane ProteinsBiological TransportEscherichia coli ProteinsModels, MolecularMutagenesis, Site-DirectedOligopeptidesProtein BindingProtein ConformationPseudomonas aeruginosaReceptors, VirusBacterial Outer Membrane ProteinsEscherichia coli ProteinsFhuA protein, E coliFpvA protein, Pseudomonas aeruginosaOligopeptidespyoverdinReceptors, Virus

Identifiers

PMID16321958
PMCPMC1317021
OpenAlexW2098013517

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.