Evidence map›Paper›PMID 23056345›Full record

ArticlePloS one2012

A novel insight into the oxidoreductase activity of Helicobacter pylori HP0231 protein.

Paula Roszczenko, Katarzyna A Radomska, Ewa Wywial, Jean-Francois Collet, Elzbieta K Jagusztyn-Krynicka

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

24 citing papers in PubMed, 31 citations in OpenAlex.

  1. Potential pathogenesis ofFuture science OA · 2026
    Article
  2. Exploring the inhibitory potential ofFrontiers in molecular biosciences · 2023
    Article
  3. Article
  4. Evolution ofPeerJ · 2022
    Article
  5. Interplay between DsbA1, DsbA2 and C8J_1298 Periplasmic Oxidoreductases ofInternational journal of molecular sciences · 2021
    Article
  6. Review
  7. Article
  8. Cysteine Residues inMicroorganisms · 2020
    Article
  9. Article
  10. Article
  11. Disulfide bond formation in prokaryotes.Nature microbiology · 2018
    Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

5 authors at 4 institutions in 2 countries.

Paula RoszczenkoDepartment of Bacterial Genetics, Institute of Microbiology, the University of Warsaw, Warsaw, Poland.
Katarzyna A Radomska
Ewa Wywial
Jean-Francois Collet
Elzbieta K Jagusztyn-Krynicka
University of Warsaw · PLCollege of Europe, Warsaw · PLInternational Institute of Molecular and Cell Biology · PLWalloon Excellence in Lifesciences and Biotechnology · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe formation of a disulfide bond between two cysteine residues stabilizes protein structure. Although we now have a good understanding of the Escherichia coli disulfide formation system, the machineries at work in other bacteria, including pathogens, are poorly characterized. Thus, the objective of this work was to improve our understanding of the disulfide formation machinery of Helicobacter pylori, a leading cause of ulcers and a risk factor for stomach cancer worldwide. METHODS AND

resultsThe protein HP0231 from H. pylori, a structural counterpart of E. coli DsbG, is the focus of this research. Its function was clarified by using a combination of biochemical, microbiological and genetic approaches. In particular, we determined the biochemical properties of HP0231 as well as its redox state in H. pylori cells.

conclusionAltogether our results show that HP0231 is an oxidoreductase that catalyzes disulfide bond formation in the periplasm. We propose to call it HpDsbA.

Indexed as

Genetic Complementation TestHelicobacter pyloriMicroscopy, Electron, TransmissionMutagenesisOxidoreductasesPlasmidsReverse Transcriptase Polymerase Chain ReactionOxidoreductases

Identifiers

PMID23056345
PMCPMC3463561
OpenAlexW2125712585

What OpenQuestion holds

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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.