Evidence map›Paper›PMID 12485986›Full record

ArticleThe EMBO journal2002

Structural and functional characterization of the Pseudomonas hydroperoxide resistance protein Ohr.

Jacob Lesniak, William A Barton, Dimitar B Nikolov

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
1.8field-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

52 citing papers in PubMed, 98 citations in OpenAlex.

  1. Article
  2. Article
  3. Thiol Reductases inAntioxidants (Basel, Switzerland) · 2022
    Review
  4. Organic Hydroperoxide Resistance GeneApplied and environmental microbiology · 2021
    Article
  5. Article
  6. Article
  7. Article
  8. TheJournal of bacteriology · 2019
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Ohr plays a central role in bacterial responses against fatty acid hydroperoxides and peroxynitrite.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  15. Draft Genome Sequence of the Nitrogen-FixingFrontiers in microbiology · 2017
    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

3 authors at 1 institution in 1 country.

Jacob LesniakJoan and Sanford I.Weill Graduate School of Medical Sciences of Cornell University, New York City, NY 10021, USA.
William A Barton
Dimitar B Nikolov
Cornell University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bacteria have developed complex strategies to detoxify and repair damage caused by reactive oxygen species. These compounds, produced during bacterial aerobic respiration as well as by the host immune system cells as a defense mechanism against the pathogenic microorganisms, have the ability to damage nucleic acids, proteins and phospholipid membranes. Here we describe the crystal structure of Pseudomonas aeruginosa Ohr, a member of a recently discovered family of organic hydroperoxide resistance proteins. Ohr is a tightly folded homodimer, with a novel alpha/beta fold, and contains two active sites located at the monomer interface on opposite sides of the molecule. Using in vitro assays, we demonstrate that Ohr functions directly as a hydroperoxide reductase, converting both inorganic and organic hydroperoxides to less toxic metabolites. Site-directed mutagenesis confirms that the two conserved cysteines in each active site are essential for catalytic activity. We propose that the Ohr catalytic mechanism is similar to that of the structurally unrelated peroxiredoxins, directly utilizing highly reactive cysteine thiol groups to elicit hydroperoxide reduction.

Indexed as

Drug ResistanceAmino Acid SequenceBacterial ProteinsBinding SitesCatalytic DomainCrystallography, X-RayDimerizationDose-Response Relationship, DrugEscherichia coliHydrogen PeroxideModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedOxidative StressPeroxidasePeroxidasesBacterial ProteinsHydrogen Peroxideorganic hydroperoxide resistance protein, Xanthomonas campestrisPeroxidasePeroxidasesPeroxiredoxins

Identifiers

PMID12485986
PMCPMC139091
OpenAlexW2081213093

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.