Evidence map›Paper›PMID 25964471›Full record

ArticleInfection and immunity2015

Comparative Roles of the Two Helicobacter pylori Thioredoxins in Preventing Macromolecule Damage.

Lisa G Kuhns, Ge Wang, Robert J Maier

Open access · bronzeAbstract read
In one paragraph

Article in Infection and immunity, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

16 citing papers in PubMed, 23 citations in OpenAlex.

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  5. Thiol Reductases inAntioxidants (Basel, Switzerland) · 2022
    Review
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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

3 authors at 1 institution in 1 country.

Lisa G KuhnsDepartment of Microbiology, The University of Georgia, Athens, Georgia, USA.
Ge WangDepartment of Microbiology, The University of Georgia, Athens, Georgia, USA.
Robert J MaierDepartment of Microbiology, The University of Georgia, Athens, Georgia, USA rmaier@uga.edu.
University of Georgia · US

Funding

Amino Acid Repair Activity in Helicobacter pyloriR01AI077569 · NIAID · UNIVERSITY OF GEORGIA · PI MAIER, ROBERT J. · 2009 to 2013
$1.8M
NIAID NIH HHS R01 AI077569NIAID NIH HHS R01AI077569
6 · The paper itself

Abstract

Thioredoxins are highly conserved throughout a wide range of organisms, and they are essential for the isurvival of oxygen-sensitive cells. The gastric pathogen Helicobacter pylori uses the thioredoxin system to maintain its thiol/disulfide balance. There are two thioredoxins present in H. pylori, Trx1 and Trx2 (herein referred to as TrxA and TrxC). TrxA has been shown to be important as an electron donor for some antioxidant enzymes, but the function of TrxC remains unknown (L. M. Baker, A. Raudonikiene, P. S. Hoffman, and L. B. Poole, J Bacteriol 183:1961-1973, 2001; P. Alamuri and R. J. Maier, J Bacteriol 188:5839-5850, 2006). We demonstrate that both TrxA and TrxC are important in protecting H. pylori from oxidative stress. Individual ΔtrxA and ΔtrxC deletion mutant strains each show a greater abundance of lipid peroxides and suffer more DNA damage and more protein carbonylation than the parent. Both deletion mutants were much more sensitive to O2-mediated viability loss than the parent. Unexpectedly, the oxidative DNA damage and protein carbonylation was more severe in the ΔtrxC mutant than in the ΔtrxA mutant; it had 20-fold- and 4-fold-more carbonylated protein content than the wild type and the ΔtrxA strain, respectively, after 4 h of atmospheric O2 stress. trx transcript abundance was altered by the deletion of the heterologous trx gene. The ΔtrxC mutant lacked mouse colonization ability, while the ability to colonize mouse stomachs was significantly reduced in the ΔtrxA mutant.

Indexed as

Oxidative StressStress, PhysiologicalAnimalsDNA DamageFemaleGene DeletionHelicobacter pyloriLipid PeroxidesMice, Inbred C57BLMicrobial ViabilityOxidantsProtein CarbonylationSalmonella Infections, AnimalThioredoxinsVirulenceLipid PeroxidesOxidantsThioredoxins

Identifiers

PMID25964471
PMCPMC4468550
OpenAlexW2141796402

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.