Evidence map›Paper›PMID 26121694›Full record

ArticlePloS one2015

Ohr Protects Corynebacterium glutamicum against Organic Hydroperoxide Induced Oxidative Stress.

Meiru Si, Jianbo Wang, Xiao Xiao, Jingyuan Guan, Yaoling Zhang, Wei Ding, Muhammad Tausif Chaudhry, Yao Wang, Xihui Shen

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.5field-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

18 citing papers in PubMed, 38 citations in OpenAlex.

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  9. Mechanisms of TLR4-Mediated Autophagy and Nitroxidative Stress.Frontiers in cellular and infection microbiology · 2021
    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

9 authors at 2 institutions in 2 countries.

Meiru SiState Key Laboratory of Crop Stress Biology for Arid Areas, Northwest A&F University, Yangling, Shaanxi, 712100, P. R. China.
Jianbo WangDepartment of Biochemistry and Molecular Biology, College of Life Sciences, Northwest A&F University, Yangling, Shaanxi, 712100, P. R. China.
Xiao XiaoState Key Laboratory of Crop Stress Biology for Arid Areas, Northwest A&F University, Yangling, Shaanxi, 712100, P. R. China.
Jingyuan GuanDepartment of Biochemistry and Molecular Biology, College of Life Sciences, Northwest A&F University, Yangling, Shaanxi, 712100, P. R. China.
Yaoling ZhangState Key Laboratory of Crop Stress Biology for Arid Areas, Northwest A&F University, Yangling, Shaanxi, 712100, P. R. China.
Wei DingState Key Laboratory of Crop Stress Biology for Arid Areas, Northwest A&F University, Yangling, Shaanxi, 712100, P. R. China.
Muhammad Tausif ChaudhryEnvironmental Analytical Laboratory, National Physical & Standards Laboratory, PCSIR, Islamabad, Pakistan.
Yao WangDepartment of Biochemistry and Molecular Biology, College of Life Sciences, Northwest A&F University, Yangling, Shaanxi, 712100, P. R. China.
Xihui ShenState Key Laboratory of Crop Stress Biology for Arid Areas, Northwest A&F University, Yangling, Shaanxi, 712100, P. R. China.
Northwest A&F University · CNNational Centre of Excellence in Analytical Chemistry · PK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ohr, a bacterial protein encoded by the Organic Hydroperoxide Resistance (ohr) gene, plays a critical role in resistance to organic hydroperoxides. In the present study, we show that the Cys-based thiol-dependent Ohr of Corynebacterium glutamicum decomposes organic hydroperoxides more efficiently than hydrogen peroxide. Replacement of either of the two Cys residues of Ohr by a Ser residue resulted in drastic loss of activity. The electron donors supporting regeneration of the peroxidase activity of the oxidized Ohr of C. glutamicum were principally lipoylated proteins (LpdA and Lpd/SucB). A Δohr mutant exhibited significantly decreased resistance to organic hydroperoxides and marked accumulation of reactive oxygen species (ROS) in vivo; protein carbonylation was also enhanced notably. The resistance to hydrogen peroxide also decreased, but protein carbonylation did not rise to any great extent. Together, the results unequivocally show that Ohr is essential for mediation of organic hydroperoxide resistance by C. glutamicum.

Indexed as

Amino Acid SequenceBacterial ProteinsCorynebacterium glutamicumEnzyme ActivationGene Expression Regulation, BacterialHydrogen PeroxideKineticsMicrobial ViabilityMolecular Sequence DataMutationOxidation-ReductionOxidative StressPeroxidasesReactive Oxygen SpeciesSequence AlignmentBacterial ProteinsHydrogen PeroxidePeroxidasesReactive Oxygen Species

Identifiers

PMID26121694
PMCPMC4486171
OpenAlexW1574002303

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.