Evidence map›Paper›PMID 22873401›Full record

ArticleBMC molecular biology2012

Structural/functional analysis of the human OXR1 protein: identification of exon 8 as the anti-oxidant encoding function.

Kenan C Murphy, Michael R Volkert

Open access · hybridAbstract read
In one paragraph

Article in BMC molecular biology, 2012. 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, 33 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Tender love and disassembly: How a TLDc domain protein breaks the V-ATPase.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023
    Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Induction of a unique isoform of the NCOA7 oxidation resistance gene by interferon β-1b.Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research · 2015
    Article
  16. Article
  17. Article
  18. 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

2 authors at 1 institution in 1 country.

Kenan C MurphyDepartment of Microbiology and Physiological Systems, University of Massachusetts Medical School, Worcester, MA 01655, USA. michael.volkert@umassmed.edu
Michael R Volkert
University of Massachusetts Chan Medical School · US

Funding

HUMAN OXIDATION RESISTANCE GENESR01CA100122 · NCI · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI VOLKERT, MICHAEL R · 2004 to 2007
$1.3M
NCI NIH HHS CA100122NCI NIH HHS R01 CA100122
6 · The paper itself

Abstract

backgroundThe human OXR1 gene belongs to a class of genes with conserved functions that protect cells from reactive oxygen species (ROS). The gene was found using a screen of a human cDNA library by its ability to suppress the spontaneous mutator phenotype of an E. coli mutH nth strain. The function of OXR1 is unknown. The human and yeast genes are induced by oxidative stress and targeted to the mitochondria; the yeast gene is required for resistance to hydrogen peroxide. Multiple spliced isoforms are expressed in a variety of human tissues, including brain.

resultsIn this report, we use a papillation assay that measures spontaneous mutagenesis of an E. coli mutM mutY strain, a host defective for oxidative DNA repair. Papillation frequencies with this strain are dependent upon a G→T transversion in the lacZ gene (a mutation known to occur as a result of oxidative damage) and are suppressed by in vivo expression of human OXR1. N-terminal, C-terminal and internal deletions of the OXR1 gene were constructed and tested for suppression of the mutagenic phenotype of the mutM mutY strain. We find that the TLDc domain, encoded by the final four exons of the OXR1 gene, is not required for papillation suppression in E. coli. Instead, we show that the protein segment encoded by exon 8 of OXR1 is responsible for the suppression of oxidative damage in E. coli.

conclusionThe protein segment encoded by OXR1 exon 8 plays an important role in the anti-oxidative function of the human OXR1 protein. This result suggests that the TLDc domain, found in OXR1 exons 12-16 and common in many proteins with nuclear function, has an alternate (undefined) role other than oxidative repair.

Indexed as

DNA PrimersEscherichia coliExonsGene Expression RegulationGene LibraryHumansMitochondriaMitochondrial ProteinsMutagenesisOxidative StressPlasmidsProteinsDNA PrimersMitochondrial ProteinsOXR1 protein, humanProteins

Identifiers

PMID22873401
PMCPMC3462732
OpenAlexW2170284861

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.