ArticleDNA repair2007
Role of a MutY DNA glycosylase in combating oxidative DNA damage in Helicobacter pylori.
Article in DNA repair, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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.
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.
Who cites it
17 citing papers in PubMed, 38 citations in OpenAlex.
- Toad's survivability and soil microbiome alterations impacted via individual abundance.Biologia futura · 2025Article
- An interstrand DNA crosslink glycosylase aidsProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Antibiotic-induced ROS-mediated Fur allosterism contributes toAntimicrobial agents and chemotherapy · 2024Article
- Helicobacter pylori diversification during chronic infection within a single host generates sub-populations with distinct phenotypes.PLoS pathogens · 2020Article
- Inhibitors of DNA Glycosylases as Prospective Drugs.International journal of molecular sciences · 2020Review
- A Mutator Phenotype Promoting the Emergence of Spontaneous Oxidative Stress-Resistant Mutants in Campylobacter jejuni.Applied and environmental microbiology · 2017Article
- Oxidative and nitrosative stress defences of Helicobacter and Campylobacter species that counteract mammalian immunity.FEMS microbiology reviews · 2016Article
- A novel DNA-binding protein plays an important role in Helicobacter pylori stress tolerance and survival in the host.Journal of bacteriology · 2015Article
- The BER necessities: the repair of DNA damage in human-adapted bacterial pathogens.Nature reviews. Microbiology · 2015Review
- A histone-like protein of Helicobacter pylori protects DNA from stress damage and aids host colonization.DNA repair · 2012Article
- Mutation of the NADH oxidase gene (nox) reveals an overlap of the oxygen- and acid-mediated stress responses in Streptococcus mutans.Applied and environmental microbiology · 2012Article
- Unexpected role for Helicobacter pylori DNA polymerase I as a source of genetic variability.PLoS genetics · 2011Article
- Porphyromonas gingivalis mutY is involved in the repair of oxidative stress-induced DNA mispairing.Molecular oral microbiology · 2011Article
- Antibiotic resistance in Pseudomonas aeruginosa strains with increased mutation frequency due to inactivation of the DNA oxidative repair system.Antimicrobial agents and chemotherapy · 2009Article
- Genome dynamics in major bacterial pathogens.FEMS microbiology reviews · 2009Review
- Mosaic DNA imports with interspersions of recipient sequence after natural transformation of Helicobacter pylori.PloS one · 2008Article
- Critical role of RecN in recombinational DNA repair and survival of Helicobacter pylori.Infection and immunity · 2008Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
MutY is an adenine glycosylase that has the ability to efficiently remove adenines from adenine/7,8-dihydro-8-oxoguanine (8-oxo-G) or adenine/guanine mismatches, and plays an important role in oxidative DNA damage repair. The human gastric pathogen Helicobacter pylori has a homolog of the MutY enzyme. To investigate the physiological roles of MutY in H. pylori, we constructed and characterized a mutY mutant. H. pylori mutY mutants incubated at 5% O2 have a 325-fold higher spontaneous mutation rate than its parent. The mutation rate is further increased by exposing the mutant to atmospheric levels of oxygen, an effect that is not seen in an E. coli mutY mutant. Most of the mutations that occurred in H. pylori mutY mutants, as examined by rpoB sequence changes that confer rifampicin resistance, are GC to TA transversions. The H. pylori enzyme has the ability to complement an E. coli mutY mutant, restoring its mutation frequency to the wild-type level. Pure H. pylori MutY has the ability to remove adenines from A/8-oxo-G mismatches, but strikingly no ability to cleave A/G mismatches. This is surprising because E. coli MutY can more rapidly turnover A/G than A/8-oxo-G. Thus, H. pylori MutY is an adenine glycosylase involved in the repair of oxidative DNA damage with a specificity for detecting 8-oxo-G. In addition, H. pylori mutY mutants are only 30% as efficient as wild-type in colonizing the stomach of mice, indicating that H. pylori MutY plays a significant role in oxidative DNA damage repair in vivo.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.