Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Role of a MutY DNA glycosylase in combating oxidative DNA damage in Helicobacter pylori.

DNA repair - 4 Jan 2007

Eutsey Rory, Wang Ge, Maier Robert J

Abstract excerpt

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....

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to DNA Damage
Share to DNA Glycosylases
Share to Genetic Complementation Test

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Guanine

Share to Helicobacter Infections

Share to Helicobacter pylori

Share to Oxidative Stress

Share to Stomach

Source

Open in PubMed Open full text

Identifiers

PMID: 16996809
DOI: 10.1016/j.dnarep.2006.08.006
PMCID: PMC1829490

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Role of a MutY DNA glycosylase in combating oxidative DNA damage in Helicobacter pylori.PMID 16996809Read ↗

Antimutator role of the DNA glycosylase mutY gene in Helicobacter pylori.Semantic proximity Read ↗

Evidence that MutY and MutM combine to prevent mutations by an oxidatively damaged form of guanine in DNA.Semantic proximity Read ↗

Mutational diversity in mutY deficient Helicobacter pylori and its effect on adaptation to the gastric environment.Semantic proximity Read ↗

The Helicobacter pylori MutS protein confers protection from oxidative DNA damageSemantic proximity Read ↗

MutY and MutY homologs (MYH) in genome maintenance.Semantic proximity Read ↗

Helicobacter pylori genes involved in avoidance of mutations induced by 8-oxoguanine.Semantic proximity Read ↗

Escherichia coli MutY protein has a guanine-DNA glycosylase that acts on 7,8-dihydro-8-oxoguanine:guanine mispair to prevent spontaneous G:C-->C:G transversions.Semantic proximity Read ↗

Mutations in the mutY gene of Escherichia coli enhance the frequency of targeted G:C-->T:a transversions induced by a single 8-oxoguanine residue in single-stranded DNA.Semantic proximity Read ↗

The C-terminal domain of MutY glycosylase determines the 7,8-dihydro-8-oxo-guanine specificity and is crucial for mutation avoidance.Semantic proximity Read ↗

A distinct physiological role of MutY in mutation prevention in mycobacteria.Semantic proximity Read ↗

MUTYH DNA glycosylase: the rationale for removing undamaged bases from the DNASemantic proximity Read ↗

Insight into the roles of tyrosine 82 and glycine 253 in the Escherichia coli adenine glycosylase MutY.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.