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

A monofunctional-like mutant of DNA glycosylase NTHL1 changes the dynamics of DNA repair during acute oxidative stress.

The Journal of biological chemistry - 1 Apr 2026

Haslam James, Rudolfova Natalie, Zhou Kaixin, Homan Evert, Jemth Ann-Sofie, Michel Maurice, Helleday Thomas, Mortusewicz Oliver

Abstract excerpt

Bifunctional DNA glycosylases, which initiate the base excision repair (BER) of oxidized bases, act by first excising the base and then incising the DNA backbone. In vitro, these enzymes are often rate-limited by their apurinic/apyrimidinic (AP)-lyase activity; however, the significance of this step in cells has remained unclear, because AP-endonuclease 1 (APE1) can efficiently bypass this step. To analyze the...

Read the complete abstract on PubMed

Topics

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

Share to Deoxyribonuclease (Pyrimidine Dimer)
Share to DNA-(Apurinic or Apyrimidinic Site) Lyase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to DNA Glycosylases

Share to DNA Repair

Share to XRCC1 gene

Share to Mutation

Share to Oxidative Stress

Source

Open in PubMed Open full text

Identifiers

PMID: 41763309
DOI: 10.1016/j.jbc.2026.111332
PMCID: PMC13022620

Genes

NTHL1
XRCC1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A monofunctional-like mutant of DNA glycosylase NTHL1 changes the dynamics of DNA repair during acute oxidative stress.PMID 41763309Read ↗

DNA repair glycosylase hNEIL1 triages damaged bases via competing interaction modes.Semantic proximity Read ↗

Functional Impact of Nth-like DNA glycosylase on Mitochondrial DynamicsSemantic proximity Read ↗

Base Excision Repair: Mechanisms and Impact in Biology, Disease, and MedicineSemantic proximity Read ↗

Base excision repair of oxidative DNA damage: from mechanism to disease.Semantic proximity Read ↗

Heritable pattern of oxidized DNA base repair coincides with pre-targeting of repair complexes to open chromatin.Semantic proximity Read ↗

The novel DNA glycosylase, NEIL1, protects mammalian cells from radiation-mediated cell death.Semantic proximity Read ↗

New paradigms in the repair of oxidative damage in human genome: mechanisms ensuring repair of mutagenic base lesions during replication and involvement of accessory proteins.Semantic proximity Read ↗

Unique structural features of mammalian NEIL2 DNA glycosylase prime its activity for diverse DNA substrates and environmentsSemantic proximity Read ↗

Inspiring basic and applied research in genome integrity mechanisms: Dedication to Samuel H. Wilson.Semantic proximity Read ↗

NTHL1 in genomic integrity, aging and cancer.Semantic proximity Read ↗

Processing of oxidatively damaged DNA dirty ends by APE1Semantic proximity Read ↗

A Dynamic Search Mechanism Enables APE1 to Identify AP-Sites in DNASemantic proximity Read ↗

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