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

Coordination of DNA repair by NEIL1 and PARP-1: a possible link to aging

26 Oct 2012

Abstract excerpt

Oxidative DNA damage accumulates with age and is repaired primarily via the base excision repair (BER) pathway. This process is initiated by DNA glycosylases, which remove damaged bases in a substrate-specific manner. The DNA glycosylases human 8-oxoguanine-DNA glycosylase (OGG1) and NEIL1, a mammalian homolog ofEscherichia coli endonuclease VIII, have overlapping yet distinct substrate specificity. Recently, we...

Read the complete abstract on PubMed

Topics

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

Share to CRISPR and Genetic Engineering
Share to DNA Repair Mechanisms
Share to PARP inhibition in cancer therapy

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 23104860
DOI: 10.18632/aging.100492

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Coordination of DNA repair by NEIL1 and PARP-1: a possible link to agingPMID 23104860Read ↗

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

NEIL1 and NEIL2 Are Recruited as Potential Backup for OGG1 upon OGG1 Depletion or Inhibition by TH5487.Semantic proximity Read ↗

Interaction between RECQL4 and OGG1 promotes repair of oxidative base lesion 8-oxoG and is regulated by SIRT1 deacetylaseSemantic 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 ↗

Interaction of the human DNA glycosylase NEIL1 with proliferating cell nuclear antigen. The potential for replication-associated repair of oxidized bases in mammalian genomes.Semantic proximity Read ↗

Identification and characterization of a human DNA glycosylase for repair of modified bases in oxidatively damaged DNA.Semantic proximity Read ↗

Pleiotropic Cellular Functions of PARP1 in Longevity and Aging: Genome Maintenance Meets InflammationSemantic proximity Read ↗

PARP-1: Friend or Foe of DNA Damage and Repair in Tumorigenesis?Semantic proximity Read ↗

Major oxidative products of cytosine are substrates for the nucleotide incision repair pathway.Semantic proximity Read ↗

Phosphorylation Sites Identified in the NEIL1 DNA Glycosylase Are Potential Targets for the JNK1 Kinase.Semantic proximity Read ↗

Human Apurinic/Apyrimidinic Endonuclease 1Semantic proximity Read ↗

Barrier-to-autointegration factor 1 (Banf1) regulates poly [ADP-ribose] polymerase 1 (PARP1) activity following oxidative DNA damage.Semantic proximity Read ↗

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