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Article

Repair of oxidized bases in DNA bubble structures by human DNA glycosylases NEIL1 and NEIL2.

The Journal of biological chemistry - 12 Dec 2003

Dou Hong, Mitra Sankar, Hazra Tapas K

Abstract excerpt

Repair of oxidatively damaged bases in the genome via the base excision repair pathway is initiated with excision of these lesions by DNA glycosylases with broad substrate range. The newly discovered human DNA glycosylases, NEIL1 and NEIL2, are distinct in structural features and reaction mechani...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 14522990
DOI: 10.1074/jbc.M308658200

Genes

OGG1
NEIL1
NEIL2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-14522990-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

Repair of oxidized bases in DNA bubble structures by human DNA glycosylases NEIL1 and NEIL2.PMID 14522990Read ↗

Mutation versus repair: NEIL1 removal of hydantoin lesions in single-stranded, bulge, bubble, and duplex DNA contexts.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 ↗

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 ↗

Human endonuclease VIII-like (NEIL) proteins in the giant DNA Mimivirus.Semantic proximity Read ↗

Mutator phenotype of mammalian cells due to deficiency of NEIL1 DNA glycosylase, an oxidized base-specific repair enzyme.Semantic proximity Read ↗

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

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

Functional roles and cancer variants of the bifunctional glycosylase NEIL2Semantic proximity Read ↗

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

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

Human polymorphic variants of the NEIL1 DNA glycosylase.Semantic proximity Read ↗

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