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Article

Identification of a zinc finger domain in the human NEIL2 (Nei-like-2) protein.

The Journal of biological chemistry - 5 Nov 2004

Das Aditi, Rajagopalan Lavanya, Mathura Venkatarajan S, Rigby Samuel J, Mitra Sankar, Hazra Tapas K

Abstract excerpt

The recently identified human NEIL2 (Nei-like-2) protein, a DNA glycosylase/AP lyase specific for oxidatively damaged bases, shares structural features and reaction mechanism with the Escherichia coli DNA glycosylases, Nei and Fpg. Amino acid sequence analysis of NEIL2 suggested it to have a zinc finger-like Nei/Fpg. However, the Cys-X2-His-X16-Cys-X2-Cys (CHCC) motif present near the C terminus of NEIL2 is...

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Source

Identifiers

PMID: 15339932
DOI: 10.1074/jbc.M406224200

Genes

NEIL2

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

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

Identification of a zinc finger domain in the human NEIL2 (Nei-like-2) protein.PMID 15339932Read ↗

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

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

Increased risk of lung cancer associated with a functionally impaired polymorphic variant of the human DNA glycosylase NEIL2.Semantic proximity Read ↗

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

Single nucleotide polymorphisms 5' upstream the coding region of the NEIL2 gene influence gene transcription levels and alter levels of genetic damage.Semantic proximity Read ↗

Identification and validation of Nei-like DNA glycosylase 2 as a novel prognostic biomarker in cervical cancerSemantic 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 ↗

Acetylation of the human DNA glycosylase NEIL2 and inhibition of its activity.Semantic proximity Read ↗

Human NEIL3 is mainly a monofunctional DNA glycosylase removing spiroimindiohydantoin and guanidinohydantoin.Semantic proximity Read ↗

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

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

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

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