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Article

The mouse ortholog of NEIL3 is a functional DNA glycosylase in vitro and in vivo.

Proceedings of the National Academy of Sciences of the United States of America - 16 Mar 2010

Liu Minmin, Bandaru Viswanath, Bond Jeffrey P, Jaruga Pawel, Zhao Xiaobei, Christov Plamen P, Burrows Cynthia J, Rizzo Carmelo J, Dizdaroglu Miral, Wallace Susan S

Abstract excerpt

To protect cells from oxidative DNA damage and mutagenesis, organisms possess multiple glycosylases to recognize the damaged bases and to initiate the Base Excision Repair pathway. Three DNA glycosylases have been identified in mammals that are homologous to the Escherichia coli Fpg and Nei proteins, Neil1, Neil2, and Neil3. Neil1 and Neil2 in human and mouse have been well characterized while the properties of...

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Share to DNA Glycosylases
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 20185759
DOI: 10.1073/pnas.0908307107
PMCID: PMC2841873

Genes

NEIL3

Provenance

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Related research

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

The mouse ortholog of NEIL3 is a functional DNA glycosylase in vitro and in vivo.PMID 20185759Read ↗

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

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

Genome and cancer single nucleotide polymorphisms of the human NEIL1 DNA glycosylase: activity, structure, and the effect of editing.Semantic proximity Read ↗

No cancer predisposition or increased spontaneous mutation frequencies in NEIL DNA glycosylases-deficient mice.Semantic proximity Read ↗

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

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

NEIL1 mRNA splicing variants are expressed in normal mouse organs.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 ↗

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

The oxidative DNA glycosylases of Mycobacterium tuberculosis exhibit different substrate preferences from their Escherichia coli counterparts.Semantic proximity Read ↗

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

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

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