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

NEIL1 mRNA splicing variants are expressed in normal mouse organs.

Journal of radiation research - 1 Jan 2012

Yamamoto Ryohei, Yamamoto Mizuki, Kusaka Hiroyuki, Masatsugu Hideaki, Matsuyama Satoshi, Tajima Tomoko, Ide Hiroshi, Kubo Kihei

Abstract excerpt

Oxidized pyrimidines are mainly repaired by base excision repair, which is initiated by damage-specific DNA glycosylases. NEIL1, the mammalian homolog of Escherichia coli endonuclease VIII and a major DNA glycosylase, initiates repair of oxidized pyrimidines. Here, we investigated the expression of two putative variant mouse NEIL1 (mNEIL1) mRNAs--variant 1 ("Neil1 protein" mRNA; BC043297 in the NCBI database) and...

Read the complete abstract on PubMed

Topics

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

Share to DNA Glycosylases
Share to Alternative Splicing

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Mice, Inbred ICR

Share to Organ Specificity

Share to Reference Values

Share to RNA Splicing

Share to Tissue Distribution

Share to Viscera

Source

Identifiers

PMID: 22510596
DOI: 10.1269/jrr.11029

Genes

NEIL1

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

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

NEIL1 mRNA splicing variants are expressed in normal mouse organs.PMID 22510596Read ↗

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

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

Uracil–DNA glycosylase UNG1 isoform variant supports class switch recombination and repairs nuclear genomic uracilSemantic proximity Read ↗

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

Inactivating mutations of the human base excision repair gene NEIL1 in gastric cancer.Semantic proximity Read ↗

The mouse and human genes encoding the recognition component of the N-end rule pathwaySemantic proximity Read ↗

Targeted deletion of the genes encoding NTH1 and NEIL1 DNA N-glycosylases reveals the existence of novel carcinogenic oxidative damage to DNA.Semantic proximity Read ↗

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

Arginyltransferase, its specificity, putative substrates, bidirectional promoter, and splicing-derived isoforms.Semantic proximity Read ↗

Biochemical and molecular analysis of spontaneous and induced mutations at the mouse Mod-1 locus.Semantic proximity Read ↗

Molecular characterization of the DYX1C1 gene and its application as a cancer biomarker.Semantic proximity Read ↗

Expression of high in normal-1 (HIN-1) and uteroglobin related protein-1 (UGRP-1) in adult and developing tissues.Semantic proximity Read ↗

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