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Article

Loss of MUTYH function in human cells leads to accumulation of oxidative damage and genetic instability.

Oncogene - 19 Sept 2013

Ruggieri V, Pin E, Russo M T, Barone F, Degan P, Sanchez M, Quaia M, Minoprio A, Turco E, Mazzei F, Viel A, Bignami M

Abstract excerpt

The DNA glycosylase MUTYH (mutY homolog (Escherichia coli)) counteracts the mutagenic effects of 8-oxo-7,8-dihydroguanine (8-oxodG) by removing adenine (A) misincorporated opposite the oxidized purine. Biallelic germline mutations in MUTYH cause the autosomal recessive MUTYH-associated adenomatous polyposis (MAP). Here we designed new tools to investigate the biochemical defects and biological consequences...

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Topics

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 23108399
DOI: 10.1038/onc.2012.479

Genes

MUTYH
OGG1

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

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Loss of MUTYH function in human cells leads to accumulation of oxidative damage and genetic instability.PMID 23108399Read ↗

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