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Among various types of oxidative DNA damage, 8\u2010oxo\u20107,8\u2010dihydroguanine (8\u2010oxoguanine or 8\u2010oxoG) is the most abundant, and plays significant roles in mutagenesis because of its ability to pair with adenine as well as cytosine. Enzymatic activities that may be responsible for preventing 8\u2010oxoG\u2010evoked mutations were identified in mammalian cells. We have focused on the following three enzymes: MTH1, OGG1 and MUTYH. MTH1 is a mammalian ortholog of <jats:italic>Escherichia coli<\/jats:italic> MutT, which hydrolyzes 8\u2010oxo\u2010dGTP to its monophosphate form in nucleotide pools, thereby preventing incorporation of the mutagenic substrate into DNA. OGG1, a functional counterpart of <jats:italic>E.\u00a0coli<\/jats:italic> MutM, has an 8\u2010oxoG DNA glycosylase activity. MUTYH, a mammalian ortholog of <jats:italic>E.\u00a0coli<\/jats:italic> MutY, excises an adenine paired with 8\u2010oxoG. These three enzymes are thought to prevent mutagenesis caused by 8\u2010oxoG in mammals. To analyze the functions of mammalian MTH1 (Mth1), OGG1 (Ogg1) and MUTYH (Mutyh) <jats:italic>in\u00a0vivo<\/jats:italic>, we established mutant mice for these three enzymes by targeted mutagenesis, and investigated spontaneous tumorigenesis as well as mutagenesis. Here we discuss our recent investigation of mutagenesis and carcinogenesis in these mutant mice. 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