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- W1969964329 abstract "About 23% of mutations in hereditary human diseases and 24% of mutations in p53 in human cancers are G to A transitions at sites of cytosine methylation suggesting that these sites are either foci for DNA damage, or foci for damage that is poorly repaired. Thymine produced at these sites by the hydrolytic deamination of 5-methylcytosine is removed by thymine-DNA glycosylase. Thymine-DNA glycosylase will also remove 3,N(4)-ethenocytosine and uracil from DNA. The action of this enzyme is limited by its very low k(cat) and by tight binding to the apurinic site produced when the thymine is removed. These properties of the enzyme suggest that the inefficiency of the base excision repair pathway that it initiates may be the underlying cause of the prevalence of these mutations." @default.
- W1969964329 created "2016-06-24" @default.
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- W1969964329 date "2000-04-01" @default.
- W1969964329 modified "2023-09-30" @default.
- W1969964329 title "Thymine-DNA glycosylase and G to A transition mutations at CpG sites" @default.
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- W1969964329 doi "https://doi.org/10.1016/s1383-5742(00)00031-4" @default.
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