DNA glycosylase activities for thymine residues oxidized in the methyl group are functions of the AlkA enzyme in Escherichia coli (original) (raw)
DNA glycosylase activities for thymine residues damaged by ring saturation, fragmentation, or ring contraction are functions of endonuclease III in Escherichia coli
Lars Breimer
Journal of Biological Chemistry, 1984
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The Journal of biological chemistry, 1982
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1987
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AlkA Protein Is the Third Escherichia coli DNA Repair Protein Excising a Ring Fragmentation Product of Thymine †
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Molecular Microbiology, 1992
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Separating Substrate Recognition from Base Hydrolysis in Human Thymine DNA Glycosylase by Mutational Analysis
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[methyl-3H]Thymidine in DNA induces lesions which are recognized by a mammalian DNA-repair endonuclease
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Relative efficiencies of the bacterial, yeast, and human DNA methyltransferases for the repair of O6-methylguanine and O4-methylthymine. Suggestive evidence for O4-methylthymine repair by eukaryotic methyltransferases
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The Journal of biological chemistry, 1991
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Janet Salisbury
Chemico-Biological Interactions, 1976
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3,N4-ethenocytosine, a highly mutagenic adduct, is a primary substrate for Escherichia coli double-stranded uracil-DNA glycosylase and human mismatch-specific thymine-DNA glycosylase
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