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Enzymatic repair of 5-formyluracil. I. Excision of 5-formyluracil site-specifically incorporated into oligonucleotide substrates by alka protein (Escherichia coli 3-methyladenine DNA glycosylase II).
Masaoka A, Terato H, Kobayashi M, Honsho A, Ohyama Y, Ide H. Masaoka A, et al. J Biol Chem. 1999 Aug 27;274(35):25136-43. doi: 10.1074/jbc.274.35.25136. J Biol Chem. 1999. PMID: 10455195 Free article.
Therefore, fU can exist in DNA as a correctly paired fU:A form or an incorrectly paired fU:G form. In this work, fU was site-specifically incorporated opposite A in oligonucleotide substrates to delineate the cellular repair mechanism of fU paired with A
Therefore, fU can exist in DNA as a correctly paired fU:A form or an incorrectly paired fU:G form. In this work, fU was site-s …
Enzymatic repair of 5-formyluracil. II. Mismatch formation between 5-formyluracil and guanine during dna replication and its recognition by two proteins involved in base excision repair (AlkA) and mismatch repair (MutS).
Terato H, Masaoka A, Kobayashi M, Fukushima S, Ohyama Y, Yoshida M, Ide H. Terato H, et al. Among authors: masaoka a. J Biol Chem. 1999 Aug 27;274(35):25144-50. doi: 10.1074/jbc.274.35.25144. J Biol Chem. 1999. PMID: 10455196 Free article.
5-Formyluracil (fU), a major methyl oxidation product of thymine, forms correct (fU:A) and incorrect (fU:G) base pairs during DNA replication. In the accompanying paper (Masaoka, A., Terato, H., Kobayashi, M., Honsho, A., Ohyama, Y., and Ide, H. …
5-Formyluracil (fU), a major methyl oxidation product of thymine, forms correct (fU:A) and incorrect (fU:G) base pairs during …
279 results