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1 ndonucleases Nth (endonuclease III) and Fpg (formamidopyrimidine DNA glycosylase).
2 dative stress and are efficiently excised by formamidopyrimidine DNA glycosylase.
3 ndo III), endonuclease VIII (endo VIII), and formamidopyrimidine DNA glycosylase.
4 igestion by the enzymes endonuclease III and formamidopyrimidine DNA glycosylase.
5 with the repair enzymes endonuclease III and formamidopyrimidine DNA glycosylase.
6 ares structural and functional homology with formamidopyrimidine-DNA glycosylase.
8 fferent damage products sensitive to E. coli formamidopyrimidine DNA glycosylase and hot piperidine,
9 at oxidized bases with endonuclease III and formamidopyrimidine DNA glycosylase and then using the l
10 Rs using RNase H and two DNA repair enzymes (formamidopyrimidine DNA glycosylase and uracil-DNA glyco
11 sylases of the base excision repair pathway: formamidopyrimidine-DNA glycosylase and 8-oxoguanine DNA
12 ing oxidative DNA damage (sites sensitive to formamidopyrimidine-DNA glycosylase and single-strand br
15 amage was quantitated using Escherichia coli formamidopyrimidine DNA glycosylase (Fpg) in a gene-spec
16 approach was based on digestion of DNA with formamidopyrimidine DNA glycosylase (FPG) to convert 8-o
19 oxoG), is processed by two DNA glycosylases, formamidopyrimidine DNA glycosylase (Fpg), which removes
24 es have been identified for Escherichia coli formamidopyrimidine-DNA glycosylase (Fpg) and Drosophila
25 alf-life of Schiff bases formed when E. coli formamidopyrimidine-DNA glycosylase (Fpg) and endonuclea
27 is initiated by DNA glycosylases such as the formamidopyrimidine-DNA glycosylase (Fpg) in Escherichia
31 ed by treatment with either Escherichia coli formamidopyrimidine-DNA glycosylase (Fpg), Escherichia c
32 counterpart, guanine, by the repair enzyme, formamidopyrimidine-DNA glycosylase (Fpg), likely involv
33 and comet analysis revealed introduction of formamidopyrimidine-DNA glycosylase (Fpg)-sensitive oxid
37 on (lactoglyglutathione lyase gene), repair (formamidopyrimidine-DNA glycosylase gene), osmotic prote
38 Endo VIII do not serve as back up enzymes to formamidopyrimidine DNA glycosylase in the repair of for
39 ybrids were used as substrates for bacterial formamidopyrimidine-DNA glycosylase, Nth protein (endonu
40 displayed subtle biases in damage chemistry (formamidopyrimidine DNA glycosylase/piperidine ratio).
41 t Ug was a better substrate for endo III and formamidopyrimidine DNA glycosylase than Tg; for endonuc