ライフサイエンスコーパス: formamidopyrimidine

1 roxy-5-formamidopyrimidine and 4,6-diamino-5-formamidopyrimidine.

2 ss and have a high basal level of endogenous formamidopyrimidines.

3 opyrimidine DNA glycosylase in the repair of formamidopyrimidines.

4 L1 possesses equal specificity for these two formamidopyrimidines.

5 dy examines the role of CSB in the repair of formamidopyrimidines 2,6-diamino-4-hydroxy-5-formamidopy

6 factual increases in 2,6-diamino-4-hydroxy-5-formamidopyrimidine, 4,6-diamino-5-formamidopyrimidine,

7 ihydro-8-oxoguanine; 2,6-diamino-4-hydroxy-5-formamidopyrimidine; 4,6-diamino-5-formamidopyrimidine)

8 These were 4, 6-diamino-5-formamidopyrimidine, 5,6-dihydroxyuracil, and 5, 6-dihyd

9 r mutagenic lesions (2,6-diamino-4-hydroxy-5-formamidopyrimidine, 8-hydroxyadenine, 5-hydroxycytosine

10 Fpg protein (formamidopyrimidine/8-oxoguanine DNA N-glycosylase) is a

11 dary lesions, an apurinic site and an AFB(1)-formamidopyrimidine (AFB(1)-FAPY) adduct.

12 B(1) exo-8,9-epoxide hydrolyzes to form the formamidopyrimidine (AFB-FAPY) adduct, which interconver

13 urination or imidazole-ring opening yielding formamidopyrimidine AFB1 (AFB1-Fapy-dG).

14 ine-derived lesions, 2,6-diamino-4-hydroxy-5-formamidopyrimidine and 4,6-diamino-5-formamidopyrimidin

15 rine-derived lesions 2,6-diamino-4-hydroxy-5-formamidopyrimidine and 4,6-diamino-5-formamidopyrimidin

16 substrates, namely, 2,6-diamino-4-hydroxy-5-formamidopyrimidine and 4,6-diamino-5-formamidopyrimidin

17 iety of DNA base damage that is dominated by formamidopyrimidine and 5-hydroxy-6-hydropyrimidine lesi

18 thro-pentofuranosyl)-2,6-diamino-4-hydroxy-5-formamidopyrimidine) and 8-OxodGuo (8-oxo-7,8-dihydro-2'

19 hydroxy-5-formamidopyrimidine; 4,6-diamino-5-formamidopyrimidine) and strong plant growth inhibition

20 hydroxy-5-formamidopyrimidine, 4,6-diamino-5-formamidopyrimidine, and 8-hydroxyadenine.

21 Formamidopyrimidines are preferred substrates of D. radi

22 The formamidopyrimidines are produced in significant quantit

23 ]pyridine and the base adduct aflatoxin B(1)-formamidopyrimidine by acylation.

24 the following modified bases: 4,6-diamino-5-formamidopyrimidine, cis- and trans-thymine glycols, 5-h

25 Endonuclease III (Nth), formamidopyrimidine DNA glycosylase (Fpg) and endonuclea

26 Cleavage assays with formamidopyrimidine DNA glycosylase (Fpg) coupled to alk

27 amage was quantitated using Escherichia coli formamidopyrimidine DNA glycosylase (Fpg) in a gene-spec

28 approach was based on digestion of DNA with formamidopyrimidine DNA glycosylase (FPG) to convert 8-o

29 Escherichia coli formamidopyrimidine DNA glycosylase (Fpg), MutY DNA glyc

30 Escherichia coli formamidopyrimidine DNA glycosylase (Fpg), which recogni

31 oxoG), is processed by two DNA glycosylases, formamidopyrimidine DNA glycosylase (Fpg), which removes

32 DNA strand by beta,delta-elimination as does formamidopyrimidine DNA glycosylase (Fpg).

33 e regions of T4-Pdg and the Escherichia coli formamidopyrimidine DNA glycosylase (Fpg).

34 ycosylase (hOgg1) or Escherichia coli enzyme formamidopyrimidine DNA glycosylase (Fpg).

35 spair, and repair of the resulting damage by formamidopyrimidine DNA glycosylase (Fpg).

36 urity is assayed using the DNA repair enzyme formamidopyrimidine DNA glycosylase and by ESI-MS.

37 fferent damage products sensitive to E. coli formamidopyrimidine DNA glycosylase and hot piperidine,

38 at oxidized bases with endonuclease III and formamidopyrimidine DNA glycosylase and then using the l

39 Rs using RNase H and two DNA repair enzymes (formamidopyrimidine DNA glycosylase and uracil-DNA glyco

40 Endo VIII do not serve as back up enzymes to formamidopyrimidine DNA glycosylase in the repair of for

41 t Ug was a better substrate for endo III and formamidopyrimidine DNA glycosylase than Tg; for endonuc

42 ndonucleases Nth (endonuclease III) and Fpg (formamidopyrimidine DNA glycosylase).

43 ndo III), endonuclease VIII (endo VIII), and formamidopyrimidine DNA glycosylase.

44 igestion by the enzymes endonuclease III and formamidopyrimidine DNA glycosylase.

45 with the repair enzymes endonuclease III and formamidopyrimidine DNA glycosylase.

46 dative stress and are efficiently excised by formamidopyrimidine DNA glycosylase.

47 displayed subtle biases in damage chemistry (formamidopyrimidine DNA glycosylase/piperidine ratio).

48 tex were demonstrated using Escherichia coli formamidopyrimidine DNA N-glycosylase (Fpg protein)-sens

49 ve oxygen paralleled a four-fold increase in formamidopyrimidine DNA N-glycosylase (FPG)-sensitive cl

50 reduced the efficiency of 8-oxoG cleavage by formamidopyrimidine DNA N-glycosylase and increased the

51 min of reperfusion based on the presence of formamidopyrimidine DNA N-glycosylase-sensitive sites.

52 es have been identified for Escherichia coli formamidopyrimidine-DNA glycosylase (Fpg) and Drosophila

53 alf-life of Schiff bases formed when E. coli formamidopyrimidine-DNA glycosylase (Fpg) and endonuclea

54 Formamidopyrimidine-DNA glycosylase (Fpg) excises 8-oxog

55 is initiated by DNA glycosylases such as the formamidopyrimidine-DNA glycosylase (Fpg) in Escherichia

56 Formamidopyrimidine-DNA glycosylase (Fpg) is a 30.2 kDa

57 Formamidopyrimidine-DNA glycosylase (Fpg) is a primary p

58 Formamidopyrimidine-DNA glycosylase (Fpg) protein plays

59 ed by treatment with either Escherichia coli formamidopyrimidine-DNA glycosylase (Fpg), Escherichia c

60 counterpart, guanine, by the repair enzyme, formamidopyrimidine-DNA glycosylase (Fpg), likely involv

61 and comet analysis revealed introduction of formamidopyrimidine-DNA glycosylase (Fpg)-sensitive oxid

62 a, whereas in most bacteria it is removed by formamidopyrimidine-DNA glycosylase (Fpg).

63 ndonuclease III, but a sequence homologue of formamidopyrimidine-DNA glycosylase (Fpg).

64 sylases of the base excision repair pathway: formamidopyrimidine-DNA glycosylase and 8-oxoguanine DNA

65 ing oxidative DNA damage (sites sensitive to formamidopyrimidine-DNA glycosylase and single-strand br

66 on (lactoglyglutathione lyase gene), repair (formamidopyrimidine-DNA glycosylase gene), osmotic prote

67 ybrids were used as substrates for bacterial formamidopyrimidine-DNA glycosylase, Nth protein (endonu

68 ares structural and functional homology with formamidopyrimidine-DNA glycosylase.

69 MutY and formamidopyrimidine-DNA-glycosylase (Fpg) are base-excis

70 The formamidopyrimidines Fapy.dA and Fapy.dG are produced in

71 The structure of a formamidopyrimidine (FAPY) adduct arising from imidazole

72 zed ring opening to give a highly persistent formamidopyrimidine (FAPY) adduct which exists as a mixt

73 ic (8-OH) lesions to putatively nonmutagenic formamidopyrimidine (Fapy) lesions of adenine (Ade) and

74 oxypurine (8-OH) and putatively nonmutagenic formamidopyrimidine (Fapy) lesions.

75 uanine, resulting in imidazole ring opening [formamidopyrimidine (Fapy)] and is associated with signi

76 Formamidopyrimidine (Fapy*dG) is a major lesion arising

77 4,6-Diamino-5-formamidopyrimidine (Fapy*dG) is an abundant form of oxi

78 osine (8-oxo-dG) and 2,6-diamino-4-hydroxy-5-formamidopyrimidine (Fapy-dG), could be useful in treati

79 ,8-dihydro-2'-deoxyguanosine (8-OxodGuo) and formamidopyrimidine (Fapy.dG), are produced from a commo

80 ormamidopyrimidine (FapyG) and 4,6-diamino-5-formamidopyrimidine (FapyA) are formed abundantly in DNA

81 5-formamidopyrimidine (FapyG), 4,6-diamino-5-formamidopyrimidine (FapyA), and 8-oxo-7,8-dihydroadenin

82 rmamidopyrimidine (FapyG) and 4,6-diamino- 5-formamidopyrimidine (FapyA), but not 8-oxo-7,8-dihydrogu

83 ong preference for excision of 4,6-diamino-5-formamidopyrimidine (FapyAde) and 2,6-diamino-4-hydroxy-

84 amidopyrimidine (FapyGua) and 4, 6-diamino-5-formamidopyrimidine (FapyAde) in cultured cells irradiat

85 formamidopyrimidine (FapyGua), 4,6-diamino-5-formamidopyrimidine (FapyAde), and 8-hydroxyguanine (8-O

86 mamidopyrimidine (FapyGua) and 4,6-diamino-5-formamidopyrimidine (FapyAde), which are substrates for

87 amidopyrimidine (FapyGua) and 4, 6-diamino-5-formamidopyrimidine (FapyAde).

88 other common lesion, 2,6-diamino-4-hydroxy-5-formamidopyrimidine (FapydG), shares the same precursor

89 idinohydantoin (Gh), 2,6-diamino-4-hydroxy-5-formamidopyrimidine (FapyG) and 4,6-diamino- 5-formamido

90 induced DNA lesions 2,6-diamino-4-hydroxy-5-formamidopyrimidine (FapyG) and 4,6-diamino-5-formamidop

91 droguanine (8-oxoG), 2,6-diamino-4-hydroxy-5-formamidopyrimidine (FapyG), 4,6-diamino-5-formamidopyri

92 guanine (8-oxoG) and 2,6-diamino-4-hydroxy-5-formamidopyrimidine (FapyG).

93 yguanine (8-OH-Gua), 2,6-diamino-4-hydroxy-5-formamidopyrimidine (FapyGua) and 4, 6-diamino-5-formami

94 cytosine (5-OH-Cyt), 2,6-diamino-4-hydroxy-5-formamidopyrimidine (FapyGua) and 4, 6-diamino-5-formami

95 formamidopyrimidines 2,6-diamino-4-hydroxy-5-formamidopyrimidine (FapyGua) and 4,6-diamino-5-formamid

96 midine (FapyAde) and 2,6-diamino-4-hydroxy-5-formamidopyrimidine (FapyGua) from DNA with no specifici

97 anine (8-OH-Gua) and 2,6-diamino-4-hydroxy-5-formamidopyrimidine (FapyGua) were efficiently excised f

98 on of purine lesions 2,6-diamino-4-hydroxy-5-formamidopyrimidine (FapyGua), 4,6-diamino-5-formamidopy

99 on by S3 protein was 2,6-diamino-4-hydroxy-5-formamidopyrimidine (FapyGua).

100 Escherichia coli formamidopyrimidine (Fpg) DNA glycosylase and MutY DNA g

101 icity by inactivation of the uracil (Ung) or formamidopyrimidine (Fpg) DNA glycosylases but not by in

102 roxy-5-formamidopyrimidine and 4,6-diamino-5-formamidopyrimidine from gamma-irradiated DNA.

103 glycosylases, which specifically remove the formamidopyrimidines from DNA.

104 s and a purine-derived lesion, 4,6-diamino-5-formamidopyrimidine, from DNA containing multiple modifi

105 In bacteria, 8OG is excised by formamidopyrimidine glycosylase (Fpg) as the initial ste

106 Formamidopyrimidine glycosylase (Fpg) is an important ba

107 We apply the assay to the bifunctional formamidopyrimidine glycosylase (Fpg) repair enzyme (E)

108 ion induces a significantly higher amount of formamidopyrimidine glycosylase-sensitive ODD in MCs tha

109 characterize the binding of Escherichia coli formamidopyrimidine-glycosylase (Fpg), a bifunctional re

110 how elevated 8-OHG, 8-OHA, and 5,6-diamino-5-formamidopyrimidine in both nuclear and mtDNA isolated f

111 thropentofuranosyl)-2,6-diamino-4-hydroxy -5-formamidopyrimidine) is a modified purine lesion produce

112 Under conditions of oxidative stress, the formamidopyrimidine lesions (FapyG and FapyA) are formed

113 Oligodeoxynucleotides containing formamidopyrimidine lesions and C-nucleoside analogues a

114 lability of oligodeoxynucleotides containing formamidopyrimidine lesions indicate that Fapy.dA is rea

115 The formamidopyrimidine lesions reduce the T(M) of dodecamer

116 Formamidopyrimidine lesions were introduced as dinucleot

117 i against possible mutations attributable to formamidopyrimidine lesions.

118 d without the addition of the repair enzymes formamidopyrimidine N-glycosylase (Fpg), endonuclease II

119 Endonuclease (Endo) III and formamidopyrimidine-N-glycosylase (Fpg) are two of the p

120 ring-fragmented lesion, N(5)-NM-substituted formamidopyrimidine (NM-Fapy-dG).

121 hat Endo III and/or Endo VIII play a role in formamidopyrimidine nucleoside repair by examining Fapy*

122 sidered whether the genome is protected from formamidopyrimidine nucleosides (Fapy*dA, Fapy*dG) via a

123 Previous reports suggest that the formamidopyrimidine nucleosides are substrates for endon

124 t to their action on duplexes containing the formamidopyrimidines opposite native deoxyribonucleotide

125 8-oxoguanine (8-oxoG), ring-opened purines (formamidopyrimidines or Fapys), and other oxidized DNA b

126 s suggest that CSB plays a role in repair of formamidopyrimidines, possibly by interacting with and s

127 or substrates compared with those containing formamidopyrimidine-pyrimidine base pairs.

128 yladenine and 7-methylguanine whereas methyl-formamidopyrimidine was excised efficiently.

129 roxy-5-formamidopyrimidine and 4,6-diamino-5-formamidopyrimidine were significantly excised.

130 e lesions 8-hydroxyadenine and 4,6-diamino-5-formamidopyrimidine, were not excised from any of the DN

131 ance of anomer dynamics, a feature unique to formamidopyrimidines, when considering the incorporation

132 duces a variety of DNA lesions including the formamidopyrimidines, which are derived from the purines