ライフサイエンスコーパス: Gua

1 s abolished by the denaturants triton X-100, Gua-HCl, Gua-thiocyanate, SDS and urea in a dose-depende

2 ns (X(2-) = FPO3(2-), HPO3(2-), or SO4(2-)), Gua(+) and GA into a functioning catalyst of the reducti

3 anine derived from BP (6-BP-8-Ade and 6-BP-8-Gua) and DBC (10-DBC-8-Ade and 10-DBC-8-Gua) were synthe

4 BP-8-Gua) and DBC (10-DBC-8-Ade and 10-DBC-8-Gua) were synthesized in good yields by this method.

5 of the SM alpha-actin CArGs (both contain a Gua or Cyt substitution in their A/T-rich center) and th

6 the Gly136-Arg147 peptide cross-linked to a Gua at the N7 position, with the site of reaction being

7 n frequency of the three guanine C8 adducts, Gua-C8-AP, Gua-C8-1,6-ANP, and Gua-C8-1,8-ANP in a CGCG*

8 1-NP adduct, N-(guanin-8-yl)-1-aminopyrene (Gua-C8-AP).

9 1-amino-6 ()-nitropyrene (Gua-C8-1,6-ANP and Gua-C8-1,8-ANP), which contain a nitro group on the pyre

10 e C8 adducts, Gua-C8-AP, Gua-C8-1,6-ANP, and Gua-C8-1,8-ANP in a CGCG*CG sequence.

11 ymerase iota complexed with N2-ethyl-Gua and Gua at the active site suggests movements in the DNA pol

12 NA polymerase iota opposite N2-ethyl-Gua and Gua using Mn2+ is lower relative to that using Mg2+ indi

13 d base pairs, Cyt/Oxa, Thy/Oxa, Ade/Oxa, and Gua/Oxa, with no preference to base pairing.

14 y perturbed by cutting hlGPDH into R269A and Gua(+) pieces.

15 ble for the observed selectivity against any Gua-containing basepair; 3) the Pro and Leu residues can

16 of the three guanine C8 adducts, Gua-C8-AP, Gua-C8-1,6-ANP, and Gua-C8-1,8-ANP in a CGCG*CG sequence

17 s with additional isosteric modifications at Gua and filter binding experiments revealed that the mec

18 transition state by 1.0 M guanidine cation (Gua(+)).

19 s mutant enzyme by added guanidinium cation (Gua(+)): 1 M Gua(+) stabilizes the transition state by c

20 a (8-oxoGua-37-mer) positioned opposite Cyt, Gua, Thy, or Ade.

21 the enzyme pieces, (DeltaGS(double dagger))E+Gua = 2.4 kcal/mol, for Gua(+) activation of the R269A h

22 + HPi) pieces, (DeltaGS(double dagger))HPi+E+Gua = 5.6 kcal/mol, is nearly equal to the sum of the ad

23 Both 1,N(2)-epsilon-Gua and heptanone-1,N(2)-epsilon-Gua were substrates for

24 (2)-epsilon-Gua and heptanone-1,N(2)-epsilon-Gua were substrates for enzymatic oxidation in rat liver

25 ucts [1,N(2)-epsilon-guanine (1,N(2)-epsilon-Gua), N(2),3-epsilon-Gua, heptanone-1,N(2)-epsilon-Gua,

26 N(2),3-epsilon-Gua, heptanone-1,N(2)-epsilon-Gua, 1,N(6)-epsilon-adenine (1,N(6)-epsilon-Ade), and 3,

27 guanine (1,N(2)-epsilon-Gua), N(2),3-epsilon-Gua, heptanone-1,N(2)-epsilon-Gua, 1,N(6)-epsilon-adenin

28 mber of differences between the 1,N2-epsilon-Gua and HO-ethanoGua adducts (which formally differ only

29 shifts were detected with both 1,N2-epsilon-Gua and HO-ethanoGua with some of the polymerases.

30 dGTP and dATP across from both 1,N2-epsilon-Gua and HO-ethanoGua, with the extent varying considerab

31 1,N2-Ethenoguanine (1,N2-epsilon-Gua) and 5,6,7,9-tetrahydro-7-hydroxy-9-oxoimidazo[1,2-a

32 1, N2-Ethenoguanine (1,N2-epsilon-Gua), a product known to be formed from several 2-carbon

33 ated etheno ring derivative of 1, N2-epsilon-Gua, 5,6,7,9-tetrahydro-9-oxoimidazo[1,2-a]purine (ethan

34 ally the hydrated derivative of 1,N2-epsilon-Gua, is a stable DNA product also derived from vinyl hal

35 rder ethanoGua > HO-ethanoGua > 1,N2-epsilon-Gua.

36 lyzed reaction is well suited for N(2)-ethyl-Gua bypass.

37 DNA polymerase iota complexed with N2-ethyl-Gua and Gua at the active site suggests movements in the

38 ion by DNA polymerase iota opposite N2-ethyl-Gua and Gua using Mn2+ is lower relative to that using M

39 ase iota incorporates dCMP opposite N2-ethyl-Gua and unadducted Gua with similar efficiencies in the

40 ructure of DNA polymerase iota with N2-ethyl-Gua at the active site reveals the adducted base in the

41 ncorporation and extension opposite N2-ethyl-Gua by DNA polymerase iota was measured and structures o

42 ructures of the DNA polymerase iota-N2-ethyl-Gua complex with incoming nucleotides were solved.

43 ity of DNA polymerase iota opposite N2-ethyl-Gua was determined by steady state kinetic analysis with

44 NA polymerase iota extends from the N2-ethyl-Gua:Cyt 3' terminus more efficiently than from the Gua:C

45 (1) The first Gua is recognized by K9, removal of which abrogates the

46 nd 22 microM for insertion of dTTP following Gua.C, 8-oxoGua.C, and 8-oxoGua.A base pairs, respective

47 aGS(double dagger))E+Gua = 2.4 kcal/mol, for Gua(+) activation of the R269A hlGPDH-catalyzed reaction

48 monstration that MMR specifically detects FU:Gua (in the first round of DNA replication), signaling a

49 cated that there was more misincorporated FU:Gua in the DNA of MMR-deficient HCT116 cells.

50 mic DNA detected a mis-sense mutation (Ade-->Gua) that substitutes a conserved histidine at amino aci

51 pective bases hypoxanthine (Hx) and guanine (Gua) and the phosphoribosyl donor 5-phosphoribosyl-1-pyr

52 (Fapy) lesions of adenine (Ade) and guanine (Gua) to elucidate radical (.OH)-induced changes in DNA o

53 osine (cyclo-dG), and the free base guanine (Gua).

54 36-mer DNA duplex containing either guanine (Gua).C, 8-oxoGua.C, or 8-oxoGua.A base pairs at the prim

55 ine (8-oxoGua) residue; compared to guanine (Gua).

56 ed by the denaturants triton X-100, Gua-HCl, Gua-thiocyanate, SDS and urea in a dose-dependent manner

57 moethane-induced mutagenicity, one involving Gua N7-alkylation by alkyltransferase-S-CH2CH2Br and dep

58 s more error-prone opposite the cross-linked Gua.

59 me by added guanidinium cation (Gua(+)): 1 M Gua(+) stabilizes the transition state by ca. 3 kcal/mol

60 age for connection of hlGPDH (R269A mutant + Gua(+)) and substrate pieces (GA + HPi) pieces, (DeltaGS

61 )-guanyl)-9-hydroxyaflatoxin B(1) (AFB(1)-N7-Gua), which is converted naturally to two secondary lesi

62 mately 6 times higher than that of AFB(1)-N7-Gua, and (ii) one proposed rotamer of AFB(1)-FAPY is a b

63 oligonucleotide containing a single AFB1-N7-Gua (at the underlined guanine).

64 It is concluded that the AFB1-N7-Gua adduct, and not the apurinic site, has genetic requi

65 zation procedures indicated that the AFB1-N7-Gua genome was approximately 95% pure with a small (5%)

66 he mutational asymmetry observed for AFB1-N7-Gua is consistent with structural models indicating that

67 oli yielded a mutation frequency for AFB1-N7-Gua of 4%.

68 ditions determined to be optimal for AFB1-N7-Gua stability.

69 8-(N7-guanyl)-9-hydroxyaflatoxin B1 (AFB1-N7-Gua) adduct was inserted into the single-stranded genome

70 - (N7-guanyl)-9-hydroxyaflatoxin B1 (AFB1-N7-Gua) adduct, the major DNA adduct of the potent liver ca

71 erty of the primary AFB1-DNA adduct, AFB1-N7-Gua, in mammalian cells has not been studied extensively

72 The G --> T mutations of AFB1-N7-Gua, unlike those (if the AFB1-N7-Gua-derived apurinic s

73 of AFB1-N7-Gua, unlike those (if the AFB1-N7-Gua-derived apurinic site, were much more strongly depen

74 zeta were able to accurately bypass AFB1-N7-Gua.

75 r the conditions of the assay, the 4-OHE2-N7-Gua adduct (Km, 4.6+/-0.7 micromol/L; kcat, 45+/-1.6/h)

76 ydroxyestradiol-quinone to produce 4-OHE2-N7-Gua and 4-OHE2-N3-Ade in a time- and concentration-depen

77 4-OHE(2)-1(alpha,beta)-N7-guanine (4-OHE2-N7-Gua) and 4-OHE(2)-1(alpha,beta)-N3-adenine (4-OHE2-N3-Ad

78 s, N-(guanin-8-yl)-1-amino-6 ()-nitropyrene (Gua-C8-1,6-ANP and Gua-C8-1,8-ANP), which contain a nitr

79 This stabilization is due to the binding of Gua(+) to the binary E(mut) x OMP complex, with a K(d) o

80 th neil1(-/-) and ogg1(-/-) mice, while 8-OH-Gua accumulated in ogg1(-/-) only.

81 nificant change in background levels of 8-OH-Gua and 8-OH-Ade was observed in control human cells, in

82 sure the biologically important lesions 8-OH-Gua and 8-OH-Ade.

83 On the other hand, 8-OH-Gua and FapyGua were not excised from H2O2/Fe(III)-EDTA/

84 olysates should not generate additional 8-OH-Gua because of the absence of guanine, which is not rele

85 ble artifacts during the measurement of 8-OH-Gua by GC/MS.

86 oreover, the Ntg1 protein releases free 8-OH-Gua from 8-OH-Gua/Gua duplex but not from duplexes conta

87 For removal of 8-OH-Gua from DNA, we used either formic acid hydrolysis or s

88 ce artifacts by oxidation of guanine to 8-OH-Gua in acid-hydrolysates of DNA, although the extent of

89 The measurement of 8-OH-Gua in calf thymus DNA by GC/isotope-dilution MS (GC/IDM

90 .6-fold (P < .02), whereas no change in 8-OH-Gua levels was observed in peripheral blood mononuclear

91 ntially cleaves a DNA duplex containing 8-OH-Gua mispaired with a guanine.

92 duplex but not from duplexes containing 8-OH-Gua mispaired with adenine, thymine or cytosine.

93 ein does not incise duplexes containing 8-OH-Gua mispaired with any of the four DNA bases.

94 34mer DNA duplexes containing a single 8-OH-Gua residue mispaired with each of the four DNA bases.

95 erent stable-isotope labeled analogs of 8-OH-Gua used as internal standards for GC/IDMS analysis yiel

96 ties from three DNA substrates, whereas 8-OH-Gua was the least preferred lesion.

97 e results showed that 8-hydroxyguanine (8-OH-Gua) and 2,6-diamino-4-hydroxy-5-formamidopyrimidine (Fa

98 role in the repair of 8-hydroxyguanine (8-OH-Gua) in transcription-coupled and non-strand discriminat

99 8-hydroxyguanine (8-OH-Gua) is one of many lesions generated in DNA by oxidativ

100 midine (FapyAde), and 8-hydroxyguanine (8-OH-Gua) was observed among 17 lesions detected in damaged D

101 or example, mutagenic 8-hydroxyguanine (8-OH-Gua) was reduced approximately 50% (P = 0.02) in mice fe

102 efficient excision of 8-hydroxyguanine (8-OH-Gua), 2,6-diamino-4-hydroxy-5-formamidopyrimidine (FapyG

103 th no specificity for 8-hydroxyguanine (8-OH-Gua).

104 mathematical model log(10)[(8-OH-Ade + 8-OH-Gua)/(FapyAde + FapyGua)].

105 Ogg1 protein, which excises FapyGua and 8-OH-Gua, but not FapyAde.

106 ferences of Fpg protein for excision of 8-OH-Gua, FapyGua and FapyAde from each DNA substrate.

107 e findings suggest that, in addition to 8-OH-Gua, FapyGua and FapyAde may be primary substrates for t

108 e findings suggest that, in addition to 8-OH-Gua, FapyGua may also be a primary substrate of yOgg1 in

109 g that NAC lowered the concentration of 8-OH-Gua, the log ratio, and the variance (previously associa

110 Pyridine reduced the level of 8-OH-Gua, when compared with acetonitrile, indicating its pot

111 ates of D. radiodurans Fpg protein over 8-OH-Gua, whereas E. coli Fpg protein excises these three les

112 ted by the observation that incision of 8-OH-Gua- or 8-OH-Ade-containing oligodeoxynucleotides by who

113 nt hydrolyses yielded similar levels of 8-OH-Gua.

114 leased by acid may be oxidized to yield 8-OH-Gua.

115 NAC reduced the log(10) (8-OH-Gua/FapyGua) ratio from 0.58 +/- 0.15 to essentially zer

116 tg1 protein releases free 8-OH-Gua from 8-OH-Gua/Gua duplex but not from duplexes containing 8-OH-Gua

117 ation in the minor groove at Ade/Thy- and/or Gua/Cyt-rich sequences.

118 ) for the addition of C opposite 8-oxoGua or Gua by KF- and pol II- were all biphasic, with a rapid i

119 ine glycosylase (hOGG1), which excises 8-oxo-Gua to yield single-strand breaks.

120 ine glycosylase (hOGG1), which excises 8-oxo-Gua, strand breaks dependent upon this lesion were measu

121 uilibrium with the open form, N2-(2-oxoethyl)Gua.

122 uced by 1,2-dibromoethane were predominantly Gua to Ade transitions but, in the spectrum of such rifa

123 ic form of the complexes cis-[Pt(NH3)2(Am)(R-Gua)](2+), where R-Gua is 9-methyl- or 9-ethylguanine, i

124 lexes cis-[Pt(NH3)2(Am)(R-Gua)](2+), where R-Gua is 9-methyl- or 9-ethylguanine, is preferred over th

125 at adenine, the molecules designed to target Gua/Cyt sequences also generate lesions at guanine; howe

126 s obtained for DNA adducts other than at the Gua N7 atom and for mutations other than those attributa

127 en from the apurinic site generated from the Gua-N7 adduct.

128 t 3' terminus more efficiently than from the Gua:Cyt base pair.

129 e nitro-containing adducts compared with the Gua-C8-AP adduct itself.

130 incorporation opposite 8-oxoGua compared to Gua.

131 es dCMP opposite N2-ethyl-Gua and unadducted Gua with similar efficiencies in the presence of Mg2+ an

132 et RNA-binding platform, which mimics 5'-Ura-Gua-3' by making Watson-Crick-like hydrogen bonds with 5

133 The order of reaction determined was Gua>Thy>Cyt>Ade.

134 sistant mutations in the RpoB gene, 20% were Gua to Thy transversions.

135 conformational change was rate-limiting when Gua.C was the preceding base pair.

136 substrate, a 275-fold decrease in kcat with Gua, and a 500-fold decrease in kcat for IMP pyrophospho

137 9-fold more reactive ternary E(mut) x OMP x Gua(+) complex.