ライフサイエンスコーパス: glutathione disulfide

1 otal glutathione and increased percentage of glutathione disulfide.

2 lutathione, and dissociation the presence of glutathione disulfide.

3 d involves a redox buffer of glutathione and glutathione disulfide.

4 l thiols, including oxidizing glutathione to glutathione disulfide.

5 titation of NADP+ following the reduction of glutathione disulfides.

6 etics and equilibrium of GSSH formation from glutathione disulfide and H(2)S.

7 ol oxidant diamide showed elevated levels of glutathione disulfide and increased protein-S-glutathion

8 applied to follow the reaction of H(2)S with glutathione disulfide and to quantify the production of

9 ed by glutathione metabolism (oxidized mixed glutathione disulfide) and histidine-containing dipeptid

10 sine, m-tyrosine, nitrotyrosine, dityrosine, glutathione disulfide, and 8-hydroxydeoxyguanosine) as w

11 DTNB, glutathione disulfide, and cystine were only marginally

12 , cystathionine, cysteine, hydrogen sulfide, glutathione disulfide, and glutathione, differed between

13 omitant formation of glutathione persulfide, glutathione disulfide, and H2S.

14 -3-ol derivatives for "prickly", and sugars, glutathione disulfide, AntD, FOL, and one HA for "unctuo

15 amounts of selenodiglutathione (GSSeSG) and glutathione disulfide are formed from selenite and 4 GSH

16 2 Tyr residues (residues 106 and 114) at the glutathione disulfide-binding site.

17 athione reductase catalyzes the reduction of glutathione disulfide by NADPH.

18 from substrates observed in the presence of glutathione disulfide can be explained by competition fo

19 ly, we also identified endogenous coenzyme A glutathione disulfide (CoA-S-S-G) in tissue for the firs

20 with a glutathione-cysteine adduct, and in a glutathione disulfide complex in order to initiate a res

21 in carbonyl content, reduced glutathione, or glutathione disulfide content, although the total consum

22 luding the endogenous compounds glutathione, glutathione disulfide, cysteine, cystine, homocysteine,

23 A significant decline in GSH-glutathione disulfide, cysteine-cystine, and vitamin E s

24 le acid-independent bile flow by stimulating glutathione disulfide excretion, effects that are indepe

25 ron reduced enzyme (EH(2)) interchanges with glutathione disulfide forming two molecules of glutathio

26 The redox state of the glutathione disulfide-glutathione couple is a well known

27 idney, which was consistent with a decreased glutathione disulfide/glutathione ratio.

28 de phosphate , flavin adenine dinucleotide , glutathione disulfide/glutathione).

29 Plasma glutathione/glutathione disulfide (GSH/GSSG) and cysteine/cystine (C

30 We demonstrate that the glutathione/glutathione disulfide (GSH/GSSG) pair controls the coppe

31 corresponds to the intracellular glutathione/glutathione disulfide (GSH/GSSG) potential at the redox

32 levels of Cys, CySS, glutathione (GSH), and glutathione disulfide (GSSG) and calculated E(h) accordi

33 ociated with an increase of GSH oxidation to glutathione disulfide (GSSG) and decrease of the GSH/GSS

34 taneous quantification of glutathione (GSH), glutathione disulfide (GSSG) and glutathione-S-sulfonate

35 Under traditional conditions, 0.125 mM glutathione disulfide (GSSG) and no glutathione (GSH), t

36 idized half the cells' GSH, producing mainly glutathione disulfide (GSSG) and other low-molecular-wei

37 have been identified as transporters of GSH, glutathione disulfide (GSSG) and/or GSH conjugates (GS-X

38 Reduced glutathione (GSH) and glutathione disulfide (GSSG) are critical modulators of

39 lated TK2 was detected after the addition of glutathione disulfide (GSSG) but not GSH.

40 Both proteins selectively transported glutathione disulfide (GSSG) but not reduced glutathione

41 the enzymatic mechanism of the reduction of glutathione disulfide (GSSG) by the reduced a domain of

42 The glutathione disulfide (GSSG) formed can be recycled to G

43 n shown to catalyze the production of NO and glutathione disulfide (GSSG) from GSNO in aqueous soluti

44 e of the importance of glutathione (GSH) and glutathione disulfide (GSSG) in cellular signal transduc

45 ne reductase (GR) catalyzes the reduction of glutathione disulfide (GSSG) into reduced glutathione (G

46 In healthy cells, glutathione disulfide (GSSG) is rapidly reduced back to

47 Cellular glutathione (GSH) and glutathione disulfide (GSSG) levels were measured by hig

48 Biological disulfides such as glutathione disulfide (GSSG) oxidize MT with concomitant

49 otential whereas a dramatic oxidation in GSH/glutathione disulfide (GSSG) pool occurred in parental r

50 educed glutathione (GSH) or a mixture of GSH/glutathione disulfide (GSSG) potentiated platelet aggreg

51 ficant decrease in reduced glutathione (GSH)/glutathione disulfide (GSSG) ratio.

52 oxidative damage markers, glutathione (GSH)/glutathione disulfide (GSSG) ratios, and activation of s

53 Glutathione disulfide (GSSG) reductase (GR) activity was

54 diamide and reduced glutathione or with only glutathione disulfide (GSSG) results in a modification d

55 This enzyme catalyzes the reduction of glutathione disulfide (GSSG) to reduced glutathione (GSH

56 ATP, Arabidopsis PLANT ELICITOR PEPTIDE, and glutathione disulfide (GSSG) treatments induced rapid sp

57 was developed to detect and quantify GSH and glutathione disulfide (GSSG) using LC-HRMS.

58 In contrast to GSH, glutathione disulfide (GSSG) was a potent stimulator of

59 Glutathione disulfide (GSSG) was not transported in eith

60 Cx50), whereas permeation of divalent anion glutathione disulfide (GSSG) was undetectable.

61 Intracellular glutathione (GSH) and glutathione disulfide (GSSG) were measured by HPLC.

62 ORP, reduced glutathione (GSH), and glutathione disulfide (GSSG) were monitored throughout f

63 ant increase of hepatic and plasma levels of glutathione disulfide (GSSG), an indicator of oxidant st

64 have also examined the effect of CORM-2,3 on glutathione disulfide (GSSG), which is a very important

65 t MAO-generated H2O2 oxidizes glutathione to glutathione disulfide (GSSG), which undergoes thiol-disu

66 eloped for quantification of glutathione and glutathione disulfide (GSSG), which was used for the det

67 orption and orientation of the model peptide glutathione disulfide (GSSG).

68 n to reactive oxygen species, thus producing glutathione disulfide (GSSG).

69 hiols, including oxidation of glutathione to glutathione disulfide (GSSG).

70 uce molecular oxygen, forming superoxide and glutathione disulfide (GSSG).

71 se (NOX4) and early significant increases in glutathione disulfide (GSSG)/glutathione (GSH), a marker

72 ure to Hg also oxidized glutathione (GSH) to glutathione disulfide (GSSG); however, goslings were cap

73 lood glutathione (reduced glutathione [GSH], glutathione disulfide [GSSG], and total glutathione [tGS

74 in the presence of GSH reveals a molecule of glutathione disulfide in the active site.

75 GSH decreases, whereas glutathione disulfide increases, ATP binding.

76 e by glutathione and reoxidation of EH(2) by glutathione disulfide indicate that the mixed disulfide

77 of O2(.-) and H2O2, increases in glutathione/glutathione disulfide (indicative of oxidative stress),

78 Exposure to glutathione disulfide induced cMyBP-C S-glutathiolation,

79 e oxidants hydrogen peroxide, superoxide and glutathione disulfide inhibited the phosphatase activity

80 previously shown that glutathione (GSH) and glutathione disulfide interact with metallothionein (MT)

81 NOV-002 is a novel glutathione disulfide mimetic that when administered in

82 evels of total glutathione (glutathione plus glutathione disulfide), occurring before losses in mitoc

83 or DNA dissociation following treatment with glutathione disulfide or hydrogen peroxide.

84 c transfer from enzymes to thionein, whereas glutathione disulfide oxidizes MT with enhanced release

85 Glutaredoxin 2 is the major glutathione disulfide oxidoreductase in E. coli, but its

86 ed for glutaredoxin 2, a vertebrate-specific glutathione-disulfide oxidoreductase with a critical rol

87 Increased intracellular reduced glutathione/glutathione disulfide ratio and greater nuclear redox fa

88 B26 cells exhibited an increased glutathione/glutathione disulfide ratio in the medium in comparison

89 smutase activity, the reduced glutathione-to-glutathione disulfide ratio, and lipid peroxidation indi

90 d glutathione to maintain a high glutathione/glutathione disulfide ratio.

91 cipitated by changing either the glutathione/glutathione-disulfide ratio (GSH/GSSG) and/or the reduce

92 Glutathione/glutathione disulfide ratios were decreased by adenoviru

93 ng, perturbed NAD-to-NADH and glutathione-to-glutathione disulfide ratios, increased NOX4 expression,

94 ecrease in intracellular reduced glutathione:glutathione disulfide ratios, protecting cells from prot

95 le, the inhibitory potency of the kinase was glutathione disulfide S-dioxide (GS-DSDO) (IC50, approxi

96 utathione disulfide S-monoxide (GS-DSMO) and glutathione disulfide S-dioxide (GS-DSDO), we showed tha

97 id, glutathione disulfide S-oxide (GS(O)SG), glutathione disulfide S-dioxide, and GSSG as the major d

98 CPS-DSDO) (IC50, approximately 450 microM) > glutathione disulfide S-monoxide (GS-DSMO) and captopril

99 otential mediators of oxidants in the brain, glutathione disulfide S-monoxide (GS-DSMO) and glutathio

100 We identified glutathione sulfonic acid, glutathione disulfide S-oxide (GS(O)SG), glutathione dis

101 dation of CaMKII, probably via the action of glutathione disulfide S-oxides or their analogues, may b

102 g) altered in tissue and serum, and cysteine-glutathione disulfide showed the highest change (232.4-f

103 f glutathione, nitrosylated glutathione, and glutathione disulfide solubilized in 2 M HCl.

104 ione, and it is involved in the formation of glutathione disulfide, the oxidized form of glutathione.

105 e reductase (Gsr) catalyzes the reduction of glutathione disulfide to glutathione, which plays an imp

106 e reductase (Gsr) catalyzes the reduction of glutathione disulfide to glutathione, which plays an imp

107 rogenase activity also have higher levels of glutathione disulfide under aerobic conditions, so it is

108 TR/GR-null livers cannot reduce oxidized glutathione disulfide using NADPH but still require cont

109 nsensive pathway is subject to inhibition by glutathione disulfide, vanadate, verapamil, and vinblast

110 .0001), which were almost entirely caused by glutathione disulfide, whereas the excretion of reduced

111 The pheromone nereithione (cysteine-glutathione disulfide), which is released by swimming fe

112 ne (GSH) was accompanied by the formation of glutathione disulfide, which could not be ascribed to th

113 SO significantly increased the percentage of glutathione disulfide, which was also inhibited by NAC.

114 The reaction of glutathione disulfide with EH(2) is stoichiometric in th

115 Oxidation of GSH to glutathione disulfide with H2O2 and glutathione peroxida

116 e catalyzes the NADPH-dependent reduction of glutathione disulfide, yielding two molecules of glutath