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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 ol oxidant diamide showed elevated levels of glutathione disulfide and increased protein-S-glutathion
7 sine, m-tyrosine, nitrotyrosine, dityrosine, glutathione disulfide, and 8-hydroxydeoxyguanosine) as w
9 , cystathionine, cysteine, hydrogen sulfide, glutathione disulfide, and glutathione, differed between
11 amounts of selenodiglutathione (GSSeSG) and glutathione disulfide are formed from selenite and 4 GSH
14 from substrates observed in the presence of glutathione disulfide can be explained by competition fo
15 in carbonyl content, reduced glutathione, or glutathione disulfide content, although the total consum
16 luding the endogenous compounds glutathione, glutathione disulfide, cysteine, cystine, homocysteine,
18 le acid-independent bile flow by stimulating glutathione disulfide excretion, effects that are indepe
19 ron reduced enzyme (EH(2)) interchanges with glutathione disulfide forming two molecules of glutathio
25 corresponds to the intracellular glutathione/glutathione disulfide (GSH/GSSG) potential at the redox
26 levels of Cys, CySS, glutathione (GSH), and glutathione disulfide (GSSG) and calculated E(h) accordi
27 ociated with an increase of GSH oxidation to glutathione disulfide (GSSG) and decrease of the GSH/GSS
29 have been identified as transporters of GSH, glutathione disulfide (GSSG) and/or GSH conjugates (GS-X
33 the enzymatic mechanism of the reduction of glutathione disulfide (GSSG) by the reduced a domain of
35 e of the importance of glutathione (GSH) and glutathione disulfide (GSSG) in cellular signal transduc
36 ne reductase (GR) catalyzes the reduction of glutathione disulfide (GSSG) into reduced glutathione (G
40 otential whereas a dramatic oxidation in GSH/glutathione disulfide (GSSG) pool occurred in parental r
41 educed glutathione (GSH) or a mixture of GSH/glutathione disulfide (GSSG) potentiated platelet aggreg
43 oxidative damage markers, glutathione (GSH)/glutathione disulfide (GSSG) ratios, and activation of s
45 diamide and reduced glutathione or with only glutathione disulfide (GSSG) results in a modification d
51 ant increase of hepatic and plasma levels of glutathione disulfide (GSSG), an indicator of oxidant st
52 t MAO-generated H2O2 oxidizes glutathione to glutathione disulfide (GSSG), which undergoes thiol-disu
53 eloped for quantification of glutathione and glutathione disulfide (GSSG), which was used for the det
58 se (NOX4) and early significant increases in glutathione disulfide (GSSG)/glutathione (GSH), a marker
59 lood glutathione (reduced glutathione [GSH], glutathione disulfide [GSSG], and total glutathione [tGS
62 e by glutathione and reoxidation of EH(2) by glutathione disulfide indicate that the mixed disulfide
63 of O2(.-) and H2O2, increases in glutathione/glutathione disulfide (indicative of oxidative stress),
65 e oxidants hydrogen peroxide, superoxide and glutathione disulfide inhibited the phosphatase activity
66 previously shown that glutathione (GSH) and glutathione disulfide interact with metallothionein (MT)
68 evels of total glutathione (glutathione plus glutathione disulfide), occurring before losses in mitoc
69 c transfer from enzymes to thionein, whereas glutathione disulfide oxidizes MT with enhanced release
71 ed for glutaredoxin 2, a vertebrate-specific glutathione-disulfide oxidoreductase with a critical rol
72 Increased intracellular reduced glutathione/glutathione disulfide ratio and greater nuclear redox fa
73 B26 cells exhibited an increased glutathione/glutathione disulfide ratio in the medium in comparison
74 smutase activity, the reduced glutathione-to-glutathione disulfide ratio, and lipid peroxidation indi
76 cipitated by changing either the glutathione/glutathione-disulfide ratio (GSH/GSSG) and/or the reduce
78 ecrease in intracellular reduced glutathione:glutathione disulfide ratios, protecting cells from prot
79 le, the inhibitory potency of the kinase was glutathione disulfide S-dioxide (GS-DSDO) (IC50, approxi
80 utathione disulfide S-monoxide (GS-DSMO) and glutathione disulfide S-dioxide (GS-DSDO), we showed tha
81 id, glutathione disulfide S-oxide (GS(O)SG), glutathione disulfide S-dioxide, and GSSG as the major d
82 CPS-DSDO) (IC50, approximately 450 microM) > glutathione disulfide S-monoxide (GS-DSMO) and captopril
83 otential mediators of oxidants in the brain, glutathione disulfide S-monoxide (GS-DSMO) and glutathio
84 We identified glutathione sulfonic acid, glutathione disulfide S-oxide (GS(O)SG), glutathione dis
85 dation of CaMKII, probably via the action of glutathione disulfide S-oxides or their analogues, may b
86 g) altered in tissue and serum, and cysteine-glutathione disulfide showed the highest change (232.4-f
88 ione, and it is involved in the formation of glutathione disulfide, the oxidized form of glutathione.
89 e reductase (Gsr) catalyzes the reduction of glutathione disulfide to glutathione, which plays an imp
90 rogenase activity also have higher levels of glutathione disulfide under aerobic conditions, so it is
91 TR/GR-null livers cannot reduce oxidized glutathione disulfide using NADPH but still require cont
92 nsensive pathway is subject to inhibition by glutathione disulfide, vanadate, verapamil, and vinblast
93 .0001), which were almost entirely caused by glutathione disulfide, whereas the excretion of reduced
95 ne (GSH) was accompanied by the formation of glutathione disulfide, which could not be ascribed to th
96 SO significantly increased the percentage of glutathione disulfide, which was also inhibited by NAC.
99 e catalyzes the NADPH-dependent reduction of glutathione disulfide, yielding two molecules of glutath
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