ライフサイエンスコーパス: GSSG

1 GSSG adsorbed on native, -NH2-functionalized, and -SO3H-

2 GSSG export by MRP1 leads to a perturbation of endotheli

3 GSSG is likely to bind via the carboxylate groups of one

4 GSSG levels were, however, similar between all study gro

5 GSSG oxidizes copper-coordinating cysteines of Atox1 wit

6 analogues of the analytes ((310)GSH and (616)GSSG), along with N-ethylmaleimide (NEM), and treated wi

7 of glutathione biosynthesis and accumulated GSSG in the mitochondria.

8 ance-associated protein-1 (MRP-1), an active GSSG efflux mechanism, showed 2-fold increased activity

9 phenic acid, glutathione sulphinic acid, and GSSG are rather reaction intermediates.

10 yledons and older leaves yellowed early, and GSSG, the oxidized form of glutathione, accumulated in t

11 Our results portray the role of GSH and GSSG as markers of oxidative stress in live organisms un

12 We used quantitative GSH and GSSG biosensors to monitor glutathione import into the E

13 Fasting plasma GSH and GSSG concentrations were measured to calculate the GSH/G

14 as calculated to be -171 mV based on GSH and GSSG concentrations.

15 These data demonstrate that GSH and GSSG contamination must be accounted for when determinin

16 iciency of photosystem II, decreased GSH and GSSG contents, and the ratio of GSH to GSSG.

17 rat liver samples demonstrated that GSH and GSSG coprecipitated with proteins similar to the range f

18 de was used for the determination of GSH and GSSG in rat urine and plasma samples, intoxicated or not

19 -dependent chemical modifications on GSH and GSSG in the presence of iron(II) and iron(III) complexes

20 by day 56; concomitantly, levels of GSH and GSSG increased in both cytosol and mitochondria.

21 The lowest detection for GSH and GSSG is 0.103 nM in a 96-well plate.

22 ing is shown to occur when the total GSH and GSSG is close to 1 mM, whereas pool sizes below 0.9 mM r

23 For GSH and GSSG measurement, the sample was spiked with isotopicall

24 is based on the masking of GSH in a GSH and GSSG mixture via a 1,4-addition reaction with p-benzoqui

25 -dependent chemical modifications on GSH and GSSG that are caused by dielectric barrier discharge und

26 2.1% to 7.9%, and accuracy values of GSH and GSSG were 96% and 105%, respectively.

27 the detection of total glutathione (GSH and GSSG).

28 t of intracellular concentrations of GSH and GSSG, and the calculation of Eh using the Nernst equatio

29 h for reliable detection of cellular GSH and GSSG.

30 Measurements of Cys, CySS, GSH, and GSSG were used with the Nernst equation to calculate the

31 ited by 45 and 98% the formation of GSNO and GSSG, respectively.

32 formation of GAPDH-SSG, compared to GSNO and GSSG.

33 likely depends on ER glutathione import and GSSG export.

34 hearts showed more normal levels of mRNA and GSSG.

35 ctrocatalytic activity for GSH oxidation and GSSG reduction, enabling the simultaneous detection of b

36 ell as products of oxidative stress (such as GSSG and 4-HNE) generated by these enzymes, induced neut

37 N-Acetyl cysteine attenuated GSSG elevation and diamide-induced apoptosis.

38 uction of glutathionylated substrates avoids GSSG accumulation in an organism lacking GSH reductase.

39 t associations between As exposure and blood GSSG or plasma Cys.

40 The orientation of particle bound GSSG was assessed by the release of glutathione after re

41 ects of the composition of the redox buffer, GSSG and GSH, on folding has not been extensively invest

42 h a 3-fold stimulation of ATPase activity by GSSG.

43 Inhibition of the Na,K-ATPase by GSSG did not occur in the presence of ATP at concentrati

44 ys-264 were specifically glutathionylated by GSSG.

45 e conclude that the inactivation of GmPTP by GSSG is regulated at two levels.

46 as in both cases enhanced by H2O2 but not by GSSG, indicating that the intermediate sulfenylation is

47 The currents were also suppressed by GSSG and the thiol oxidants pyridine disulfides (PDSs),

48 e to inactivate the enzyme when thiolated by GSSG or alkylated with iodoacetamide.

49 We found that GRx catalyzes GSSG formation in the presence of GS-thiyl radical gener

50 althy murine aortic endothelial (MAE) cells, GSSG/GSH was over twice as high in EOMA cells.

51 ial in the plastid stroma, where it counters GSSG accumulation and developmental arrest.

52 ssential role of the DmTrx system in cycling GSSG/GSH and maintaining the intracellular redox homeost

53 Consistent with the location of Cys158, GSSG inhibited the channel only when the channel was ope

54 lutathione (GSH), and glutathione disulfide (GSSG) and calculated E(h) according to the Nernst equati

55 e of GSH oxidation to glutathione disulfide (GSSG) and decrease of the GSH/GSSG ratio.

56 conditions, 0.125 mM glutathione disulfide (GSSG) and no glutathione (GSH), the folding pathway of B

57 GSH, producing mainly glutathione disulfide (GSSG) and other low-molecular-weight disulfides.

58 transporters of GSH, glutathione disulfide (GSSG) and/or GSH conjugates (GS-X).

59 after the addition of glutathione disulfide (GSSG) but not GSH.

60 lectively transported glutathione disulfide (GSSG) but not reduced glutathione in agreement with a 3-

61 m of the reduction of glutathione disulfide (GSSG) by the reduced a domain of human protein disulfide

62 The glutathione disulfide (GSSG) formed can be recycled to GSH by glutathione reduc

63 yzes the reduction of glutathione disulfide (GSSG) into reduced glutathione (GSH).

64 In healthy cells, glutathione disulfide (GSSG) is rapidly reduced back to glutathione (GSH) by gl

65 glutathione (GSH) and glutathione disulfide (GSSG) levels were measured by high-performance liquid ch

66 ) or a mixture of GSH/glutathione disulfide (GSSG) potentiated platelet aggregation.

67 ced glutathione (GSH)/glutathione disulfide (GSSG) ratio.

68 rs, glutathione (GSH)/glutathione disulfide (GSSG) ratios, and activation of stress-response transcri

69 Glutathione disulfide (GSSG) reductase (GR) activity was not altered.

70 yzes the reduction of glutathione disulfide (GSSG) to reduced glutathione (GSH) with the accompanying

71 ELICITOR PEPTIDE, and glutathione disulfide (GSSG) treatments induced rapid spatiotemporally overlapp

72 Glutathione disulfide (GSSG) was not transported in either Cyd(+) or Cyd(-) str

73 ion of divalent anion glutathione disulfide (GSSG) was undetectable.

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

75 on of glutathione and glutathione disulfide (GSSG), which was used for the determination of PSSG in b

76 of the model peptide glutathione disulfide (GSSG).

77 ecies, thus producing glutathione disulfide (GSSG).

78 nificant increases in glutathione disulfide (GSSG)/glutathione (GSH), a marker of oxidative stress, c

79 reduced glutathione (GSH) to its disulfide (GSSG) and promotes the formation of protein-glutathione

80 ed glutathione [GSH], glutathione disulfide [GSSG], and total glutathione [tGSH]) and plasma von Will

81 lutathione (GSH) and glutathione disulphide (GSSG) forms the most important redox buffer in organisms

82 lutathione (GSH) and glutathione disulphide (GSSG) molecules as the most important redox pair in orga

83 assay, glutathione (GSH) levels by the DTNB-GSSG reductase method, apoptosis, reactive oxygen specie

84 ameters indicative of oxidative stress (i.e. GSSG and steady-state levels of oxygen-centered radicals

85 and is not directly influenced by endogenous GSSG reductase activity.

86 idative stress by metabolizing extracellular GSSG, while GGT2 might be important in transporting glut

87 We find GSSG, S-oxidised glutathione species, and S-nitrosogluta

88 +), H(+), and anion dynamics, but except for GSSG, only weakly affected the cytosolic redox state.

89 The Michaelis constants (K(m)) for GSSG and beta-NADPH were found to be 40 +/- 11 and 4.4 +

90 on limits of 100 muM for GSH and 8.3 muM for GSSG, respectively.

91 O2 production on the reduction potential for GSSG/2GSH exists between -150 and -300 mV.

92 A hyperactive MRP-1 system for GSSG efflux acts as a critical survival factor for these

93 ioxidant thiol, its oxidized disulfide form (GSSG), and their redox state (E(h) GSH/GSSG), and 2) cys

94 d glutathione (GSH), over its oxidized form (GSSG), and glutathione reductase (GR) in human serum.

95 uced glutathione (GSH) to its oxidized form (GSSG).

96 n that regenerates the free enzyme and forms GSSG.

97 yme involved in the regeneration of GSH from GSSG.

98 e GSH synthesis and regeneration of GSH from GSSG.

99 ne (GSH) and oxidized disulfide glutathione (GSSG) in cell extracts and isolated mitochondria as a me

100 resence of the oxidized form of glutathione (GSSG), except in the presence of the enzyme glutathione

101 P6), reduced (GSH) and oxidised glutathione (GSSG) contents, antioxidant and reducing capacity and Ma

102 lpha after 4 hours and oxidized glutathione (GSSG) after 8 hours indicated development of oxidative s

103 well as the amount of oxidized glutathione (GSSG) and 4-hydroxynonenal (4-HNE) in airway-lining flui

104 glutathione (GSH) and oxidized glutathione (GSSG) and initiated mitochondrial fusion through the coo

105 Determinations of oxidized glutathione (GSSG) and reduced glutathione (GSH) were performed in mo

106 tracellularly [altered oxidized glutathione (GSSG) and reduced glutathione levels and ratio; increase

107 hibition was seen with oxidized glutathione (GSSG) and thiol-modulating reagents.

108 Glutathione (GSH) and oxidized glutathione (GSSG) control cellular function and efficiency of antica

109 MT-2 with an excess of oxidized glutathione (GSSG) increased metal donation fourfold, whereas reduced

110 of the Na,K-ATPase to oxidized glutathione (GSSG) resulted in an increase in the number of S-glutath

111 lyzes the reduction of oxidized glutathione (GSSG) to GSH in the presence of beta-NADPH (beta-nicotin

112 increased recycling of oxidized glutathione (GSSG) to reduced glutathione (GSH), which is due to the

113 glutathione (GSH) and oxidized glutathione (GSSG) were linear over more than four orders of magnitud

114 glutathione (GSH) and oxidized glutathione (GSSG) were measured by HPLC.

115 s of reduced (GSH) and oxidized glutathione (GSSG), and it enables the calculation of the GSH:GSSG ra

116 , electrolyte leakage, oxidized glutathione (GSSG), and total glutathione (GT), reduced glutathione (

117 levels, via increased oxidized glutathione (GSSG), induce isoform-specific S-glutathionylation of 6-

118 had elevated levels of oxidized glutathione (GSSG), resulting in a dramatic change in the ELF redox s

119 ted by the presence of oxidized glutathione (GSSG).

120 fully reactivated with oxidized glutathione (GSSG).

121 of increased levels of oxidized glutathione (GSSG).

122 ed glutathione (GSH)]/[oxidized glutathione (GSSG)] ratio was significantly decreased, whereas the di

123 the sum of oxidized and reduced glutathione (GSSG and GSH) can be measured with essentially no additi

124 panel, oxidized (GSH) & reduced glutathione (GSSG) were also evaluated for each participant.

125 he ratio of oxidised to reduced glutathione (GSSG/GSH).

126 Oxidized GSH (GSSG) can be recycled to GSH by the GSH reductase or exp

127 subcellular redox state using oxidized GSH (GSSG) reductase localization mutants.

128 SH adducts with cell-permeable oxidized GSH (GSSG-ethyl ester) or 2-acetylamino-3-[4-(2-acetylamino-2

129 lity of the total glutathione content (GSH + GSSG) and GSH in saliva is significantly greater than in

130 oenzymes (ATP, ADP, AMP), antioxidants (GSH, GSSG), and a vast pool of other metabolites using a sing

131 Using HPLC-BDD and -UV, hepatic GSH, GSSG, and GSH/GSSG from mice (r=0.64-0.94) and rats (r=0

132 d in families that have a known role in GSH, GSSG, and/or GS-X transport was employed to help identif

133 Blood glutathione levels (GSH, GSSG, and tGSH) were lower (P < 0.001, P = 0.039, and P

134 in- and between-day precision values of GSH, GSSG, and GSH/GSSG were 2.1% to 7.9%, and accuracy value

135 Concentrations of GSH, GSSG, Cys, and CySS were measured using HPLC.

136 Exposure of complex I to oxidized GSH, GSSG, resulted in specific S-glutathiolation at the 51 k

137 .e., a low reduced/oxidized glutathione (GSH-GSSG) ratio.

138 ADP/NADPH-Glo(TM), ROS-Glo(TM)/H(2)O(2), GSH/GSSG-Glo(TM) and Caspase-Glo(R) 3/7 assays.

139 d hepatic DNA oxidation damage, aberrant GSH/GSSG profiles, and altered activation patterns for AP-1.

140 ater extent in the autism LCLs, although GSH/GSSG and ATP concentrations were similarly decreased in

141 HPLC-BDD and -UV, hepatic GSH, GSSG, and GSH/GSSG from mice (r=0.64-0.94) and rats (r=0.79-0.92) were

142 and p66(shc), coupled with low AGER1 and GSH/GSSG levels, insulin resistance, marked myocardial and r

143 tively by DCF fluorescence intensity and GSH/GSSG ratio, and promoted ERK1/2 phosphorylation (P<0.001

144 Cys/CySS and GSH/GSSG redox states in human plasma undergo diurnal variat

145 E(h) of Cys/CySS and GSH/GSSG was -120 to -20 and -200 to -50 mV, respectively.

146 n-day precision values of GSH, GSSG, and GSH/GSSG were 2.1% to 7.9%, and accuracy values of GSH and G

147 tial and intracellular levels of GSH and GSH/GSSG.

148 dox status was systematically clamped at GSH/GSSG ratios ranging from 300:1 to 20:1.

149 in human breast cancer cells attenuated GSH/GSSG, total GSH, nuclear factor erythroid 2-related fact

150 Reliable detection of cellular GSH/GSSG is challenging due to their ultralow concentration

151 ce a progressive decline in the cellular GSH/GSSG ratio, in parallel with a linear increase in newly

152 The glutathione redox couple, GSH/GSSG, oscillated in parallel with DeltaPsi(m) and the NA

153 ine whether the redox state of GSH, Cys, GSH/GSSG, or Cys/CySS undergoes diurnal variation in healthy

154 ed apoptosis associated with a decreased GSH/GSSG ratio, augmented nuclear factor erythroid-related f

155 Cebpd(-/-) mice show decreased GSH/GSSG ratio, increased S-nitrosoglutathione and 3-nitroty

156 creases the HSP-FRET ratio and decreases GSH/GSSG, indicating an increase in oxidant stress.

157 lasma glutathione/glutathione disulfide (GSH/GSSG) and cysteine/cystine (Cys/CySS) couples are oxidiz

158 t the glutathione/glutathione disulfide (GSH/GSSG) pair controls the copper transport pathway by regu

159 lular glutathione/glutathione disulfide (GSH/GSSG) potential at the redox boundary between cellular d

160 Elevated GSH/GSSG ratio (especially in mitochondria), decreased LPO a

161 ne beta-synthase (CBS) promotes elevated GSH/GSSG.

162 CML levels, via Nrf2 pathway, enhancing GSH/GSSG ratio, heme oxygenase-1 and glyoxalase 1 in liver t

163 llular glutathione/oxidized glutathione (GSH/GSSG) and nicotinamide adenine dinucleotide reduced/oxid

164 atio of reduced to oxidized glutathione (GSH/GSSG) as well as a pro-oxidizing shift in the calculated

165 levels and reduced/oxidized glutathione (GSH/GSSG) ratios.

166 atio of reduced to oxidized glutathione (GSH/GSSG), chlorophyll content, photosynthesis and related g

167 atio of reduced to oxidized glutathione (GSH/GSSG), in a well-controlled study of twins.

168 rements of reduced/oxidized glutathione (GSH/GSSG), to assess cytosolic redox responses in cultured p

169 atio of reduced to oxidized glutathione (GSH/GSSG).

170 1), CySS (r = 0.18, p = 0.049), and E(h) GSH/GSSG (r = 0.34, p < 0.0002) correlated with IMT.

171 E(h) GSH/GSSG predicted IMT in a manner that was both independent

172 ional risk factors and hs-CRP, only E(h) GSH/GSSG remained an independent predictor of IMT.

173 Glutathione redox state (E(h) GSH/GSSG), an in vivo measure of intracellular oxidative str

174 form (GSSG), and their redox state (E(h) GSH/GSSG), and 2) cysteine (Cys), an important extracellular

175 et score was associated with a 7% higher GSH/GSSG ratio (P = 0.03) after adjustment for energy intake

176 ed with a 10% (95% CI: 2.7, 18.0) higher GSH/GSSG ratio in the twin with the higher score than in the

177 ant decrease in intracellular GSH and in GSH/GSSG ratios.

178 in cardiomyocytes and that intermediate GSH/GSSG ratios cause reversible DeltaPsi(m) depolarization,

179 accompanied by an increase in intraislet GSH/GSSG ratio (control, 7.1 +/- 0.1; 10 ng/ml IL-1 beta, 8.

180 long-term caloric restriction, had lower GSH/GSSG ratios and higher protein-mixed disulfides than age

181 s in glutathione metabolism, where lower GSH/GSSG ratios decrease labile Cu(I) availability without a

182 dox couples (NADH/NAD(+), NADPH/NADP(+), GSH/GSSG, Trx(SH)(2)/TrxSS).

183 The ratio of GSH/GSSG has been used as an indicator of oxidative stress.

184 With a ratio of GSH/GSSG of 5/1, similar to that of blood, the addition of G

185 icated elevated levels and a decrease of GSH/GSSG ratio in PER group compared with the CTRL group.

186 Also interesting, no nitrosylation of GSH/GSSG was oberved in the presence of iron complexes, whic

187 ened GSH content as well as the ratio of GSH/GSSG when compared to non-sprayed water stressed plants.

188 ng equilibria like in the NAD(+)/NADH or GSH/GSSG couples), on non-natural molecules such as dyes for

189 glutathione/glutathione-disulfide ratio (GSH/GSSG) and/or the reduced/oxidized thioredoxin ratio.

190 ered glutathione reduced/oxidized ratio (GSH/GSSG) similar to MDs, human myopathies, and neurogenic a

191 ed the cellular glutathione redox ratio (GSH/GSSG).

192 glutathione/oxidative glutathione ratio [GSH/GSSG]), and matrix metalloproteinase-8 (MMP-8) levels; a

193 and reduced/oxidized glutathione ratios (GSH/GSSG) and increased cell sensitivity to oxidative stress

194 Carbon monoxide (CO) reduced GSH/GSSG in three breast cancer cell lines by inhibiting CBS

195 The results indicate that GSH/GSSG redox status governs the sequential opening of mito

196 iently oxidized (>90 mV) relative to the GSH/GSSG (-250 mV) and thioredoxin (Trx1, -280 mV) redox cou

197 The calculated redox states of the GSH/GSSG and Cys/CySS couples varied in association with the

198 0, whereas the respective values for the GSH/GSSG couple occurred at 0330 and 1330.

199 al resulted in a greater decrease in the GSH/GSSG ratio and increase in free radical generation in au

200 vely old mice (17 months), increased the GSH/GSSG ratio and redox potential at 19 months in the same

201 mitant increase in the total GSH and the GSH/GSSG ratio was also observed; the NAD(P)H/NAD(P)+ ratio

202 rrier family 7 member 11), decreased the GSH/GSSG ratio, and increased ROS levels.

203 akfast reduced plasma GSH levels and the GSH/GSSG ratio, increased protein carbonyl levels, and induc

204 act dose and with minimal decline in the GSH/GSSG ratio, whereas MAP kinase activation required a hig

205 increase cellular ROS, and decrease the GSH/GSSG ratio.

206 levated oxidative stress detected by the GSH/GSSG ratio.

207 were the levels of NADPH, NADH, and the GSH/GSSG ratio.

208 ntrations were measured to calculate the GSH/GSSG ratio.

209 one disulfide (GSSG) and decrease of the GSH/GSSG ratio.

210 The results indicated that the GSH/GSSG redox ratio was decreased and percentage oxidized g

211 er was retained; however, decreasing the GSH/GSSG to 50:1 irreversibly depolarized DeltaPsi(m) and in

212 This is in sharp contrast to GSH/GSSG treatment with DBD plasma in the absence of metal i

213 Altering GSH:GSSG ratios in mouse primary neurons in vitro also induc

214 uction of GSSG to GSH to maintain a high GSH:GSSG ratio.

215 alone sufficient to reduce intracellular GSH:GSSG ratio and cause eNOS S-glutathionylation.

216 ant proteins showed that as the ratio of GSH:GSSG decreased significant S-glutathionylation occurred

217 izes the in vitro underestimation of the GSH:GSSG ratio arising from the degradation of GSH and forma

218 ), and it enables the calculation of the GSH:GSSG ratios in human plasma and saliva samples.

219 O] ratio and to be independent of the [GSH]/[GSSG] ratio.

220 xidizing glutathione redox potential, E(hc) (GSSG/2GSH), respectively.

221 hich is reflected by low GSH levels and high GSSG levels and significant glutathionylation of mitocho

222 thiol redox switch), and a +10 mV change in GSSG/2GSH reduction potential.

223 thiol redox switches, and a -25 mV change in GSSG/2GSH reduction potential.

224 he brain regions examined, and elevations in GSSG amount that were most pronounced in the striatum an

225 alpha and GSH with a significant increase in GSSG and in pro-fibrogenic transforming growth factor be

226 25% GSH reduction, and a 5-fold increase in GSSG in 20 min.

227 th decreases in GSH and Cys and increases in GSSG and CySS (i.e., a more oxidized environment).

228 TNF-alpha levels after 4 hours and increased GSSG after 8 hours of reperfusion, AdvBcl-2-treated hear

229 oxygen tensions decreased GSNO and increased GSSG formation.

230 extracellular oxidants but not intracellular GSSG.

231 ative stress shown by elevated mitochondrial GSSG/GSH and protein carbonyls.

232 lds more efficiently in the presence of 5 mM GSSG and 5 mM GSH than it does under traditional conditi

233 However, with 5 mM GSSG and 5 mM GSH the formation of the double mixed disu

234 he use of [(13)C2,(5)N]GSH and [(13)C4,(5)N2]GSSG validated these results and demonstrated that the r

235 dant enzyme glutathione reductase (GR; NADPH+GSSG+H(+) <==> NADP(+)+2 GSH) has become an attractive d

236 GSH but not GSSG also inhibited rhinovirus-induced ICAM-1 promoter a

237 s, compared with in the cytosol, the nuclear GSSG/GSH ratio was 5-fold higher.

238 ibition as well as knockdown trapped nuclear GSSG, causing cell death of EOMA.

239 Addition of GSSG or 4-HNE to Amb a 1 challenge material boosted alle

240 1, similar to that of blood, the addition of GSSG potentiated the stimulatory effect as compared to G

241 The addition of GSSG to platelets generated sulfhydryls in the beta subu

242 d with the addition of low concentrations of GSSG to the GSH.

243 -NDH) decreased in parallel as the dosage of GSSG increased.

244 ve a heavy oxidant burden by rapid efflux of GSSG, which is lethal if trapped within the cell.

245 llatory shear also caused a robust export of GSSG that was prevented by the MRP1 inhibitor MK571 and

246 RP1) and use this as their major exporter of GSSG.

247 from the degradation of GSH and formation of GSSG.

248 The fractions of GSSG were 0.2-2.2% (RBC and blood) and 15-47% (saliva) o

249 Disulfide loading of cells by inhibition of GSSG reductase (bischoloronitrosourea) or thioredoxin re

250 y by cytosolic and mitochondrial isoforms of GSSG reductase.

251 miao accumulates high levels of GSSG and exhibits increased glutathione oxidation.

252 The levels of GSSG correlated positively with SBP, DBP and MBP values

253 e proteins in the presence of high levels of GSSG in conditions of oxidative stress.

254 olated from old donors had a higher ratio of GSSG to GSH.

255 storation of GSH levels through reduction of GSSG and deglutathionylation of mitochondrial proteins.

256 e used to observe the enzymatic reduction of GSSG to GSH in real time.

257 The enzyme catalyzes the reduction of GSSG to GSH to maintain a high GSH:GSSG ratio.

258 tional GSH biosynthesis and the reduction of GSSG.

259 and converts the gamma-glutamyl residues of GSSG to 5-hydroxybutyrolactam.

260 direct incorporation of biotinylated GSH or GSSG into the purified recombinant p53 protein was obser

261 lasting reductions in glutathione oxidation (GSSG/GSH) and remarkably concordant nitrite-induced card

262 emonstrate that HOCl and chloramines oxidize GSSG to two irreversible products in high yield.

263 activity, converting reduced GSH to oxidized GSSG with concomitant scrubbing of ambient dissolved O2

264 electrode toward reduced (GSH) and oxidized (GSSG) forms of glutathione was assessed by CV studies at

265 utathione in its reduced (GSH) and oxidized (GSSG) forms.

266 accurately quantify reduced (GSH), oxidized (GSSG) and total (tGSH) glutathione in biological samples

267 electrochemical quantification of oxidized (GSSG) and reduced glutathione (GSH), biomarkers of oxida

268 ore, the ratio of reduced (GSH) to oxidized (GSSG) glutathione was also increased suggesting a role f

269 ondria with respiratory substrates prevented GSSG formation and, consequently, ATP synthase glutathio

270 one peroxidase/glutathione reductase (GSH-Px/GSSG-R) functions, protein expression of gamma-glutamylc

271 Glutathione oxidized/reduced ratio (GSSG/GSH) was increased in the blood of exposed animals,

272 es in GSH reductase, an enzyme that recycles GSSG back to GSH, both in vitro and in vivo.

273 ion to its normal functions, it also reduces GSSG for antioxidant protection.

274 CAT, POD, SOD and GR activities and reducing GSSG.

275 Since GSSG cannot be reduced in the ER, maintenance of the ER

276 ely, 45 or 90 atomic mass units lighter than GSSG.

277 We here report that GSSG, when added to platelets alone, also potentiates pl

278 A biotin switch assay shows that GSSG-ester-induced HIF-1alpha contains reversibly modifi

279 is associated with an oxidising shift in the GSSG/GSH redox potential and is inhibited by the antioxi

280 In addition, dissociation of the GSSG product is inhibited by TriCHQ.

281 Most of the GSSG was converted to GSH by a flavoprotein-dependent pl

282 he release of glutathione after reducing the GSSG disulfide bond and by zeta potential measurements.

283 effects of NOV-002 can be attributed to the GSSG component of the drug, and modulation of cellular r

284 eophilic attack of the Cys53-thiolate to the GSSG-disulfide followed by the deprotonation of Cys56-th

285 Thus, GSSG adsorption and orientation can be tailored by varyi

286 reby facilitating the conversion of GS(.) to GSSG or transfer of GS(.) to form protein-SSG.

287 ts or for a redox potential (ratio of GSH to GSSG), aggregation was further studied with the addition

288 and correction for auto-oxidation of GSH to GSSG.

289 H and GSSG contents, and the ratio of GSH to GSSG.

290 NDH), the flavin subcomplex of complex I, to GSSG resulted in specific S-glutathiolation on the 51 kD

291 and promotes glutathione (GSH) oxidation to GSSG.

292 Up to 3% GSH was auto-oxidized to GSSG during sample workup; the highest oxidations (>1%)

293 se, consisting of diminished GSH relative to GSSG, decreased potential to reduce protein-SSG mixed di

294 ate, consisting of increased GSH relative to GSSG, increases in type 1 and type 2 thiol redox switche

295 The rat alpha2 isoform was more sensitive to GSSG than the alpha1 isoform.

296 to native and -NH2-modified alumina, whereas GSSG is suggested to bind to -SO3H-modified alumina via

297 The mechanism by which GSSG is exported and the consequence of its export from

298 lyceraldehyde-3-phosphate dehydrogenase with GSSG or S-nitrosoglutathione, but these glutathionyl don

299 diamide or incubating cellular extracts with GSSG oxidized PTEN in a manner similar to that of CSNO.

300 cobalamin by a second molecule of GSH yields GSSG.