ライフサイエンスコーパス: glutathione reductase

1 tioxidant defense (thioredoxin reductase and glutathione reductase).

2 drogenase and reoxidation to N(tz) ADP(+) by glutathione reductase.

3 y of both serine acetyltransferase (SAT) and glutathione reductase.

4 id residues that are different from those in glutathione reductase.

5 oth the mitochondrial and cytosolic forms of glutathione reductase.

6 n dipteran insects, where it substitutes for glutathione reductase.

7 reductase, which shares common ancestry with glutathione reductase.

8 e in the presence of reduced glutathione and glutathione reductase.

9 of unmodified and bisnitrated P. falciparum glutathione reductase.

10 etase and glutathione synthetase, as well as glutathione reductase.

11 vin, just as with lipoamide dehydrogenase or glutathione reductase.

12 in titrations of lipoamide dehydrogenase or glutathione reductase.

13 yl] propionic acid (2-AAPA), an inhibitor of glutathione reductase.

14 smutase, catalase, ascorbate peroxidase, and glutathione reductase.

15 M-45 and M-90 were resistant to reduction by glutathione reductase.

16 xins with the small molecule glutathione and glutathione reductase.

17 7, as suggested for the analogous residue in glutathione reductase.

18 ld increased expression of transketolase and glutathione reductase.

19 per-zinc superoxide-dismutase, catalase, and glutathione-reductase.

20 ermine if two of the genes, glyoxalase 1 and glutathione reductase 1, have a causal role in the genes

21 ione synthesis (L-buthionine-sulfoximine) or glutathione reductase (1,3-bis(2-chloroethyl)-1-nitrosou

22 Active site Cys peptides of glutathione reductase 2, NADPH-thioredoxin reductase a/b

23 protein content, whereas the rice plastidial glutathione reductase 3 mutant showed increased sensitiv

24 National survey data of erythrocyte glutathione reductase activation coefficient (EGRac) ind

25 Plasma PLP and erythrocyte glutathione reductase activation coefficient (EGRac), as

26 pe groups (8% to 12% response in erythrocyte glutathione reductase activation coefficient; P<0.01 in

27 Both superoxide dismutase and glutathione reductase activities were increased early (4

28 In addition, thioredoxin reductase and glutathione reductase activities were measured, where th

29 le to show that EGRac (14 studies) and basal glutathione reductase activity (5 studies) were effectiv

30 method is described for the determination of glutathione reductase activity (GR; EC 1.6.4.2) in plant

31 eactive oxygen species levels, and decreased glutathione reductase activity and a corresponding incre

32 Using an erythrocyte FAD-dependent glutathione reductase activity assay, we identified indi

33 ammalian NAD(P)H dehydrogenase and possesses glutathione reductase activity controlling respiratory c

34 Glutathione reductase activity did not increase signific

35 Glutathione reductase activity does not appear to be a r

36 ONOO- decreased glutathione reductase activity in a concentration depend

37 lutathione peroxidase activity and increased glutathione reductase activity in the liver.

38 ave measured the effects of GSH depletion on glutathione reductase activity of the rat brain.

39 Brain glutathione reductase activity was dose-dependently inhi

40 Glutathione reductase activity was found to be inducible

41 d with SSM in both young and old rats, while glutathione reductase activity was not different with ag

42 with buthionine sulfoximine or inhibition of glutathione reductase activity with BCNU inhibited nitri

43 ion, an effect partly mediated via increased glutathione reductase activity.

44 However, there was no change in glutathione reductase activity.

45 y results from cyanate-induced inhibition of glutathione reductase activity.

46 est that GSH is important in the maintenance glutathione reductase activity.

47 nal requirement mediating selection for high glutathione reductase activity.

48 Similarly, glutathione reductase (an H-TrxR homologue lacking Sec)

49 uorescent readout in response to NAD(P)H via glutathione reductase and a subsequent thiol-mediated un

50 activities of catalase hydroperoxidase I and glutathione reductase and an increased sensitivity to ex

51 Targeting genes encoding glutathione reductase and catalase indicated that these

52 he mechanisms of lipoamide dehydrogenase and glutathione reductase and differs fundamentally from the

53 modium falciparum, the crystal structures of glutathione reductase and glutamate dehydrogenase are no

54 amily that includes lipoamide dehydrogenase, glutathione reductase and mercuric reductase, thioredoxi

55 Expression of quinone reductase, glutathione reductase and methionine sulfoxide reductase

56 However, expressions of only glutathione reductase and methionine sulfoxide reductase

57 (GSSG), except in the presence of the enzyme glutathione reductase and NADPH which enabled 1.Tb to be

58 on HPLC, with enzymatic reduction of GSSG by glutathione reductase and NADPH, appear to be valid but

59 Similarly, RNA levels of glutathione reductase and ribonucleotide reductase were

60 e integrity, ascorbate peroxidase, catalase, glutathione reductase and superoxide dismutase activitie

61 ), and activities of glutathione peroxidase, glutathione reductase and superoxide dismutase were meas

62 ynthase, EF hands, haemoglobins, lipocalins, glutathione reductase and the alpha/beta hydrolases.

63 oxidation, and calcium levels along with the glutathione reductase and thioltransferase enzyme activi

64 An Escherichia coli mutant lacking both glutathione reductase and thioredoxin reductase cannot g

65 vitro resulted in the decreased activity of glutathione reductase and thioredoxin reductase, but not

66 one, NOV-002 was an equivalent substrate for glutathione reductase and was an inhibitor of protein di

67 ent dehydrogenase, thioredoxin reductase and glutathione reductase) and their effects on the rheologi

68 , Se-NPs regulated activities of peroxidase, glutathione reductase, and ascorbate, glutathione conten

69 of glucose-6-phosphate dehydrogenase (G6PD), glutathione reductase, and glutathione peroxidase.

70 downstream antioxidant targets thioredoxin, glutathione reductase, and superoxide dismutase 2.

71 ysteine ligase modulatory subunit, catalase, glutathione reductase, and superoxide dismutase were low

72 shed from the collective activities of ArsB, glutathione reductase, and the global regulator Crc.

73 Leishmania and other trypanosomatids lack glutathione reductase, and therefore rely on the novel t

74 nd structures of lipoamide dehydrogenase and glutathione reductase are alike irrespective of the sour

75 oxin reductase, lipoamide dehydrogenase, and glutathione reductase are members of the pyridine nucleo

76 Cells lacking both thioredoxins and glutathione reductase are not viable under aerobic condi

77 closely similar to the FAD-binding domain of glutathione reductase but with NAD+ replacing FAD.

78 sitioned for electron transfer to the FAD in glutathione reductase, but in TrR, these two components

79 Reduction of yeast glutathione reductase by glutathione and reoxidation of

80 Transgenic animals stably overexpressed glutathione reductase by up to 100% throughout adult lif

81 Pteropods showed higher activities of glutathione reductase, catalase, and lipid peroxidation,

82 cluding glutathione, glutathione peroxidase, glutathione reductase, catalase, and superoxide dismutas

83 nolic content, ascorbic acid and the enzymes glutathione reductase, catalase, ascorbate peroxidase an

84 The flavoenzyme glutathione reductase catalyzes the NADPH-dependent redu

85 Glutathione reductase catalyzes the reduction of glutath

86 reductase activity in vitro by the method of glutathione reductase-coupled spectrophotometric assay.

87 Thioredoxin reductase and glutathione reductase create new inter disulfide bonds.

88 of this family, lipoamide dehydrogenase and glutathione reductase, cycle between the two electron-re

89 uctase (DSOR) family of enzymes that include glutathione reductase, dihydrolipoamide dehydrogenase, t

90 vin status was assessed with the erythrocyte glutathione reductase (EC 1.6.4.2) activity coefficient.

91 ion continuously by studying the kinetics of glutathione reductase (EC 1.8.1.7), an enzyme that catal

92 Cr(VI)-induced apoptosis, whereas NADPH and glutathione reductase, enhancers of Cr(VI)-induced ROS g

93 nificantly higher levels of malondialdehyde, glutathione reductase enzyme activity, and calcium level

94 ng plants, improved heavy metal tolerance in glutathione reductase expressing lines, and improved tol

95 nistically, Klotho deficiency suppressed GR (glutathione reductase) expression and activity in the he

96 VioA belongs to the glutathione reductase family 2 of FAD-dependent oxidored

97 Similarity of Pdr to the enzymes of the glutathione reductase family is discussed.

98 zymes, antioxidants (glutathione peroxidase, glutathione reductase, ferritin, and haptaglobin), and b

99 edoxin 5), and unchanged levels of catalase, glutathione reductase, gamma-glutamyl transpeptidase, an

100 ensatory increase in expression of catalase, glutathione reductase, gamma-glutamyl transpeptidase, an

101 ess response genes (e.g., gadB, ctc, and the glutathione reductase gene lmo1433) and virulence genes

102 a P element construct containing the genomic glutathione reductase gene of Drosophila, with 4 kb upst

103 Complementation experiments in yeast lacking glutathione reductase glr1 show that human PYROXD1 has r

104 Yeast mutants that lack glutathione reductase (glr1 delta) accumulate high level

105 ygenase-1, NAD(P)H dehydrogenase, quinone 1, glutathione reductase, glutamate-cysteine ligase catalyt

106 of glutathione-associated enzymes, including glutathione reductases, glutaredoxins, and glutathione S

107 s encoding glutathione biosynthetic enzymes, glutathione reductases, glutaredoxins, thioredoxins, and

108 , ALR islets expressed constitutively higher glutathione reductase, glutathione peroxidase, and highe

109 Glutathione reductase, glutathione peroxidase, and manga

110 not mediated by changes in the activities of glutathione reductase, glutathione peroxidase, catalase,

111 atalase, superoxide dismutase (SOD)-1, SOD3, glutathione reductase, glutathione S-transferase and ald

112 in, and the glutaredoxin system, composed of glutathione reductase, glutathione, and three glutaredox

113 ide dismutase (MnSOD) or an Escherichia coli glutathione reductase (gor) gene.

114 in spite of the homologous nature of E3 and glutathione reductase (goR) in sequence and structure, E

115 nts lacking thioredoxin reductase (trxB) and glutathione reductase (gor) or glutathione biosynthesis

116 abolite repression control protein (Crc), or glutathione reductase (Gor) were more sensitive to As(II

117 xidase (POD), superoxide dismutase (SOD) and glutathione reductase (GR) activities, which led to a ma

118 levation was followed by marked decreases in glutathione reductase (GR) activity in mitochondria, and

119 hione consistent with a 1.6-fold increase in glutathione reductase (GR) activity.

120 ts were correlated with an early increase in glutathione reductase (GR) and GST activities.

121 substrate complexes of the flavoenzyme human glutathione reductase (GR) at nominal resolutions betwee

122 hat the T. muris genome lacks gsr-1 encoding Glutathione Reductase (GR) but has GR activity that can

123 cose-6-phosphate dehydrogenase (G6PDH), and, glutathione reductase (GR) by UV spectrophotometry and d

124 strated herein that the FAD-dependent enzyme glutathione reductase (GR) catalyzes the NADPH-dependent

125 Glutathione reductase (GR) catalyzes the reduction of gl

126 Glutathione reductase (GR) catalyzes the reduction of ox

127 A second glutathione reductase (GR) cDNA has been cloned and sequ

128 phila melanogaster (DmTR) is a member of the glutathione reductase (GR) family of pyridine nucleotide

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

130 y tested as thioredoxin reductase (TrxR) and glutathione reductase (GR) inhibitors, directly against

131 Glutathione reductase (GR) is a critical enzyme in the h

132 laria, we show that the antioxidative enzyme glutathione reductase (GR) is inactivated by peroxynitri

133 Glutathione reductase (GR) is one of important antioxida

134 G also showed increased glutathione reductase (GR) levels vs. C, but reduced the

135 investigates whether the salivary levels of glutathione reductase (GR) may be linked with periodonta

136 Out of two glutathione reductase (GR) proteins in Arabidopsis, GR2

137 rane domains and high sequence similarity to glutathione reductase (GR) was implicated in this proces

138 oxidase (APX), guaiacol peroxidase (GPX) and glutathione reductase (GR) were significantly higher in

139 Furthermore, inhibition of glutathione reductase (GR) with 1,3-bis[2-chloroethyl]-1

140 n in mean D/B ratio of serum (catalase, 2.4; glutathione reductase (GR), 1.33; Thiols, 1.2), liver (c

141 ioxidant enzymes superoxide dismutase (SOD), glutathione reductase (GR), and catalase (CAT) as well a

142 oxidant enzymes ascorbate peroxidase (APOX), glutathione reductase (GR), and superoxide dismutase (SO

143 atalase (CAT), glutathione peroxidase (GPx), glutathione reductase (GR), Glutathione-S-Transferase (G

144 as activities of ascorbate peroxidase (APX), glutathione reductase (GR), monodehydroascorbate reducta

145 power to thioredoxin reductase-1 (TrxR1) and glutathione reductase (GR), thereby supporting fundament

146 seventh decades and analyzed for TTase, TRx, glutathione reductase (GR), thioredoxin reductase (TR),

147 utase (SOD), ascorbate peroxidase (APX), and glutathione reductase (GR), under salt stress.

148 Cu/Zn-superoxide-dismutase (Cu/Zn-SOD), and glutathione reductase (GR), were quantified using qRT-PC

149 ysis of human lens resulted in a 70% loss in glutathione reductase (GR)-specific activity and a 24% l

150 Glutathione reductase (GR; EC 1.6.4.2) activity was assa

151 tive stress, and thus the antioxidant enzyme glutathione reductase (GR; NADPH+GSSG+H(+) <==> NADP(+)+

152 rbituric acid-reactive substances -TBARS and glutathione reductases - GR values by 34.5% and 45.4%, r

153 The enzymes superoxide dismutase (SOD) and glutathione reductase (GRd) were positively associated w

154 in that lacks both thioredoxin reductase and glutathione reductase grows extremely poorly.

155 Glutathione reductases (GRs) are important components of

156 eracts suppression of glutathione peroxidase/glutathione reductase (GSH-Px/GSSG-R) functions, protein

157 atalase, glutathione peroxidase (GSH-Px) and glutathione reductase (GSH-Rd) in the liver.

158 hyde (MDA), DNA fragmentation, caspase-3 and glutathione reductase (GSR) activities, while the level

159 Glutathione reductase (Gsr) catalyzes the reduction of g

160 Glutathione reductase (Gsr) catalyzes the reduction of g

161 ntig was initiated by isolating YACs for the glutathione reductase (GSR) gene and extended in either

162 Mechanistically, AMPKalpha1 regulate the glutathione reductase (GSR) phosphorylation possibly thr

163 al genes that are linked to anxiety, such as glutathione reductase (Gsr), exhibited altered expressio

164 discover a mechanism of zinc regulation over glutathione reductase (GSR), which drives cell death in

165 Thioredoxin reductase-1 (TrxR1)-, glutathione reductase (Gsr)-, and Nrf2 transcription fac

166 ds to i) reduction in glyoxalase (GLO)-1 and glutathione reductase (GSR)-1 expression; ii) calpain me

167 le the protein levels of glyoxalase (GLO)-1, glutathione reductase (GSR)-1, calcium/calmodulin-depend

168 se (GPX), glucose 6-phosphate dehydrogenase, glutathione reductase, GST, catalase (CAT), and superoxi

169 Under normoxic conditions, overexpression of glutathione reductase had no effect on longevity, protei

170 yme), for yeast, Escherichia coli, and human glutathione reductase have been determined between pH 6.

171 H forms of protein tyrosine phosphatases and glutathione reductase have been suggested to play key ro

172 3H-xanthene-9-propionic acid (XAN) and human glutathione reductase (hGR).

173 nhanced enzymatic activities of catalase and glutathione reductase in a dose-dependent manner.

174 ever, to date the activity and regulation of glutathione reductase in conditions such as PD have not

175 hieve this by engineering the life-essential glutathione reductase in Escherichia coli to exclusively

176 The role of thioltransferase and glutathione reductase in the cellular reduction of disul

177 fide (GSSG) formed can be recycled to GSH by glutathione reductase in the presence of NADPH.

178 o test the hypothesis that overexpression of glutathione reductase in transgenic Drosophila melanogas

179 The genetic analysis of thioredoxin and glutathione reductase in yeast runs counter to previous

180 smutase, catalase, ascorbate peroxidase, and glutathione reductase) in both CT and CS genotypes.

181 nly minimal contributions: 25% decrease with glutathione reductase inhibition and no effect by glutat

182 igh sensitivity of mature gametocytes to the glutathione reductase inhibitor and redox cycler drug me

183 r redox homeostasis in D. melanogaster where glutathione reductase is absent.

184 The enzyme glutathione reductase is also important in GSH homeostas

185 Glutathione reductase is the principal enzyme involved i

186 The enzyme, glutathione reductase, is highly specific to glutathione

187 he only enzyme affected by GSH depletion was glutathione reductase; its activity being reduced by app

188 This method of subcellular distribution of glutathione reductase may be conserved in mammalian cell

189 cluding glutathione, glutathione peroxidase, glutathione reductase, metallothionein, and superoxide d

190 superoxide dismutase mimetic CuDIPs and the glutathione reductase mimetic ebselen, TPA-stimulated TN

191 base catalyst, both the EH2 and EH- forms of glutathione reductase must be catalytically active, in c

192 including catalase, glutathione synthetase, glutathione reductase, NADPH-cytochrome P450 reductase,

193 A glutathione reductase null mutant of Saccharomyces cerev

194 ase in catalytic efficiency (k(cat)/K(m)) of glutathione reductase observed at physiologic pH.

195 uced glutathione (GSH) by supplying NADPH to glutathione reductase or thioredoxin reductase.

196 iting either GSH uptake, the NADPH-dependent glutathione reductase, or the NADH/NADPH transhydrogenas

197 the activity of ascorbic acid peroxidase and glutathione reductase over the experimental storage dura

198 rbate reductase, dehydroascorbate reductase, glutathione reductase, peroxidase and glutathione-S-tran

199 is associated with increased levels of alpha-glutathione reductase protein expression.

200 structure with that of two-electron reduced glutathione reductase provides an insight into the sulfe

201 In contrast to H-TrxR and glutathione reductase, recombinant Escherichia coli L-Tr

202 al concentrations of glutathione, NADPH, and glutathione reductase reduced the non-active site disulf

203 al concentrations of glutathione, NADPH, and glutathione reductase reduced Trx1 in vitro and that the

204 Inhibition of glutathione reductase selectively impaired long-term mem

205 oxidation is also not observed, although the glutathione reductase SelH is upregulated, likely to mai

206 roxidase, catalase, ascorbic peroxidase, and glutathione reductase showed a significant increase in t

207 ning (VS) of Schistosoma mansoni thioredoxin glutathione reductase (SmTGR) inhibitors and high conten

208 3-bis(2-chloroethyl)-1-nitrosourea (BCNU) or glutathione reductase-specific siRNA, results in diminis

209 ing to a well defined site that is unique to glutathione reductase suggests that noncompetitive inhib

210 that cells that utilize primarily the GSHPx-glutathione reductase system for degrading H2O2 would be

211 Treatment with the glutathione reductase system led to 80% reduction in PSS

212 ere done before and after reduction with the glutathione reductase system.

213 tivity of the glutathione peroxidase (GSHPx)-glutathione reductase system.

214 Thioredoxin/glutathione reductase (TGR) is a recently discovered mem

215 Thioredoxin/glutathione reductase (TGR) is a third member of this en

216 Thioredoxin glutathione reductase (TGR) is essential for schistosome

217 In addition, thioredoxin/glutathione reductase (TGR) was identified, which is a f

218 ntly identified as inhibitors of thioredoxin glutathione reductase (TGR), a selenocysteine-containing

219 le pocket in Schistosoma mansoni thioredoxin glutathione reductase (TGR), a TrxR-like enzyme, and an

220 vival relies on the redox enzyme thioredoxin glutathione reductase (TGR), a validated target for the

221 wn to inhibit a parasite enzyme, thioredoxin glutathione reductase (TGR), with activities in the low

222 sistent increase in the activity of neuronal glutathione reductase, the enzyme that regenerates reduc

223 parison of the crystal structures of TrR and glutathione reductase, the latter being a well-understoo

224 insects such as Drosophila melanogaster lack glutathione reductase, their TrxRs are particularly impo

225 ipteran insects such as D. melanogaster lack glutathione reductase, thioredoxin reductase (DmTrxR) is

226 ther thiol-disulfide oxidoreductase enzymes, glutathione reductase, thioredoxin, and thioredoxin redu

227 ell as catalase, glutathione peroxidase, and glutathione reductase tissue activity, were determined.

228 GSF acts as an alternative substrate to glutathione reductase to decrease NADPH levels and enhan

229 rapidly reduced back to glutathione (GSH) by glutathione reductase to maintain redox status.

230 itionally investigated the susceptibility of glutathione reductase to ONOO- in vitro, using purified

231 Thioredoxin/glutathione reductase (TXNRD3) is a selenoprotein compos

232 ntrast to the well-characterized DSOR enzyme glutathione reductase, undergoes conformational changes

233 Concomitantly expression of glutathione reductase was reduced leading to an increase

234 Nonprotein sulfhydryl groups and glutathione reductase were not affected by Mn or light t

235 r in a strain lacking both thioredoxin-A and glutathione reductase, which maintains reduced glutaredo

236 Glutathione reductase, which regenerates the reduced for

237 so down-regulated glutathione peroxidase and glutathione reductase, which together constitute a key e

238 be relevant for a mutant of Escherichia coli glutathione reductase with an unusually high value of a