ライフサイエンスコーパス: glutaredoxin

1 t two of the five cysteine residues in human glutaredoxin.

2 nzymes such as glutathione S-transferase and glutaredoxin.

3 from immobilized S-glutathionylated actin to glutaredoxin.

4 the reactivation of RNR through reduction of glutaredoxins.

5 isulfide on par with mammalian and bacterial glutaredoxins.

6 es required for synthesis of glutathione and glutaredoxins.

7 cystine reductase activity characteristic of glutaredoxins.

8 member of this new expanding family of large glutaredoxins.

9 lications for protein disulfide reduction by glutaredoxins.

10 utathione reductase, which maintains reduced glutaredoxins.

11 reducing proteins glutaredoxin 3 (Grx3) and glutaredoxin 1 (Grx1) are structurally similar but exhib

12 hione redox couple: Inhibition of endogenous glutaredoxin 1 (Grx1) disrupted roGFP2 responses to O(3)

13 Glutaredoxin 1 (Grx1) is an evolutionally conserved anti

14 Here we report the role of glutaredoxin 1 (Grx1), an antioxidant enzyme, in flow-me

15 Moreover, neutrophils deficient in glutaredoxin 1 (Grx1), an enzyme required for deglutathi

16 Disruption of glutaredoxin 1 (Grx1), an enzyme that catalyzes actin de

17 Glutathionylation was reversed by glutaredoxin 1 (Grx1), and GSH plus Grx1 was able to sup

18 d is deactivated by enzymatic reduction with glutaredoxin 1 (Grx1).

19 green fluorescent protein 2, coupled to the glutaredoxin 1 (Grx1-roGFP2).

20 Strains that lack thioredoxins 1 and 2 and glutaredoxin 1 do not grow because RNR remains in its ox

21 storing the ability of Atox1 to bind copper; glutaredoxin 1 facilitates this reaction when GSH is low

22 eak Na(+)-K(+) pump current when we included glutaredoxin 1 in patch pipette solutions to reverse glu

23 lically stressed monocytes by overexpressing glutaredoxin 1 protected MKP-1 from degradation and norm

24 This reaction was stimulated by glutaredoxin 1 via the so-called monothiol mechanism.

25 G, proline increased the expression of grxA (glutaredoxin 1) and trxC (thioredoxin 2) of the OxyR reg

26 edoxin superfamily, thioredoxins 1 and 2 and glutaredoxin 1, is unable to grow, a phenotype presumed

27 o that its properties are closer to those of glutaredoxin 1.

28 Glutaredoxin-1 (Glrx) is a cytosolic enzyme that regulat

29 reversed by the cytosolic thioltransferase, glutaredoxin-1 (Glrx).

30 in lungs of mice lacking and overexpressing glutaredoxin-1 (Glrx1), and wild-type (WT) mice in respo

31 and the specific deglutathionylation reagent glutaredoxin-1 (Grx1).

32 n of Fas (Fas-SSG), which can be reversed by glutaredoxin-1 (Grx1).

33 catalase, a dominant-negative p47(phox), or glutaredoxin-1 decreased GSS-Ras, Ras activation, p38, a

34 promotes clearance of P. aeruginosa and that glutaredoxin-1 impairs bacterial clearance and increases

35 Glutaredoxin-1 overexpression maintained endogenous SirT

36 n of SERCA, and adenoviral overexpression of glutaredoxin-1 prevented both the HNO-stimulated oxidati

37 PTMs of SirT1 are glutathione (GSH) adducts, glutaredoxin-1 was overexpressed to remove this modifica

38 sons with the structures of Escherichia coli glutaredoxin-1, pig liver glutaredoxin and human thiored

39 ss spectroscopy, five proteins, cathepsin G, glutaredoxin-1, thioredoxin, GP1b, and fibrinogen, showe

40 E. coli has three glutaredoxins: 1, 2, and 3, each with a classical -Cys-P

41 Glutaredoxin 2 (Grx2) from Escherichia coli is distingui

42 Vertebrate-specific glutaredoxin 2 (Grx2) is expressed in at least two isofo

43 Here, we discovered an essential function of glutaredoxin 2 during vascular development.

44 Consequently, overexpression of glutaredoxin 2 in the IMS results in a more reduced Mia4

45 revealed that morpholino-based knockdown of glutaredoxin 2 in zebrafish, a model organism to study v

46 In this report glutaredoxin 2 is shown to be the most effective hydroge

47 Glutaredoxin 2 is the major glutathione disulfide oxidor

48 umed common ancestor of cytosolic GSTs (i.e. glutaredoxin 2).

49 ryogenesis has recently been exemplified for glutaredoxin 2, a vertebrate-specific glutathione-disulf

50 ion of a functional vascular system requires glutaredoxin 2-dependent reversible S-glutathionylation

51 Thereby, glutaredoxin 2-mediated redox regulation controls enzyma

52 catalytic region of sirtuin 1 as target for glutaredoxin 2-specific deglutathionylation.

53 Glutaredoxin-2 (Grx2) modulates the activity of several

54 Here, we demonstrate that glutaredoxin-2 (Grx2), a matrix oxidoreductase, is requi

55 The reducing proteins glutaredoxin 3 (Grx3) and glutaredoxin 1 (Grx1) are stru

56 s dependent on the action of a host protein, glutaredoxin 3 (GrxC).

57 Furthermore, we show that glutaredoxin 3 requires the glutathione biosynthesis pat

58 ion of mutations in the gene for the protein glutaredoxin 3 that suppress the growth defect.

59 ations that lead to RNR overproduction allow glutaredoxin 3 to reduce sufficient RNR for growth of th

60 cell allows more effective interaction with glutaredoxin 3, thus restoring an effective pool of deox

61 tional role of the interaction between human glutaredoxin-3 (GRX3) and its protein partner BOLA2, we

62 [2Fe-2S]-bridged heterodimer formed between glutaredoxin-3 and the BolA-like protein Fe repressor of

63 Glutaredoxin 5 (GLRX5) deficiency has previously been id

64 LIAS), BolA type 3 (BOLA3), and a novel gene glutaredoxin 5 (GLRX5).

65 that Ssq1 also interacts with the monothiol glutaredoxin 5 (Grx5) at a binding site different from t

66 In mitochondria monothiol glutaredoxin 5 (GRX5) is involved in the maturation of a

67 Saccharomyces cerevisiae mitochondrial glutaredoxin 5 (Grx5) is the archetypical member of a ub

68 zebrafish mutants is caused by deficiency of glutaredoxin 5 (grx5), a gene required in yeast for Fe-S

69 de a sideroblastic anemia with deficiency of glutaredoxin 5 and a myopathy associated with a deficien

70 ever, the human diseases, Friedreich ataxia, glutaredoxin 5-deficient sideroblastic anemia, ISCU myop

71 Glutaredoxin 6 (Grx6) of Saccharomyces cerevisiae is an

72 eved with the reduced form of glutathione or glutaredoxin, a protein known to replace thioredoxin in

73 Both lipoic acid and glutaredoxins act in the reverse manner from their norma

74 een the toxin sulfurs and cysteine 22 in the glutaredoxin active site.

75 Purified recombinant Pv5-6 exhibited glutaredoxin activity that was increased 1.6-fold by 10

76 ng (13)C-labeled glucose, and an increase in glutaredoxin activity, which catalyzes the glutathione-d

77 sults reveal a novel neuroprotective role of glutaredoxin against dopaminergic neurodegeneration in m

78 Proteins such as thioredoxin, glutaredoxin, albumin, beta-lactoglobulin, and lactopero

79 ndings thus indicate that carefully balanced glutaredoxin amounts in the IMS ensure efficient oxidati

80 balance between cellular reductants such as glutaredoxin and copper activation pathways in controlli

81 f Escherichia coli glutaredoxin-1, pig liver glutaredoxin and human thioredoxin were made.

82 ese results present a physiological role for glutaredoxin and ROS- induced reversible actin glutathio

83 In Escherichia coli, the glutathione/glutaredoxin and thioredoxin pathways are essential for

84 Using these proteins, we showed that the glutaredoxin and thioredoxin reductase domains of TGR co

85 Reduction of Hsp33 is catalyzed by the glutaredoxin and thioredoxin systems in vivo, and leads

86 redox homeostasis, including the glutathione/glutaredoxin and thioredoxin systems.

87 cross talk existing between the glutathione/glutaredoxin and Trx-dependent pathways.

88 The interaction between glutaredoxins and Aft1 is not modulated by the iron stat

89 In particular, cytosolic monothiol glutaredoxins and BolA-like proteins have been identifie

90 h a high amino acid sequence similarity with glutaredoxins and mycoredoxins but with a thioredoxin-li

91 Glutaredoxins and thioredoxins are highly conserved, sma

92 Glutaredoxins and thioredoxins are ubiquitous small heat

93 ative participation of the thioltransferase (glutaredoxin) and thioredoxin systems in overall cellula

94 S] clusters on Rieske, ferredoxin (Fdx), and glutaredoxin), and cluster oxidation states.

95 including glucanase, glutathione peroxidase, glutaredoxin, and a profilin were found to be widely exp

96 lular thiol oxidoreductases, thioredoxin and glutaredoxin, and found that these enzymes can control t

97 Glutathione S-transferase, thioredoxin, glutaredoxins, and DNA repair enzymes responded most str

98 d enzymes, including glutathione reductases, glutaredoxins, and glutathione S-transferases, indicated

99 we conclude that catalase and peroxiredoxin-glutaredoxin are determinants of bacterial persistence d

100 E10R and L1R viral membrane proteins and the glutaredoxin are in the cytoplasm, in which assembly of

101 stically in fungi and higher eukaryotes, the glutaredoxins are conserved, yet their precise function

102 In yeast cells, cytosolic monothiol glutaredoxins are required for the formation of heme and

103 zing glutathione as a resolving cysteine and glutaredoxin as a redox partner.

104 ction of arsenate to arsenite using GSH with glutaredoxin as electron donors.

105 rSynArsC employed glutathione and glutaredoxin as the source of reducing equivalents, like

106 Activity required GSH and glutaredoxin as the source of reducing equivalents.

107 we demonstrate that an Arabidopsis monothiol glutaredoxin, AtGRXS17 (At4g04950), plays a critical rol

108 ich has a redox potential similar to that of glutaredoxin, becomes essential for cell survival when G

109 se, superoxide dismutases, thioredoxins, and glutaredoxins between normal Prdx6-/- and Prdx6+/+ mice

110 po-form of A4V SOD1 was highly reactive with glutaredoxin but not SOD1 containing both copper and zin

111 isulfides, containing one adducted toxin per glutaredoxin but with elimination of two sulfur atoms fr

112 Escherichia coli is distinguished from other glutaredoxins by its larger size, low overall sequence i

113 We find that glutaredoxins can promote disulfide bond formation in th

114 subclass of the thioredoxin superfamily, the glutaredoxins, can become disulfide bond-formation catal

115 g to Grx1(as) cDNA showed that two different glutaredoxin cDNAs (Grx1(as) and Grx1) were generated fr

116 es within the DsbA family different from the glutaredoxin cluster to which mycoredoxin-1 (Mrx1 or Rv3

117 The glutaredoxin domain is a monothiol glutaredoxin containing a CxxS motif at the active site,

118 e observed that the catalytic enhancement by glutaredoxin could be ascribed fully to the difference b

119 The inactivated glutaredoxin could be reactivated by dithiothreitol only

120 concentration of inducer, and the amount of glutaredoxin could be varied from barely detectable to g

121 tro by the cellular enzyme thioltransferase (glutaredoxin) coupled to GSH and GSSG reductase.

122 ave identified mutations in the gene Grxcr1 (glutaredoxin cysteine-rich 1) in five independent alleli

123 nt in GSH biosynthesis) that is defective in glutaredoxin-dependent redox signaling and ntra/ntrb (de

124 ly complex proteins or deletion of cytosolic glutaredoxins did not reduce expression of Yap5 target g

125 or of thioredoxin 1 in this environment, the glutaredoxins do so independently of DsbB.

126 edoxin reductases, it contains an N-terminal glutaredoxin domain and exhibits a wide spectrum of enzy

127 It has an additional glutaredoxin domain and shows highest expression in test

128 entified, which is a fusion of an N-terminal glutaredoxin domain and the TR module.

129 s of cells but is dependent on the conserved glutaredoxin domain Cys residue.

130 The glutaredoxin domain is a monothiol glutaredoxin containi

131 ged between a BOLA2 molecule and a monothiol glutaredoxin domain of GRX3, and to transfer both [2Fe-2

132 de center within the TR domain to either the glutaredoxin domain or Trx.

133 to 72 forming a classical "thioredoxin-fold" glutaredoxin domain, connected by an 11 residue linker t

134 he thiol/disulfide active site of TGR to the glutaredoxin domain.

135 ch is v3 that carries an atypical N-terminal glutaredoxin domain.

136 evolutionary conserved fusion of the TR and glutaredoxin domains.

137 ox pathway was found for O2L, a nonessential glutaredoxin encoded by vaccinia virus.

138 ed by hktE) and a bifunctional peroxiredoxin-glutaredoxin (encoded by pdgX) in resistance of NTHI to

139 catalase-peroxidase system, but thioredoxin/glutaredoxin enzymes might alleviate oxidative stress.

140 Importantly, treatment of inactive KGDH with glutaredoxin facilitated the GSH-dependent recovery of K

141 interaction between members of the monothiol glutaredoxin family and members of the BolA-like protein

142 ld type highlights the role of mitochondrial glutaredoxin Fe-S-binding in whole plant growth and toxi

143 However, glutaredoxins from both S. cerevisiae and E. coli were a

144 the N-terminal 141 amino acids using a novel glutaredoxin fusion expression system.

145 signaling and that cytokinins could activate glutaredoxin gene expression independent of plant nitrat

146 We determined that nitrate induction of glutaredoxin gene expression was dependent upon cytokini

147 h2 mutation was caused by transposition of a glutaredoxin gene, MALE STERILE CONVERTED ANTHER1 (MSCA1

148 RNA silencing of four of these glutaredoxin genes (AtGRXS3/4/5/8) resulted in plants wi

149 dox state of the cell, particularly a set of glutaredoxin genes.

150 The monothiol glutaredoxin Glrx3 and BolA2 function as a [2Fe-2S] chap

151 substrates are protein disulfide isomerase, glutaredoxin, glutathione peroxidase, NK-lysin/granulysi

152 Thus, thioredoxin was more efficient than glutaredoxin, glutathione, or a 14-kDa thioredoxin-like

153 these clones showed homology to known genes: glutaredoxin, growth associated protein (GAP)-43/neuromo

154 Glutaredoxin (Grx) and protein-disulfide isomerase (PDI)

155 as composed of a basic TR1 module fused to a glutaredoxin (Grx) domain that contained an unusual acti

156 Glutaredoxin (Grx) is a ubiquitous redox molecule that i

157 tion of deoxyribonucleotides are provided by glutaredoxin (Grx) or thioredoxin (Trx).

158 nhibitory RNA (siRNA) directed against GR or glutaredoxin (Grx) potentiated adriamycin-induced macrop

159 mulator fern Pteris vittata L., a cDNA for a glutaredoxin (Grx) Pv5-6 was isolated from a frond expre

160 Redox molecules thioredoxin (Trx) and glutaredoxin (Grx) superfamilies actively maintain intra

161 Glutaredoxin (Grx) was deactivated in a dose-dependent f

162 Epitope-tagged glutaredoxin (GRX) was utilized to determine the role of

163 Human glutaredoxin (GRx), also known as thioltransferase, is a

164 oxidoreductase component of the GSH system, glutaredoxin (Grx), is involved in the reduction of GSH-

165 onylation of IKK-beta Cys-179 is reversed by glutaredoxin (GRX), which restores kinase activity.

166 Glutaredoxin (GRx), which specifically catalyzes reducti

167 Glutaredoxin (Grx)-catalyzed deglutathionylation of prot

168 uction of AR-SSG to AR-SH was facilitated by glutaredoxin (GRX).

169 Glutaredoxin (GRx, thioltransferase) is implicated in ce

170 is catalyzed specifically and efficiently by glutaredoxin (GRx, thioltransferase), a thioldisulfide o

171 ard mixed disulfides between glutathione and glutaredoxin (Grx-S-SG), consistent with the in vivo req

172 The yeast monothiol multidomain glutaredoxins (Grx) 3 and 4 are essential for both trans

173 ns of oxidative stress and are controlled by glutaredoxins (Grx) that, under physiological conditions

174 (1) Several recent reports have demonstrated glutaredoxins (Grx) to form [Fe(2)S(2)] cluster-bridged

175 [2Fe-2S]-containing complexes with monothiol glutaredoxins (Grx), structural details are lacking.

176 Alternatively spliced human glutaredoxin (Grx1(as)) cDNA was isolated from a neutrop

177 il cDNA library, using a (32)P-labeled human glutaredoxin (Grx1) cDNA probe under non-stringent condi

178 frame of the previously reported first human glutaredoxin (Grx1) cDNA, but the 3'-untranslated region

179 Glutaredoxin (Grx1) plays a key role in such regulation

180 contains two gene pairs encoding cytoplasmic glutaredoxins (GRX1, GRX2) and thioredoxins (TRX1, TRX2)

181 the form of [2Fe-2S]-GSH2 from the monothiol glutaredoxin Grx3/4, and the same electron source, in th

182 We presently show that the nuclear monothiol glutaredoxins Grx3 and Grx4 are critical for iron inhibi

183 A homologue Fra2 and the cytosolic monothiol glutaredoxins Grx3 and Grx4 together play a key role in

184 likely dependent on the cytosolic monothiol glutaredoxins Grx3/Grx4 and the Fe-S cluster protein Dre

185 athway that includes the cytosolic monothiol glutaredoxins (Grx3 and Grx4) and the BolA homologue Fra

186 NG1 to suppress disease susceptibility genes glutaredoxins GRX480, GRXS13 and thioredoxin TRX-h5.

187 3 form dimeric complexes with both monothiol glutaredoxin Grx5 and Nfu1.

188 arlier in Fe-S biogenesis with the monothiol glutaredoxin, Grx5, and Bol3 functions late with Nfu1.

189 roteins, accessory factors such as monothiol glutaredoxin, GrxD, and the FeS carrier protein NfuA are

190 Cytosolic monothiol glutaredoxins (GRXs) are required in iron-sulfur (Fe-S)

191 Glutaredoxins (Grxs) are small oxidoreductases that redu

192 Glutaredoxins (Grxs) are small proteins that function as

193 Glutaredoxins (Grxs) are ubiquitous small heat-stable di

194 Glutaredoxins (GRXs) catalyze the reduction of protein d

195 Glutaredoxins (GRXs) modulate redox-dependent signaling

196 idative modification that can be reversed by glutaredoxins (Grxs).

197 ete reactivation was only possible using the glutaredoxin/GSH system (97 +/- 4% and 91 +/- 3% for hBC

198 We concluded that the two glutaredoxin homologs encoded by vaccinia virus have dif

199 ioned in two activities that are typical for glutaredoxins, hydroxyethyl disulfide reduction and elec

200 ed Srx as the reaction intermediate, whereas glutaredoxin I was more favorable for deglutathionylatin

201 Furthermore, relative to glutaredoxin I, Srx exhibited negligible deglutathionyla

202 current study sporidesmin inactivated human glutaredoxin in a time- and concentration-dependent mann

203 scU to apo-Grx5, a general purpose monothiol glutaredoxin in A. vinelandii, was monitored by circular

204 recedented role for the thiol oxidoreductase glutaredoxin in reducing the SOD1 disulfide and destabil

205 These data suggest that redox regulation by glutaredoxin in retinal glial cells is perturbed by hype

206 The C domain can substitute for glutaredoxin in vivo as demonstrated by complementation

207 rved role of cytosolic monothiol multidomain glutaredoxins in cellular iron metabolism pathways, incl

208 ristem size and revealed a novel function of glutaredoxins in meristem growth.

209 Here we demonstrate the presence of glutaredoxins in the IMS and show that limiting amounts

210 ds to Grx3 and Grx4, two cytosolic monothiol glutaredoxins, in an iron-independent fashion.

211 epidithiopiperazine-2,5-diones to inactivate glutaredoxin indicated that at least one phenyl substitu

212 ubstitutions in the active site of the three glutaredoxins indicated that only the N-terminal cystein

213 specific dethiolase enzyme thioltransferase (glutaredoxin), indicating that the inactivated form of t

214 tranferase), because Cd(II), an inhibitor of glutaredoxin, inhibits intracellular actin deglutathiony

215 s of the oxidized probe with glutathione and glutaredoxin into a larger kinetic model of peroxide met

216 Based on this observation we conclude that glutaredoxin is a direct target of v-Jun.

217 Glutaredoxin is characterized as a specific and efficien

218 R) solution structure of fully reduced human glutaredoxin is described.

219 disulfide interchange; either thioredoxin or glutaredoxin is then thought to reduce the cystine that

220 The primary function of Grx2 as a GST-like glutaredoxin is to catalyze reversible glutathionylation

221 art of the conserved CGFS motif in monothiol glutaredoxins is essential for this function.

222 n S-glutathionylation, and thioltransferase (glutaredoxin) is a specific and efficient catalyst of pr

223 Cp9 (a distant relative of bacterial glutaredoxins) is a direct electron acceptor for Cp34, p

224 By using these glutaredoxin knocked-out cells, we have demonstrated tha

225 ion, indicating that the protein possesses a glutaredoxin-like activity.

226 APR) is composed of a reductase domain and a glutaredoxin-like C-terminal domain.

227 lines with the attB site integrated into the glutaredoxin-like cg6 gene.

228 bolism encode a second thioredoxin (TrxC), a glutaredoxin-like protein and enzymes involved in the bi

229 potential thioredoxin reductases, and three glutaredoxin-like proteins.

230 as thioredoxins, thioredoxin reductases, and glutaredoxin-like proteins.

231 a and beta subunits of RNR; NrdH and TrxR, a glutaredoxin-like thioredoxin and a thioredoxin reductas

232 MtMrx1, a glutaredoxin-like, mycothiol-dependent oxidoreductase, d

233 Glutathione-dependent glutaredoxin-mediated deglutathionylation of eNOS has be

234 We hypothesized that changes in glutaredoxin might be important in the development of di

235 With this method, glutaredoxin, monitored by Western blot, was knocked out

236 Monothiol glutaredoxins (mono-Grx) represent a highly evolutionari

237 Vaccinia virus encodes two glutaredoxins, O2L and G4L, both of which exhibit thiolt

238 Specifically, the major cytosolic glutaredoxin of yeast was seen to reduce the intramolecu

239 ionylation of the alpha subunit catalyzed by glutaredoxin or dithiothreitol resulted in restoration o

240 ated more effectively by thioredoxin than by glutaredoxin or glutathione at their physiological conce

241 by PrxV is reduced by thioredoxin but not by glutaredoxin or glutathione.

242 as reductant directly in the active site, or glutaredoxins or thioredoxins reduce a C-terminal cystei

243 t of the system revealed no interaction with glutaredoxins or thioredoxins, indicating that this clas

244 lar thiol oxidoreductases that interact with glutaredoxins or thioredoxins.

245 ion are delivered by a redoxin (thioredoxin, glutaredoxin, or NrdH) via a pair of conserved active si

246 the single-cysteine omega class, which have glutaredoxin oxidoreductase activity rather than GSH-S-t

247 uctase, AhpC*, active in the glutathione and glutaredoxin pathway.

248 the thioredoxin pathway and the glutathione/glutaredoxin pathway.

249 ced state by the thioredoxin and glutathione/glutaredoxin pathways.

250 selen known to modulate both thioredoxin and glutaredoxin pathways.

251 These include catalase (HktE), peroxiredoxin/glutaredoxin (PgdX), and a ferritin-like protein (Dps).

252 Monothiol glutaredoxins play a crucial role in iron-sulfur (Fe/S)

253 olds have diverged from a common thioredoxin/glutaredoxin progenitor but did so by different mechanis

254 tein that contains a region of similarity to glutaredoxin proteins and a cysteine-rich region at its

255 IMS and show that limiting amounts of these glutaredoxins provide a kinetic barrier to prevent the t

256 of the Grx1(as) genomic gene, two additional glutaredoxin pseudogenes were also isolated.

257 owing that a poplar ortholog is reduced by a glutaredoxin rather than NADP-thioredoxin reductase.

258 er of activities that are typical of E. coli glutaredoxin rather than thioredoxin.Both the C domain a

259 d (glutathione S-transferase P) and reverse (glutaredoxin) reactions creates a functional cycle that

260 n Bacteroides fragilis lacks the glutathione/glutaredoxin redox system and possesses an extensive num

261 Thioredoxin and glutaredoxin reduce the oxidized Dio3 at physiological c

262 e functionally replaces glutathione, and the glutaredoxins replace LpdA.

263 Inactivation of glutaredoxin required the reduced (dithiol) form of the

264 ally characterized the role of mitochondrial glutaredoxin S15 (GRXS15) in biogenesis of ISC containin

265 Cells lacking both glutaredoxins show constitutive expression of iron regul

266 " cytokinin-deficient plants and "long-root" glutaredoxin-silenced plants generated hybrids that disp

267 Electrostatic calculations on the human glutaredoxin structure and that of related proteins prov

268 se has been shown to require glutathione and glutaredoxin, suggesting that thiol chemistry might be i

269 In conclusion, the glutaredoxin system and glutathione have a backup role t

270 utants lacking components of the glutathione/glutaredoxin system are unaffected.

271 e redox Western blot data indicated that the glutaredoxin system protected Trx1 in HeLa cells from ox

272 lutathionylation of hBCATc-SSG using the GSH/glutaredoxin system provides evidence that this protein

273 ts strongly suggest that the thioredoxin and glutaredoxin systems are the key regulators for hSOD1 ag

274 uctase (TryR) instead of the thioredoxin and glutaredoxin systems of mammalian hosts.

275 reased the capability of the thioredoxin and glutaredoxin systems to reduce hSOD1 compared with wild-

276 The carboxyl-terminal domain functions as a glutaredoxin that mediates the transfer of electrons fro

277 of intramolecular disulfide bonds of the G4L glutaredoxin, the L1R membrane protein, and the structur

278 Glutaredoxin therefore preferentially targets the immatu

279 und to be structurally homologous to E. coli glutaredoxin, thiol transferases, and glutathione S-tran

280 lutathionylation is most likely catalyzed by glutaredoxin (thioltranferase), because Cd(II), an inhib

281 Glutaredoxin (thioltransferase) is a thiol-disulfide oxi

282 the disulfide oxidoreductase activity of the glutaredoxin/thioredoxin family and the RNA hydrolytic a

283 osphatases using a descriptor built from the glutaredoxin/thioredoxin family, proteins that have no a

284 iol-disulfide oxidoreductase activity of the glutaredoxin/thioredoxin protein family.

285 iosynthetic enzymes, glutathione reductases, glutaredoxins, thioredoxins, and thioredoxin reductases,

286 d disulfide with GSH before being reduced by glutaredoxin to regenerate the active Acr2p reductase.

287 d disulfide with GSH before being reduced by glutaredoxin to regenerate the active ArsC reductase.

288 e active RNR, the cell uses thioredoxins and glutaredoxins to reduce the disulfide bond.

289 of [2Fe-2S] cluster transfer from monothiol glutaredoxins to target proteins is a fundamental, but s

290 Aspartic proteases, BTB/POZ proteins (BTB), Glutaredoxins, Trypsin alpha-amylase inhibitor proteins,

291 n-associated protein, focal adhesion kinase, glutaredoxin, utrophin) may be novel mediators of NFT fo

292 By comparison, glutaredoxin was less reactive toward the disulfide of w

293 Various cysteine-to-serine mutants of glutaredoxin were resistant to inactivation by sporidesm

294 Seven genes encoding class III glutaredoxins were found to be strongly and specifically

295 namely, the L1R and F9L proteins and the G4L glutaredoxin-were completely reduced.

296 iamide-GSH is partially recovered by DTT and glutaredoxin, whereas the disulfide linkage of GSH with

297 ytosolic compartment that involves monothiol glutaredoxins, which bind iron in the form of iron-sulfu

298 al member of a ubiquitous class of monothiol glutaredoxins with a strictly conserved CGFS active-site

299 th the help of thioredoxin reductase and the glutaredoxins with the small molecule glutathione and gl

300 pathways via either the thioredoxins or the glutaredoxins without, evidently, the intermediary of gl