ライフサイエンスコーパス: protein disulfide isomerase

1 eled on the active motifs of thioredoxin and protein disulfide isomerase.

2 d cysteine, which is subsequently reduced by protein disulfide isomerase.

3 R-luminal protein that oxidizes the Trx-like protein disulfide isomerase.

4 iculin and/or calnexin in association with a protein disulfide isomerase.

5 of the ER quality control molecules Bip and protein disulfide isomerase.

6 n, GRP78, calnexin, calreticulin, ERp57, and protein disulfide isomerase.

7 gomerization in the ER lumen is prevented by protein disulfide isomerase.

8 kDa glucose-regulated protein (Grp78/BiP) or protein disulfide isomerase.

9 RP78, GRP75, HSP70, HSP60, HSP54, HSP27, and protein disulfide isomerase.

10 y to increase the effectiveness of DsbG as a protein disulfide isomerase.

11 with the endoplasmic reticulum (ER) marker, protein disulfide isomerase.

12 no activity was observed for BiP, ERp72, and protein disulfide isomerase.

13 oplasmic reticulum oxidoreductases ERp57 and protein disulfide isomerase.

14 heir active sites, including thioredoxin and protein-disulfide isomerase.

15 ular switch of ADAM17 activity operated by a protein-disulfide isomerase.

16 ed folding at pH 7.5 even in the presence of protein-disulfide isomerase.

17 resemble the Escherichia coli DsbC and DsbG protein disulfide isomerases.

18 reticulum oxidoreductin1 oxidoreductase and protein disulfide isomerases.

19 of rearranging disulfide bonds, and giardial protein-disulfide isomerase-2 also displayed oxidant and

20 lly linked to an abnormal redox state of the protein disulfide-isomerase 4.

21 L1 interacted with the endomembrane proteins protein disulfide isomerase 5 (PDI5) and NAI2, with the

22 elping hand from a resident ER enzyme called protein disulfide isomerase, a chaperone that has oxidor

23 Protein disulfide isomerase, a second molecular chaperon

24 ivity of the complex was higher than that of protein-disulfide isomerase, a well characterized chaper

25 chaperone activity is comparable to that of protein-disulfide isomerase, a well characterized chaper

26 In B cells, protein disulfide isomerase A1 (PDIA1/P4HB), the most ab

27 Co-expression of protein disulfide isomerase A2 that regulates disulfide

28 that a secreted tick protein, I. scapularis protein disulfide isomerase A3 (IsPDIA3), enhances B. bu

29 formation and impaired Golgi delivery of the protein disulfide isomerase A3 (PDIA3), an enzyme that c

30 tate dehydrogenase B), redox regulation (eg, protein disulfide isomerase A3), contractile function (e

31 partners, including calnexin, calreticulin, protein disulfide isomerase A3, tapasin, TAP1, and TAP2.

32 rotein response (UPR) proteins calreticulin, protein disulfide-isomerase A3, and glutathione-S-transf

33 Protein disulfide isomerase A6 (PDIA6) interacts with pr

34 ion was in Pdia6, an essential gene encoding protein disulfide isomerase A6 (PDIA6), an oxidoreductas

35 the recombinant LQY1 protein demonstrates a protein disulfide isomerase activity.

36 Escherichia coli mutants exhibiting enhanced protein disulfide isomerase activity.

37 irst demonstration that fibronectin contains protein-disulfide isomerase activity and suggests that c

38 ay, we demonstrate here that fibronectin has protein-disulfide isomerase activity and that this activ

39 Moreover, the protein-disulfide isomerase activity of fibronectin appe

40 act fibronectin, indicating that most of the protein-disulfide isomerase activity of fibronectin is l

41 been shown to form a zinc finger and to have protein-disulfide isomerase activity.

42 eous mixed disulfides with both CaBP1/P5 and protein disulfide isomerase, although these are generall

43 rate that Hrd1 and gp78 interact with CT and protein disulfide isomerase, an ER chaperone that unfold

44 micrographs showed A9 in tubules containing protein disulfide isomerase, an ER lumenal protein, near

45 7 and glutathione S-transferase pi (GSTP), a protein disulfide isomerase and catalyst of S-glutathion

46 lasmic reticulum (ER) and is accomplished by protein disulfide isomerase and ER oxidoreductin 1beta,

47 TLR9 colocalizes with protein disulfide isomerase and is associated with eithe

48 We have identified a novel protein-disulfide isomerase and named it endothelial pro

49 olding catalysts that include members of the protein-disulfide isomerase and peptidyl-prolyl isomeras

50 reticulum (ER) chaperones (GRP78/BiP, GRP94, protein disulfide isomerase) and induction of the stress

51 eticulin, immunoglobulin-binding protein and protein disulfide isomerase, and by increased rates of a

52 ER-resident chaperone proteins such as BiP, protein disulfide isomerase, and heat shock proteins.

53 teins (CGHC) is characteristic of eukaryotic protein-disulfide isomerases, and not other members of t

54 Increased expression of protein disulfide isomerase antagonizes the rescue provi

55 ogram, in part, through de-repression of the protein disulfide isomerase anterior gradient 2 (Agr2).

56 robenzoic acid) (DTNB), bacitracin, and anti-protein disulfide isomerase antibody--inhibited cell-cel

57 addition, we show that multiple isoforms of protein disulfide isomerase are major soluble proteins i

58 osol and the nucleus, and although GRP78 and protein-disulfide isomerase are located largely in the e

59 finding is confirmed by co-localization with protein-disulfide isomerase as determined by double indi

60 ied GRP78 (glucose-regulated protein 78) and protein-disulfide isomerase as putative physiological su

61 Protein-disulfide isomerase-associated 3 (Pdia3) is a mu

62 recombinant MTP and MTPv1 had an equivalent protein disulfide isomerase association, subcellular loc

63 cells up-regulate the ER proteins GRP94 and protein disulfide isomerase at both the transcript and p

64 s an internal salt bridge leading to loss of protein disulfide isomerase binding and lipid transfer a

65 erminal beta-sheet domains are important for protein disulfide isomerase binding and lipid transfer a

66 Glucose-regulated protein 78 and protein disulfide isomerase, both endoplasmic reticulum

67 These data show that sulfhydryl oxidase and protein disulfide isomerase can cooperate in vitro in th

68 lay formed by ER oxidoreductin 1 (Ero1), and protein disulfide-isomerase can be inactivated by a feed

69 , pyruvate kinase (Ch), Annexin II (Ch), and protein disulfide isomerase (Ch).

70 Since prolyl-4-hydroxylase and protein disulfide isomerase coexist as a heterotetramer

71 s been named TR-PDI for "translocon-resident protein disulfide isomerase complex".

72 ing that this single thioredoxin-like domain protein disulfide isomerase could play a critical role i

73 ytic signaling, aPLs promote complement- and protein disulfide isomerase-dependent TF-integrin beta1

74 Sulfhydryl oxidase can also oxidize reduced protein disulfide isomerase directly.

75 In the Escherichia coli periplasm, the protein disulfide isomerase DsbC is maintained in the re

76 The bacterial protein-disulfide isomerase DsbC is a homodimeric V-shap

77 In Escherichia coli, the periplasmic protein disulfide isomerase, DsbC, is maintained reduced

78 ifferent redox potentials, or 20-fold by the protein disulfide isomerase, DsbC.

79 ERcalcistorin/protein-disulfide isomerase (ECaSt/PDI) shows a 55% iden

80 ERcalcistorin/protein-disulfide isomerase (ECaSt/PDI), a high capacity

81 disulfide isomerase and named it endothelial protein-disulfide isomerase (EndoPDI) because of its hig

82 tin-1, protein-disulfide isomerase, probable protein-disulfide isomerase (ER60), beta- or gamma-cytop

83 Several thiol isomerases including protein disulfide isomerase, ERp57, and ERp5 are secrete

84 2 (HMGB1, HMGB2), heat shock protein HSC70, protein disulfide isomerase ERp60, and glyceraldehyde 3-

85 including glucose-regulated protein 78 kDa, protein disulfide isomerase family A, member 6, ER prote

86 he heterodimer, and provided an example of a protein disulfide isomerase family member interacting wi

87 uminal H2O2 as driving force for reoxidizing protein disulfide isomerase family members, thus efficie

88 in cell surface F protein are reduced by the protein disulfide isomerase family of isomerases and tha

89 ERdj5 is a member of the protein disulfide isomerase family of proteins localized

90 encodes one of the five TMX proteins of the protein disulfide isomerase family, hitherto not linked

91 proteins were identified as a member of the protein disulfide isomerase family, thioredoxin reductas

92 Examination of the oxidation status of ER protein-disulfide isomerase family members revealed a sh

93 response involving the chaperones Grp78 and protein disulfide isomerase, followed by degradation via

94 We have characterized three novel protein-disulfide isomerases from the primitive eukaryot

95 eins in lower eukaryotes, we have isolated a protein disulfide isomerase gene from the protozoan para

96 n (Trx) as a substrate, other substrates are protein disulfide isomerase, glutaredoxin, glutathione p

97 variants, and used these to show that while protein disulfide isomerase has little capacity for 2dCD

98 GADD153), endoplasmic reticulum oxidase, and protein disulfide isomerase has revealed a consistent in

99 , keratin 18, keratin 19, ATP synthase beta, protein disulfide isomerase, heat shock protein 27, cath

100 nesis of these lysines to leucines abolished protein disulfide isomerase heterodimerization, lipid tr

101 fide (GSSG) by the reduced a domain of human protein disulfide isomerase (hPDI) with atomistic resolu

102 The human protein disulfide isomerase (hPDI), is an essential four

103 apparatus as opposed to its association with protein disulfide isomerase in CECs.

104 mic vesicles that contained calreticulin and protein-disulfide isomerase in activated RAW 264.7 macro

105 d phosphoprotein, focal adhesion kinase, and protein-disulfide isomerase in proximity to actin filame

106 ance protein ABC transporter (floppase), and protein-disulfide isomerase in proximity to short actin

107 pression patterns for the various Hsp70s and protein disulfide isomerase indicate a likely general co

108 rotein anterior gradient-2 (AGR2), a soluble protein-disulfide isomerase involved in ER protein foldi

109 e, but activity is efficiently restored when protein disulfide isomerase is also present.

110 ticulum (ER) oxidoreductin (Ero1) oxidase to protein disulfide isomerase is an important pathway lead

111 Protein disulfide isomerase is another ER chaperone that

112 cterized as an alpha2beta2 tetramer in which protein disulfide isomerase is the beta subunit with two

113 Protein-disulfide isomerase is essential for formation a

114 Pdi1p (protein-disulfide isomerase) is a folding assistant of t

115 l cloning strategy we identified variants of PROTEIN DISULFIDE ISOMERASE LIKE 5-1 (HvPDIL5-1) as the

116 ene silencing vector in maize indicated that protein disulfide isomerase-like and phosphoglycerate ki

117 rs12446492 in the adjacent gene PDILT (protein disulfide isomerase-like, testis expressed) also

118 MICA levels and a high expression of ERp5, a protein disulfide isomerase linked to MICA shedding (sMI

119 ary and tertiary structures, associated with protein disulfide isomerase, localized to the endoplasmi

120 tor beta, ATP synthase, elongation factor 2, protein disulfide isomerase, nucleophosmin-1, chaperonin

121 four thioredoxin-like domains found in most protein disulfide isomerases, of which two contain an ac

122 lutathione reductase and was an inhibitor of protein disulfide isomerase, one of the components of th

123 by replacing all lumenal proteins with only protein disulfide isomerase or all cytosolic proteins wi

124 Here we show that a gene encoding protein disulfide isomerase P5 (PDI-P5) is expressed at

125 p58(IPK), ERdj4, and HEDJ, as well as EDEM, protein disulfide isomerase-P5, and ribosome-associated

126 a-amylase; copper zinc superoxide dismutase; protein disulfide isomerase, pancreatic; tropomyosin 2 (

127 Different inhibitors of protein disulfide isomerase (PDI) activity were able to

128 yses demonstrated that the ER oxidoreductase protein disulfide isomerase (PDI) acts as a redox-depend

129 Protein disulfide isomerase (PDI) and endoplasmic reticu

130 expression of two disulfide bond isomerases, protein disulfide isomerase (PDI) and ERdj5, in cell-cel

131 n by a poorly understood mechanism requiring protein disulfide isomerase (PDI) and ERO1.

132 n in the endoplasmic reticulum (ER) requires protein disulfide isomerase (PDI) and Ero1p.

133 ) oxidation 1 (ERO1) transfers disulfides to protein disulfide isomerase (PDI) and is essential for o

134 ormation by accepting electrons from reduced protein disulfide isomerase (PDI) and passing them on to

135 olecules concentrate in the RER, and bind to protein disulfide isomerase (PDI) and prolyl 4-hydroxyla

136 over 6 hours in this model was dependent on protein disulfide isomerase (PDI) and TF expression by m

137 aled that GNA colocalizes with the ER marker protein disulfide isomerase (PDI) and the COPI coat prot

138 r results also suggest that the catalysis by protein disulfide isomerase (PDI) and thiol-disulfide ex

139 To investigate the therapeutic potential of protein disulfide isomerase (PDI) as a target to overcom

140 complex comprising an MTPalpha subunit and a protein disulfide isomerase (PDI) beta-subunit.

141 Protein disulfide isomerase (PDI) catalyzes the oxidatio

142 Protein disulfide isomerase (PDI) catalyzes the rearrang

143 This work investigates how QSOX and protein disulfide isomerase (PDI) cooperate in vitro to

144 Protein disulfide isomerase (PDI) derived from intravasc

145 bond of TF is critical for coagulation, and protein disulfide isomerase (PDI) disables coagulation b

146 We found that protein disulfide isomerase (PDI) facilitates CT retrotr

147 gets in the thioredoxin, oxidoreductase, and protein disulfide isomerase (PDI) families, among others

148 Some members of the protein disulfide isomerase (PDI) family appear to facil

149 We show that the protein disulfide isomerase (PDI) family member pancreat

150 is a novel membrane protein belonging to the protein disulfide isomerase (PDI) family, and Eps1 co-lo

151 radient 2 (AGR2), a protein belonging to the protein disulfide isomerase (PDI) family, is overexpress

152 nterior gradient 2 (AGR2) is a member of the protein disulfide isomerase (PDI) family, which plays a

153 ide bond and found them to be members of the protein disulfide isomerase (PDI) family.

154 tal microscopy in mice generated by crossing protein disulfide isomerase (PDI) floxed mice with lysoz

155 Recently, the protein disulfide isomerase (PDI) has been hypothesized

156 procollagen has been well characterized, and protein disulfide isomerase (PDI) has been suggested as

157 Protein disulfide isomerase (PDI) has long been assumed

158 Protein disulfide isomerase (PDI) has two distinct CGHC

159 nd the endoplasmic reticulum redox chaperone protein disulfide isomerase (PDI) in many cell types.

160 We show that protein disulfide isomerase (PDI) in the ER lumen functi

161 In this study, we describe a new class of protein disulfide isomerase (PDI) inhibitors that signif

162 Agr2 is a putative protein disulfide isomerase (PDI) initially identified a

163 Protein disulfide isomerase (PDI) interacts with these e

164 Protein disulfide isomerase (PDI) is a chaperone protein

165 Protein disulfide isomerase (PDI) is a folding assistant

166 Protein disulfide isomerase (PDI) is a multifunctional p

167 Protein disulfide isomerase (PDI) is a multifunctional p

168 Protein disulfide isomerase (PDI) is an essential protei

169 Protein disulfide isomerase (PDI) is an essential protei

170 Protein disulfide isomerase (PDI) is an oxidoreductase e

171 Protein disulfide isomerase (PDI) is an oxidoreductase t

172 Protein disulfide isomerase (PDI) is an oxidoreductase t

173 Protein disulfide isomerase (PDI) is one of the most abu

174 Protein disulfide isomerase (Pdi) is reported to be an i

175 Extracellular protein disulfide isomerase (PDI) is required for platel

176 Protein disulfide isomerase (PDI) is responsible for nas

177 The aim of this study was to explain whether protein disulfide isomerase (PDI) is responsible for the

178 We have previously reported that protein disulfide isomerase (PDI) is S-nitrosylated in b

179 The oxidoreductase protein disulfide isomerase (PDI) is thought to be invol

180 We previously determined that ERp29, a protein disulfide isomerase (PDI) member, extrudes the P

181 Protein disulfide isomerase (PDI) oxidizes, reduces, and

182 ndent on Eps1, a transmembrane member of the protein disulfide isomerase (PDI) oxidoreductase family.

183 f the disulfide bond Cys186-Cys 209 and that protein disulfide isomerase (PDI) regulates TF coagulant

184 r Cys239 of beta-tubulin (TUBB) and Cys53 of protein disulfide isomerase (PDI) respectively.

185 ise, primary quail myotubes transfected with protein disulfide isomerase (PDI) short hairpin RNAs sho

186 the mammalian ER contains >20 members of the protein disulfide isomerase (PDI) superfamily, which ens

187 Protein disulfide isomerase (PDI) utilizes the active si

188 Protein disulfide isomerase (PDI) was demonstrated to be

189 es of this protein, the addition of 4 microM protein disulfide isomerase (PDI) was found to lead to c

190 Protein disulfide isomerase (PDI), a folding catalyst an

191 e analysis revealed the 55-kDa protein to be protein disulfide isomerase (PDI), a member of the estro

192 Recently, protein disulfide isomerase (PDI), a protein that cataly

193 This enzyme cooperates with protein disulfide isomerase (PDI), a redox chaperone pre

194 ease of alpha-granule and lysosome cargo and protein disulfide isomerase (PDI), all of which serve to

195 Protein disulfide isomerase (PDI), an endoplasmic reticu

196 ding involves a regulatory molecule, such as protein disulfide isomerase (PDI), an enzyme that plays

197 fibrillary acidic protein (GFAP), NF-kappaB, protein disulfide isomerase (PDI), and Nissl staining.

198 ins is a novel regulator of the ER chaperone protein disulfide isomerase (PDI), and that through PDI,

199 thiols, an inhibitory monoclonal antibody to protein disulfide isomerase (PDI), and the small-molecul

200 or mercuribenzoates, or using inhibitors of protein disulfide isomerase (PDI), bacitracin or antibod

201 lded in the lumen of the ER by the action of protein disulfide isomerase (PDI), before being retrotra

202 y tandem mass spectrometry to be composed of protein disulfide isomerase (PDI), calcium binding prote

203 60), SKP1, ER luminal binding protein (BiP), protein disulfide isomerase (PDI), calreticulin (CRT), a

204 Thiol isomerases, including protein disulfide isomerase (PDI), catalyze disulfide ox

205 mes known as thiol isomerases, which include protein disulfide isomerase (PDI), endoplasmic reticulum

206 Protein disulfide isomerase (PDI), ERp5, and ERp57, amon

207 sterin, von Willebrand factor, multimerin-1, protein disulfide isomerase (PDI), ERp5, ERp57, and ERp7

208 lysts with redox-isomerase activity, such as protein disulfide isomerase (PDI), facilitate Env conver

209 nsertions in Arabidopsis thaliana PDIL2-1, a protein disulfide isomerase (PDI), have reduced seed set

210 On Th2 cells, galectin-9 binds cell surface protein disulfide isomerase (PDI), increasing retention

211 Protein disulfide isomerase (PDI), secreted by platelets

212 Protein disulfide isomerase (PDI), secreted from platele

213 Protein disulfide isomerase (PDI), the chief endoplasmic

214 ic reticulum (ER) oxido-reductases ERp57 and protein disulfide isomerase (PDI), the lectin chaperones

215 Surprisingly, we find that protein disulfide isomerase (PDI), the major protein oxi

216 his study, purified preparations of platelet protein disulfide isomerase (PDI), vitronectin, alpha-th

217 ong the differentially expressed genes was a protein disulfide isomerase (PDI), which is well known a

218 Protein disulfide isomerase (PDI)-like proteins act as o

219 abeling pattern was found for the ER luminal protein disulfide isomerase (PDI).

220 atic levels of XBP1 and XBP1 targets such as protein disulfide isomerase (PDI).

221 se, the most frequently recognized clone was protein disulfide isomerase (PDI).

222 eased levels of ER proteins calreticulin and protein disulfide isomerase (PDI).

223 s stably expressing small interfering RNA to protein disulfide isomerase (PDI).

224 t oxidative folding of proteins in the ER by protein disulfide isomerase (PDI).

225 ione, Cys, Cys-Cys, and reduced and oxidized protein disulfide isomerase (PDI).

226 role when oxidative folding was catalyzed by protein disulfide isomerase (PDI).

227 essential protein relay involving Ero1p and protein disulfide isomerase (PDI).

228 ivities match those of the in vivo catalyst, protein disulfide isomerase (PDI).

229 rane protein Ero1p to secretory proteins via protein disulfide isomerase (PDI).

230 cular mass 58 and 55 kDa, both identified as protein disulfide isomerase (PDI).

231 178A>G [p.Tyr393Cys]), the gene that encodes protein disulfide isomerase (PDI).

232 8), glucose-regulated protein 94 (GRP94) and protein disulfide isomerase (PDI).

233 ugh excessive posttranslational oxidation of protein disulfide isomerase (PDI).

234 ha subunits, and the beta subunits formed by protein disulfide isomerase (PDI).

235 d induced co-localization of Tom20/Nur77 and Protein Disulfide Isomerase (PDI)/Nur77.

236 from the canonical DsbA oxidase and the DsbC protein disulfide isomerase (PDI)/reductase of Escherich

237 the molecular chaperones BiP; GRP94; CaBP1; protein disulfide isomerase (PDI); ERdj3, a recently ide

238 a novel conserved FAD-dependent enzyme, and protein disulfide isomerase (PDI); Ero1 is oxidized by m

239 Thus, inhibition of protein disulfide isomerases (PDI) required for protein

240 in folding and to correct DSB errors through protein-disulfide isomerase (PDI) activity.

241 bond formation in eukaryotes is dependent on protein-disulfide isomerase (PDI) and its homologs, whic

242 ously reported that monoclonal antibodies to protein-disulfide isomerase (PDI) and other membrane-imp

243 Protein-disulfide isomerase (PDI) and related members of

244 ith the luminal endoplasmic reticulum marker protein-disulfide isomerase (PDI) and that was in a simi

245 Glutaredoxin (Grx) and protein-disulfide isomerase (PDI) are members of the thi

246 The folding assistant and chaperone protein-disulfide isomerase (PDI) catalyzes disulfide fo

247 Protein-disulfide isomerase (PDI) catalyzes the formatio

248 Protein-disulfide isomerase (PDI) catalyzes the formatio

249 Thiol isomerases such as protein-disulfide isomerase (PDI) direct disulfide rearr

250 ation of endoplasmic reticulum (ER)-resident protein-disulfide isomerase (PDI) family members in lumb

251 Protein-disulfide isomerase (PDI) has been proposed to e

252 Protein-disulfide isomerase (PDI) is a catalyst of foldi

253 aSt/PDI) shows a 55% identity with mammalian protein-disulfide isomerase (PDI) is a high capacity low

254 Protein-disulfide isomerase (PDI) is a ubiquitous dithio

255 Protein-disulfide isomerase (PDI) is an essential cataly

256 Protein-disulfide isomerase (PDI) switches tissue factor

257 Recently, protein-disulfide isomerase (PDI) was shown to interact

258 An increase in the levels of protein-disulfide isomerase (PDI), a multifaceted endopl

259 Protein-disulfide isomerase (PDI), an endoplasmic reticu

260 de-rich peptides, we sequenced and expressed protein-disulfide isomerase (PDI), peptidyl-prolyl cis-t

261 cking the activity of the major ER-localized protein disulfide isomerase, PDI.

262 rypsin, rendered nicked toxin susceptible to protein disulfide isomerase- (PDI-) mediated reduction.

263 the complex of the mannosidase Htm1p and the protein disulfide isomerase Pdi1p (Htm1p-Pdi1p) acts as

264 In vitro, protein disulfide isomerase (Pdi1p) introduces disulfide

265 ctively oxidizing the soluble oxidoreductase protein disulfide isomerase (Pdi1p), which in turn can d

266 ined the putative interaction of VWF and the protein disulfide isomerase PDIA1, which has previously

267 the endoplasmic reticulum and is mediated by protein disulfide isomerase (PDIA1).

268 A resident ER protein disulfide isomerase, PDIA6, limits the duration

269 ide isomerase (PDI) family member pancreatic protein disulfide isomerase (PDIp), previously considere

270 Protein disulfide isomerases (PDIs) aid protein folding

271 Protein disulfide isomerases (PDIs) are molecular chaper

272 Protein disulfide isomerases (PDIs) areERfoldases identi

273 e an investigation into the role of cellular protein disulfide isomerases (PDIs) by studying the effe

274 Protein disulfide isomerases (PDIs) catalyze the correct

275 Protein disulfide isomerases (PDIs) play a central role

276 Protein disulfide isomerases (PDIs) support endoplasmic

277 Protein disulfide isomerases play important roles in the

278 xidoreductases such as thioredoxin (Trx) and protein disulfide isomerase, play an essential role in r

279 Protein disulfide isomerase plays a key role in catalyzi

280 DsbG, a protein disulfide isomerase present in the periplasm of

281 cted proteins were identified as galectin-1, protein-disulfide isomerase, probable protein-disulfide

282 cessing and secretion, such as calreticulin, protein disulfide isomerase, proteasome subunits, and is

283 Anterior Gradient 2 (AGR2) is a protein disulfide isomerase that plays important roles i

284 We have compared our results with those of protein disulfide-isomerase, the eukaryotic counterpart

285 Unlike other protein-disulfide isomerases, the giardial enzymes have

286 e synthesis of some ER chaperones, including protein disulfide isomerase, their steady state levels d

287 Here we show that an ER protein disulfide isomerase, thioredoxin domain containi

288 elease from BiP, the toxin is transferred to protein disulfide isomerase; this ER redox chaperone is

289 e dimer to associate with calnexin, BiP, and protein-disulfide isomerase to form large, inactive comp

290 poprotein B (apoB) 17, it was unable to bind protein disulfide isomerase, transfer lipids, and suppor

291 rly strong binding to the two CxxC motifs of protein disulfide isomerase using a mutant RNase in whic

292 d mainly to the epidermis, and expression of protein disulfide isomerase was found primarily in the s

293 a Trx domain with a CxxC sequence typical of protein disulfide isomerase (WCGHC).

294 ecause GC1 interacts with the oxidoreductase protein-disulfide isomerase, we hypothesized that thiore

295 of calnexin and ERp57, whereas BiP/GRP78 and protein disulfide isomerase were only modestly affected.

296 he ER chaperones GRP94/gp96, BiP, ERp72, and protein disulfide isomerase were purified in parallel fr

297 ypertrophy, such as smooth muscle myosin and protein-disulfide isomerase were up-regulated in EH30 bu

298 proteins involved in the quality control is protein disulfide isomerase, which catalyzes the formati

299 This is the first report of protein-disulfide isomerases with a single active site t

300 Four tested fusion proteins, maize PROTEIN DISULFIDE ISOMERASE-Yellow Fluorescent Protein,