ライフサイエンスコーパス: disulfide isomerase

1 the active motifs of thioredoxin and protein disulfide isomerase.

2 ne, which is subsequently reduced by protein disulfide isomerase.

3 l protein that oxidizes the Trx-like protein disulfide isomerase.

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

5 ER quality control molecules Bip and protein disulfide isomerase.

6 tion in the ER lumen is prevented by protein disulfide isomerase.

7 , calnexin, calreticulin, ERp57, and protein disulfide isomerase.

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

9 P75, HSP70, HSP60, HSP54, HSP27, and protein disulfide isomerase.

10 rease the effectiveness of DsbG as a protein disulfide isomerase.

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

12 tch of ADAM17 activity operated by a protein-disulfide isomerase.

13 ng at pH 7.5 even in the presence of protein-disulfide isomerase.

14 reticulum oxidoreductases ERp57 and protein disulfide isomerase.

15 belongs to a unique family of plasmid-based disulfide isomerases.

16 e the Escherichia coli DsbC and DsbG protein disulfide isomerases.

17 um oxidoreductin1 oxidoreductase and protein disulfide isomerases.

18 erge from the Escherichia coli DsbC and DsbG disulfide isomerases.

19 ed to an abnormal redox state of the protein disulfide-isomerase 4.

20 acted with the endomembrane proteins protein disulfide isomerase 5 (PDI5) and NAI2, with the PDI5 int

21 and from a resident ER enzyme called protein disulfide isomerase, a chaperone that has oxidoreductase

22 Protein disulfide isomerase, a second molecular chaperone of the

23 the complex was higher than that of protein-disulfide isomerase, a well characterized chaperone.

24 ne activity is comparable to that of protein-disulfide isomerase, a well characterized chaperone.

25 In B cells, protein disulfide isomerase A1 (PDIA1/P4HB), the most abundant E

26 Co-expression of protein disulfide isomerase A2 that regulates disulfide bond for

27 secreted tick protein, I. scapularis protein disulfide isomerase A3 (IsPDIA3), enhances B. burgdorfer

28 n and impaired Golgi delivery of the protein disulfide isomerase A3 (PDIA3), an enzyme that catalyzes

29 ydrogenase B), redox regulation (eg, protein disulfide isomerase A3), contractile function (eg, filam

30 s, including calnexin, calreticulin, protein disulfide isomerase A3, tapasin, TAP1, and TAP2.

31 esponse (UPR) proteins calreticulin, protein disulfide-isomerase A3, and glutathione-S-transferase P.

32 Protein disulfide isomerase A6 (PDIA6) interacts with protein ki

33 in Pdia6, an essential gene encoding protein disulfide isomerase A6 (PDIA6), an oxidoreductase that f

34 close to the enzymatic center, and affected disulfide isomerase activity in vitro.

35 ic de novo mutation in P4HB that impairs the disulfide isomerase activity of PDI.

36 lasm is completely dependent on the level of disulfide isomerase activity of the cell.

37 M II1 (LQY1), a Zn finger protein that shows disulfide isomerase activity, interacts with the photosy

38 found that inhibitors of cell surface thiol/disulfide isomerase activity--5'5-dithio-bis(2-nitrobenz

39 activity, but it presents instead an unusual disulfide isomerase activity.

40 ombinant LQY1 protein demonstrates a protein disulfide isomerase activity.

41 than that of thioredoxin and consistent with disulfide isomerase activity.

42 hia coli mutants exhibiting enhanced protein disulfide isomerase activity.

43 wn to form a zinc finger and to have protein-disulfide isomerase activity.

44 by catalyzing the rearrangement of incorrect disulfides (isomerase activity).

45 ed disulfides with both CaBP1/P5 and protein disulfide isomerase, although these are generally viewed

46 t Hrd1 and gp78 interact with CT and protein disulfide isomerase, an ER chaperone that unfolds CTA1 t

47 aphs showed A9 in tubules containing protein disulfide isomerase, an ER lumenal protein, near immatur

48 otein, but also its ability to function as a disulfide isomerase and also impacted its interaction wi

49 utathione S-transferase pi (GSTP), a protein disulfide isomerase and catalyst of S-glutathionylation,

50 ure, to serve opposing functional roles as a disulfide isomerase and disulfide oxidase, respectively.

51 eticulum (ER) and is accomplished by protein disulfide isomerase and ER oxidoreductin 1beta, generati

52 TLR9 colocalizes with protein disulfide isomerase and is associated with either VAMP 7

53 We have identified a novel protein-disulfide isomerase and named it endothelial protein-dis

54 atalysts that include members of the protein-disulfide isomerase and peptidyl-prolyl isomerase famili

55 plasmid-encoded DsbP protein is a bona fide disulfide isomerase and suggest that a dedicated oxidati

56 These data identify a link between disulfide isomerases and tumor development, and provide

57 m (ER) chaperones (GRP78/BiP, GRP94, protein disulfide isomerase) and induction of the stress-inducib

58 , immunoglobulin-binding protein and protein disulfide isomerase, and by increased rates of apoptosis

59 dent chaperone proteins such as BiP, protein disulfide isomerase, and heat shock proteins.

60 Increased expression of protein disulfide isomerase antagonizes the rescue provided by o

61 n part, through de-repression of the protein disulfide isomerase anterior gradient 2 (Agr2).

62 c acid) (DTNB), bacitracin, and anti-protein disulfide isomerase antibody--inhibited cell-cell fusion

63 the nucleus, and although GRP78 and protein-disulfide isomerase are located largely in the endoplasm

64 n, we show that multiple isoforms of protein disulfide isomerase are major soluble proteins in Conus

65 8 (glucose-regulated protein 78) and protein-disulfide isomerase as putative physiological substrates

66 Protein-disulfide isomerase-associated 3 (Pdia3) is a multifunct

67 nant MTP and MTPv1 had an equivalent protein disulfide isomerase association, subcellular localizatio

68 p-regulate the ER proteins GRP94 and protein disulfide isomerase at both the transcript and protein l

69 ernal salt bridge leading to loss of protein disulfide isomerase binding and lipid transfer activitie

70 beta-sheet domains are important for protein disulfide isomerase binding and lipid transfer activity.

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

72 ed by ER oxidoreductin 1 (Ero1), and protein disulfide-isomerase can be inactivated by a feedback inh

73 te kinase (Ch), Annexin II (Ch), and protein disulfide isomerase (Ch).

74 Since prolyl-4-hydroxylase and protein disulfide isomerase coexist as a heterotetramer in the E

75 amed TR-PDI for "translocon-resident protein disulfide isomerase complex".

76 this single thioredoxin-like domain protein disulfide isomerase could play a critical role in the Le

77 naling, aPLs promote complement- and protein disulfide isomerase-dependent TF-integrin beta1 traffick

78 The mutation was located in the C-terminal disulfide isomerase domain of PDI, sterically close to t

79 The bacterial protein-disulfide isomerase DsbC is a homodimeric V-shaped enzym

80 The disulfide isomerase DsbC is required to regain ribonucle

81 membrane protein DsbD keeps the periplasmic disulfide isomerase DsbC reduced, using the cytoplasmic

82 cantly increased expression of the bacterial disulfide isomerase DsbC.

83 oadenylsulfate-reductase, or the periplasmic disulfide isomerase DsbC.

84 The Escherichia coli disulfide isomerase, DsbC is a V-shaped homodimer with e

85 In Escherichia coli, the periplasmic protein disulfide isomerase, DsbC, is maintained reduced by tran

86 al differences between two distantly related disulfide isomerases, DsbC and DsbG from Escherichia col

87 e isomerase and named it endothelial protein-disulfide isomerase (EndoPDI) because of its high expres

88 rotein-disulfide isomerase, probable protein-disulfide isomerase (ER60), beta- or gamma-cytoplasmic a

89 The genes encoding the disulfide isomerase ERp5 and beta-catenin were found to

90 evels of transcription and expression of the disulfide-isomerase ERp5 and of the disintegrin-metallop

91 Several thiol isomerases including protein disulfide isomerase, ERp57, and ERp5 are secreted by and

92 1, HMGB2), heat shock protein HSC70, protein disulfide isomerase ERp60, and glyceraldehyde 3-phosphat

93 ng glucose-regulated protein 78 kDa, protein disulfide isomerase family A, member 6, ER protein 44, a

94 odimer, and provided an example of a protein disulfide isomerase family member interacting with subst

95 nation of the oxidation status of ER protein-disulfide isomerase family members revealed a shift to a

96 2O2 as driving force for reoxidizing protein disulfide isomerase family members, thus efficiently con

97 surface F protein are reduced by the protein disulfide isomerase family of isomerases and that F prot

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

99 one of the five TMX proteins of the protein disulfide isomerase family, hitherto not linked to human

100 s were identified as a member of the protein disulfide isomerase family, thioredoxin reductase, and c

101 oreductase DsbC, a soluble periplasmic thiol-disulfide isomerase, for complementation.

102 Disulfide isomerases from prokaryotes and eukaryotes exh

103 lower eukaryotes, we have isolated a protein disulfide isomerase gene from the protozoan parasite Lei

104 as a substrate, other substrates are protein disulfide isomerase, glutaredoxin, glutathione peroxidas

105 s, and used these to show that while protein disulfide isomerase has little capacity for 2dCD4 reduct

106 , endoplasmic reticulum oxidase, and protein disulfide isomerase has revealed a consistent increase o

107 n 18, keratin 19, ATP synthase beta, protein disulfide isomerase, heat shock protein 27, cathepsin D,

108 these lysines to leucines abolished protein disulfide isomerase heterodimerization, lipid transfer,

109 SG) by the reduced a domain of human protein disulfide isomerase (hPDI) with atomistic resolution.

110 The human protein disulfide isomerase (hPDI), is an essential four-domain

111 cles that contained calreticulin and protein-disulfide isomerase in activated RAW 264.7 macrophages.

112 s as opposed to its association with protein disulfide isomerase in CECs.

113 oprotein, focal adhesion kinase, and protein-disulfide isomerase in proximity to actin filaments.

114 tein ABC transporter (floppase), and protein-disulfide isomerase in proximity to short actin filament

115 uggest that this complex could function as a disulfide isomerase in the rough endoplasmic reticulum.

116 Consistent with its function as a disulfide isomerase in vivo, the active sites of Pdi1p a

117 results strongly suggest that DsbC acts as a disulfide isomerase in vivo.

118 patterns for the various Hsp70s and protein disulfide isomerase indicate a likely general coordinate

119 nterior gradient-2 (AGR2), a soluble protein-disulfide isomerase involved in ER protein folding and q

120 Moreover, ERp5, a closely related disulfide isomerase involved in major histocompatibility

121 ERp57 is a disulfide isomerase involved in the folding of a subset

122 (ER) oxidoreductin (Ero1) oxidase to protein disulfide isomerase is an important pathway leading to d

123 Protein disulfide isomerase is another ER chaperone that demonst

124 A plasmid-encoded disulfide isomerase is associated with conjugation.

125 as an alpha2beta2 tetramer in which protein disulfide isomerase is the beta subunit with two differe

126 Pdi1p (protein-disulfide isomerase) is a folding assistant of the endop

127 g strategy we identified variants of PROTEIN DISULFIDE ISOMERASE LIKE 5-1 (HvPDIL5-1) as the cause of

128 ncing vector in maize indicated that protein disulfide isomerase-like and phosphoglycerate kinase wer

129 12446492 in the adjacent gene PDILT (protein disulfide isomerase-like, testis expressed) also reached

130 DsbC, the primary disulfide isomerase, likely resolves incorrect disulfide

131 els and a high expression of ERp5, a protein disulfide isomerase linked to MICA shedding (sMICA).

132 tertiary structures, associated with protein disulfide isomerase, localized to the endoplasmic reticu

133 , ATP synthase, elongation factor 2, protein disulfide isomerase, nucleophosmin-1, chaperonin, actin,

134 ioredoxin-like domains found in most protein disulfide isomerases, of which two contain an active sit

135 ne reductase and was an inhibitor of protein disulfide isomerase, one of the components of the redox-

136 acing all lumenal proteins with only protein disulfide isomerase or all cytosolic proteins with only

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

138 ), ERdj4, and HEDJ, as well as EDEM, protein disulfide isomerase-P5, and ribosome-associated membrane

139 e; copper zinc superoxide dismutase; protein disulfide isomerase, pancreatic; tropomyosin 2 (TM2); an

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

141 ng and to correct DSB errors through protein-disulfide isomerase (PDI) activity.

142 onstrated that the ER oxidoreductase protein disulfide isomerase (PDI) acts as a redox-dependent chap

143 Protein disulfide isomerase (PDI) and endoplasmic reticulum prot

144 on of two disulfide bond isomerases, protein disulfide isomerase (PDI) and ERdj5, in cell-cell fusion

145 ion 1 (ERO1) transfers disulfides to protein disulfide isomerase (PDI) and is essential for oxidative

146 mation in eukaryotes is dependent on protein-disulfide isomerase (PDI) and its homologs, which contai

147 ported that monoclonal antibodies to protein-disulfide isomerase (PDI) and other membrane-impermeant

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

149 concentrate in the RER, and bind to protein disulfide isomerase (PDI) and prolyl 4-hydroxylase 1 (P4

150 Protein-disulfide isomerase (PDI) and related members of the PDI

151 hours in this model was dependent on protein disulfide isomerase (PDI) and TF expression by myeloid c

152 t GNA colocalizes with the ER marker protein disulfide isomerase (PDI) and the COPI coat protein beta

153 s also suggest that the catalysis by protein disulfide isomerase (PDI) and thiol-disulfide exchange i

154 Glutaredoxin (Grx) and protein-disulfide isomerase (PDI) are members of the thioredoxin

155 stigate the therapeutic potential of protein disulfide isomerase (PDI) as a target to overcome resist

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

157 The folding assistant and chaperone protein-disulfide isomerase (PDI) catalyzes disulfide formation,

158 Protein-disulfide isomerase (PDI) catalyzes the formation and is

159 Protein-disulfide isomerase (PDI) catalyzes the formation of the

160 Protein disulfide isomerase (PDI) catalyzes the oxidation reduct

161 Protein disulfide isomerase (PDI) catalyzes the rearrangement of

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

163 Protein disulfide isomerase (PDI) derived from intravascular cel

164 Thiol isomerases such as protein-disulfide isomerase (PDI) direct disulfide rearrangement

165 TF is critical for coagulation, and protein disulfide isomerase (PDI) disables coagulation by target

166 We found that protein disulfide isomerase (PDI) facilitates CT retrotranslocat

167 the thioredoxin, oxidoreductase, and protein disulfide isomerase (PDI) families, among others.

168 Some members of the protein disulfide isomerase (PDI) family appear to facilitate ER

169 We show that the protein disulfide isomerase (PDI) family member pancreatic prote

170 endoplasmic reticulum (ER)-resident protein-disulfide isomerase (PDI) family members in lumbar spina

171 2 (AGR2), a protein belonging to the protein disulfide isomerase (PDI) family, is overexpressed in mu

172 gradient 2 (AGR2) is a member of the protein disulfide isomerase (PDI) family, which plays a role in

173 oscopy in mice generated by crossing protein disulfide isomerase (PDI) floxed mice with lysozyme-Cre

174 Recently, the protein disulfide isomerase (PDI) has been hypothesized to regul

175 Protein-disulfide isomerase (PDI) has been proposed to exhibit a

176 gen has been well characterized, and protein disulfide isomerase (PDI) has been suggested as a key pl

177 Protein disulfide isomerase (PDI) has long been assumed to assis

178 Protein disulfide isomerase (PDI) has two distinct CGHC redox-ac

179 ndoplasmic reticulum redox chaperone protein disulfide isomerase (PDI) in many cell types.

180 We show that protein disulfide isomerase (PDI) in the ER lumen functions to d

181 is study, we describe a new class of protein disulfide isomerase (PDI) inhibitors that significantly

182 Agr2 is a putative protein disulfide isomerase (PDI) initially identified as an est

183 Protein disulfide isomerase (PDI) interacts with these early int

184 Protein disulfide isomerase (PDI) is a chaperone protein in the

185 Protein disulfide isomerase (PDI) is a folding assistant of the

186 Protein disulfide isomerase (PDI) is a multifunctional protein c

187 Protein disulfide isomerase (PDI) is a multifunctional protein r

188 Protein-disulfide isomerase (PDI) is a ubiquitous dithiol-disulf

189 Protein-disulfide isomerase (PDI) is an essential catalyst of di

190 Protein disulfide isomerase (PDI) is an essential protein foldin

191 Protein disulfide isomerase (PDI) is an essential protein in Sac

192 Protein disulfide isomerase (PDI) is an oxidoreductase essential

193 Protein disulfide isomerase (PDI) is an oxidoreductase that has

194 Protein disulfide isomerase (PDI) is an oxidoreductase that medi

195 Protein disulfide isomerase (PDI) is one of the most abundant ER

196 Protein disulfide isomerase (Pdi) is reported to be an insulin-r

197 Extracellular protein disulfide isomerase (PDI) is required for platelet throm

198 Protein disulfide isomerase (PDI) is responsible for nascent pro

199 of this study was to explain whether protein disulfide isomerase (PDI) is responsible for the thiol-d

200 We have previously reported that protein disulfide isomerase (PDI) is S-nitrosylated in brains of

201 The oxidoreductase protein disulfide isomerase (PDI) is thought to be involved in t

202 previously determined that ERp29, a protein disulfide isomerase (PDI) member, extrudes the Py VP1 C-

203 Protein disulfide isomerase (PDI) oxidizes, reduces, and isomeri

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

205 sulfide bond Cys186-Cys 209 and that protein disulfide isomerase (PDI) regulates TF coagulant and sig

206 of beta-tubulin (TUBB) and Cys53 of protein disulfide isomerase (PDI) respectively.

207 mary quail myotubes transfected with protein disulfide isomerase (PDI) short hairpin RNAs showed a si

208 alian ER contains >20 members of the protein disulfide isomerase (PDI) superfamily, which ensure form

209 Protein-disulfide isomerase (PDI) switches tissue factor (TF) fr

210 Protein disulfide isomerase (PDI) utilizes the active site seque

211 Protein disulfide isomerase (PDI) was demonstrated to be involve

212 is protein, the addition of 4 microM protein disulfide isomerase (PDI) was found to lead to catalysis

213 Recently, protein-disulfide isomerase (PDI) was shown to interact with ADA

214 Protein disulfide isomerase (PDI), a folding catalyst and chaper

215 is revealed the 55-kDa protein to be protein disulfide isomerase (PDI), a member of the estrogen rece

216 An increase in the levels of protein-disulfide isomerase (PDI), a multifaceted endoplasmic re

217 This enzyme cooperates with protein disulfide isomerase (PDI), a redox chaperone previously

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

219 Protein-disulfide isomerase (PDI), an endoplasmic reticulum (ER)

220 Protein disulfide isomerase (PDI), an endoplasmic reticulum chap

221 olves a regulatory molecule, such as protein disulfide isomerase (PDI), an enzyme that plays a role i

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

223 novel regulator of the ER chaperone protein disulfide isomerase (PDI), and that through PDI, reticul

224 an inhibitory monoclonal antibody to protein disulfide isomerase (PDI), and the small-molecule PDI an

225 uribenzoates, or using inhibitors of protein disulfide isomerase (PDI), bacitracin or antibodies to P

226 the lumen of the ER by the action of protein disulfide isomerase (PDI), before being retrotranslocate

227 mass spectrometry to be composed of protein disulfide isomerase (PDI), calcium binding protein 1 (CA

228 1, ER luminal binding protein (BiP), protein disulfide isomerase (PDI), calreticulin (CRT), and calmo

229 Thiol isomerases, including protein disulfide isomerase (PDI), catalyze disulfide oxidation,

230 n as thiol isomerases, which include protein disulfide isomerase (PDI), endoplasmic reticulum protein

231 Protein disulfide isomerase (PDI), ERp5, and ERp57, among perhap

232 von Willebrand factor, multimerin-1, protein disulfide isomerase (PDI), ERp5, ERp57, and ERp72 eluted

233 th redox-isomerase activity, such as protein disulfide isomerase (PDI), facilitate Env conversion fro

234 s in Arabidopsis thaliana PDIL2-1, a protein disulfide isomerase (PDI), have reduced seed set, due to

235 cells, galectin-9 binds cell surface protein disulfide isomerase (PDI), increasing retention of PDI o

236 peptides, we sequenced and expressed protein-disulfide isomerase (PDI), peptidyl-prolyl cis-trans iso

237 Protein disulfide isomerase (PDI), secreted by platelets and end

238 Protein disulfide isomerase (PDI), secreted from platelets and e

239 Protein disulfide isomerase (PDI), the chief endoplasmic reticul

240 ulum (ER) oxido-reductases ERp57 and protein disulfide isomerase (PDI), the lectin chaperones calnexi

241 Surprisingly, we find that protein disulfide isomerase (PDI), the major protein oxidase of

242 differentially expressed genes was a protein disulfide isomerase (PDI), which is well known as a mole

243 Protein disulfide isomerase (PDI)-like proteins act as oxido-red

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

245 els of XBP1 and XBP1 targets such as protein disulfide isomerase (PDI).

246 most frequently recognized clone was protein disulfide isomerase (PDI).

247 vels of ER proteins calreticulin and protein disulfide isomerase (PDI).

248 expressing small interfering RNA to protein disulfide isomerase (PDI).

249 ive folding of proteins in the ER by protein disulfide isomerase (PDI).

250 s, Cys-Cys, and reduced and oxidized protein disulfide isomerase (PDI).

251 n oxidative folding was catalyzed by protein disulfide isomerase (PDI).

252 al protein relay involving Ero1p and protein disulfide isomerase (PDI).

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

254 tein Ero1p to secretory proteins via protein disulfide isomerase (PDI).

255 p.Tyr393Cys]), the gene that encodes protein disulfide isomerase (PDI).

256 ose-regulated protein 94 (GRP94) and protein disulfide isomerase (PDI).

257 ssive posttranslational oxidation of protein disulfide isomerase (PDI).

258 its, and the beta subunits formed by protein disulfide isomerase (PDI).

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

260 canonical DsbA oxidase and the DsbC protein disulfide isomerase (PDI)/reductase of Escherichia coli.

261 ecular chaperones BiP; GRP94; CaBP1; protein disulfide isomerase (PDI); ERdj3, a recently identified

262 conserved FAD-dependent enzyme, and protein disulfide isomerase (PDI); Ero1 is oxidized by molecular

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

264 e activity of the major ER-localized protein disulfide isomerase, PDI.

265 lex of the mannosidase Htm1p and the protein disulfide isomerase Pdi1p (Htm1p-Pdi1p) acts as a foldin

266 In vitro, protein disulfide isomerase (Pdi1p) introduces disulfides into p

267 oxidizing the soluble oxidoreductase protein disulfide isomerase (Pdi1p), which in turn can directly

268 putative interaction of VWF and the protein disulfide isomerase PDIA1, which has previously been use

269 plasmic reticulum and is mediated by protein disulfide isomerase (PDIA1).

270 A resident ER protein disulfide isomerase, PDIA6, limits the duration of IRE1a

271 erase (PDI) family member pancreatic protein disulfide isomerase (PDIp), previously considered exclus

272 Protein disulfide isomerases (PDIs) aid protein folding and asse

273 Protein disulfide isomerases (PDIs) are molecular chaperones tha

274 Protein disulfide isomerases (PDIs) areERfoldases identified as

275 estigation into the role of cellular protein disulfide isomerases (PDIs) by studying the effects of t

276 Protein disulfide isomerases (PDIs) catalyze the correct folding

277 Protein disulfide isomerases (PDIs) play a central role in this

278 Protein disulfide isomerases (PDIs) support endoplasmic reticulu

279 Protein disulfide isomerases play important roles in the maturat

280 ctases such as thioredoxin (Trx) and protein disulfide isomerase, play an essential role in regulatin

281 Protein disulfide isomerase plays a key role in catalyzing the f

282 DsbG, a protein disulfide isomerase present in the periplasm of Escheric

283 teins were identified as galectin-1, protein-disulfide isomerase, probable protein-disulfide isomeras

284 and secretion, such as calreticulin, protein disulfide isomerase, proteasome subunits, and isopenteny

285 Anterior Gradient 2 (AGR2) is a protein disulfide isomerase that plays important roles in divers

286 e compared our results with those of protein disulfide-isomerase, the eukaryotic counterpart of DsbA,

287 sis of some ER chaperones, including protein disulfide isomerase, their steady state levels do not dr

288 Disulfide isomerases (thiol isomerases), which catalyze

289 Here we show that an ER protein disulfide isomerase, thioredoxin domain containing 5 (TX

290 rom BiP, the toxin is transferred to protein disulfide isomerase; this ER redox chaperone is known to

291 to associate with calnexin, BiP, and protein-disulfide isomerase to form large, inactive complexes; d

292 n B (apoB) 17, it was unable to bind protein disulfide isomerase, transfer lipids, and support apoB s

293 ng binding to the two CxxC motifs of protein disulfide isomerase using a mutant RNase in which As-Mal

294 to the epidermis, and expression of protein disulfide isomerase was found primarily in the subepider

295 main with a CxxC sequence typical of protein disulfide isomerase (WCGHC).

296 C1 interacts with the oxidoreductase protein-disulfide isomerase, we hypothesized that thioredoxin-1

297 xin and ERp57, whereas BiP/GRP78 and protein disulfide isomerase were only modestly affected.

298 hy, such as smooth muscle myosin and protein-disulfide isomerase were up-regulated in EH30 but were d

299 s involved in the quality control is protein disulfide isomerase, which catalyzes the formation of pr

300 Four tested fusion proteins, maize PROTEIN DISULFIDE ISOMERASE-Yellow Fluorescent Protein, GLOSSY8a