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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 , calnexin, calreticulin, ERp57, and protein disulfide isomerase.
7 ose-regulated protein (Grp78/BiP) or protein disulfide isomerase.
8 P75, HSP70, HSP60, HSP54, HSP27, and protein disulfide isomerase.
9 rease the effectiveness of DsbG as a protein disulfide isomerase.
10 e endoplasmic reticulum (ER) marker, protein disulfide isomerase.
11 tion in the ER lumen is prevented by 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 anging disulfide bonds, and giardial protein-disulfide isomerase-2 also displayed oxidant and reducta
20 ed to an abnormal redox state of the protein disulfide-isomerase 4.
21 acted with the endomembrane proteins protein disulfide isomerase 5 (PDI5) and NAI2, with the PDI5 int
22 and from a resident ER enzyme called protein disulfide isomerase, a chaperone that has oxidoreductase
23                                      Protein disulfide isomerase, a second molecular chaperone of the
24  the complex was higher than that of protein-disulfide isomerase, a well characterized chaperone.
25 ne activity is comparable to that of protein-disulfide isomerase, a well characterized chaperone.
26                     Co-expression of protein disulfide isomerase A2 that regulates disulfide bond for
27 n and impaired Golgi delivery of the protein disulfide isomerase A3 (PDIA3), an enzyme that catalyzes
28 ydrogenase B), redox regulation (eg, protein disulfide isomerase A3), contractile function (eg, filam
29 s, including calnexin, calreticulin, protein disulfide isomerase A3, tapasin, TAP1, and TAP2.
30 esponse (UPR) proteins calreticulin, protein disulfide-isomerase A3, and glutathione-S-transferase P.
31                                      Protein disulfide isomerase A6 (PDIA6) interacts with protein ki
32  close to the enzymatic center, and affected disulfide isomerase activity in vitro.
33                        Moreover, the protein-disulfide isomerase activity of fibronectin appears to b
34 onectin, indicating that most of the protein-disulfide isomerase activity of fibronectin is localized
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 GHC) is characteristic of eukaryotic protein-disulfide isomerases, and not other members of the thior
61              Increased expression of protein disulfide isomerase antagonizes the rescue provided by o
62 n part, through de-repression of the protein disulfide isomerase anterior gradient 2 (Agr2).
63 c acid) (DTNB), bacitracin, and anti-protein disulfide isomerase antibody--inhibited cell-cell fusion
64  the nucleus, and although GRP78 and protein-disulfide isomerase are located largely in the endoplasm
65 n, we show that multiple isoforms of protein disulfide isomerase are major soluble proteins in Conus
66 is confirmed by co-localization with protein-disulfide isomerase as determined by double indirect imm
67 8 (glucose-regulated protein 78) and protein-disulfide isomerase as putative physiological substrates
68                                      Protein-disulfide isomerase-associated 3 (Pdia3) is a multifunct
69 nant MTP and MTPv1 had an equivalent protein disulfide isomerase association, subcellular localizatio
70 p-regulate the ER proteins GRP94 and protein disulfide isomerase at both the transcript and protein l
71 ernal salt bridge leading to loss of protein disulfide isomerase binding and lipid transfer activitie
72 beta-sheet domains are important for protein disulfide isomerase binding and lipid transfer activity.
73     Glucose-regulated protein 78 and protein disulfide isomerase, both endoplasmic reticulum chaperon
74 te kinase (Ch), Annexin II (Ch), and protein disulfide isomerase (Ch).
75       Since prolyl-4-hydroxylase and protein disulfide isomerase coexist as a heterotetramer in the E
76 amed TR-PDI for "translocon-resident protein disulfide isomerase complex".
77  this single thioredoxin-like domain protein disulfide isomerase could play a critical role in the Le
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                        ERcalcistorin/protein-disulfide isomerase (ECaSt/PDI) shows a 55% identity wit
88 e isomerase and named it endothelial protein-disulfide isomerase (EndoPDI) because of its high expres
89 rotein-disulfide isomerase, probable protein-disulfide isomerase (ER60), beta- or gamma-cytoplasmic a
90                       The genes encoding the disulfide isomerase ERp5 and beta-catenin were found to
91 evels of transcription and expression of the disulfide-isomerase ERp5 and of the disintegrin-metallop
92   Several thiol isomerases including protein disulfide isomerase, ERp57, and ERp5 are secreted by and
93 1, HMGB2), heat shock protein HSC70, protein disulfide isomerase ERp60, and glyceraldehyde 3-phosphat
94 ng glucose-regulated protein 78 kDa, protein disulfide isomerase family A, member 6, ER protein 44, a
95 odimer, and provided an example of a protein disulfide isomerase family member interacting with subst
96 nation of the oxidation status of ER protein-disulfide isomerase family members revealed a shift to a
97 2O2 as driving force for reoxidizing protein disulfide isomerase family members, thus efficiently con
98 surface F protein are reduced by the protein disulfide isomerase family of isomerases and that F prot
99             ERdj5 is a member of the protein disulfide isomerase family of proteins localized to the
100 s were identified as a member of the protein disulfide isomerase family, thioredoxin reductase, and c
101 e involving the chaperones Grp78 and protein disulfide isomerase, followed by degradation via a ubiqu
102 oreductase DsbC, a soluble periplasmic thiol-disulfide isomerase, for complementation.
103                                              Disulfide isomerases from prokaryotes and eukaryotes exh
104 lower eukaryotes, we have isolated a protein disulfide isomerase gene from the protozoan parasite Lei
105 as a substrate, other substrates are protein disulfide isomerase, glutaredoxin, glutathione peroxidas
106 s, and used these to show that while protein disulfide isomerase has little capacity for 2dCD4 reduct
107 , endoplasmic reticulum oxidase, and protein disulfide isomerase has revealed a consistent increase o
108 n 18, keratin 19, ATP synthase beta, protein disulfide isomerase, heat shock protein 27, cathepsin D,
109  these lysines to leucines abolished protein disulfide isomerase heterodimerization, lipid transfer,
110 SG) by the reduced a domain of human protein disulfide isomerase (hPDI) with atomistic resolution.
111                            The human protein disulfide isomerase (hPDI), is an essential four-domain
112 cles that contained calreticulin and protein-disulfide isomerase in activated RAW 264.7 macrophages.
113 s as opposed to its association with protein disulfide isomerase in CECs.
114 oprotein, focal adhesion kinase, and protein-disulfide isomerase in proximity to actin filaments.
115 tein ABC transporter (floppase), and protein-disulfide isomerase in proximity to short actin filament
116 uggest that this complex could function as a disulfide isomerase in the rough endoplasmic reticulum.
117            Consistent with its function as a disulfide isomerase in vivo, the active sites of Pdi1p a
118 results strongly suggest that DsbC acts as a disulfide isomerase in vivo.
119  patterns for the various Hsp70s and protein disulfide isomerase indicate a likely general coordinate
120 nterior gradient-2 (AGR2), a soluble protein-disulfide isomerase involved in ER protein folding and q
121            Moreover, ERp5, a closely related disulfide isomerase involved in major histocompatibility
122                                   ERp57 is a disulfide isomerase involved in the folding of a subset
123 ctivity is efficiently restored when protein disulfide isomerase is also present.
124 (ER) oxidoreductin (Ero1) oxidase to protein disulfide isomerase is an important pathway leading to d
125                                      Protein disulfide isomerase is another ER chaperone that demonst
126                            A plasmid-encoded disulfide isomerase is associated with conjugation.
127                                      Protein-disulfide isomerase is essential for formation and reshu
128  as an alpha2beta2 tetramer in which protein disulfide isomerase is the beta subunit with two differe
129                               Pdi1p (protein-disulfide isomerase) is a folding assistant of the endop
130 g strategy we identified variants of PROTEIN DISULFIDE ISOMERASE LIKE 5-1 (HvPDIL5-1) as the cause of
131 ncing vector in maize indicated that protein disulfide isomerase-like and phosphoglycerate kinase wer
132 12446492 in the adjacent gene PDILT (protein disulfide isomerase-like, testis expressed) also reached
133                            DsbC, the primary disulfide isomerase, likely resolves incorrect disulfide
134 els and a high expression of ERp5, a protein disulfide isomerase linked to MICA shedding (sMICA).
135 tertiary structures, associated with protein disulfide isomerase, localized to the endoplasmic reticu
136 , ATP synthase, elongation factor 2, protein disulfide isomerase, nucleophosmin-1, chaperonin, actin,
137 ioredoxin-like domains found in most protein disulfide isomerases, of which two contain an active sit
138 ne reductase and was an inhibitor of protein disulfide isomerase, one of the components of the redox-
139 acing all lumenal proteins with only protein disulfide isomerase or all cytosolic proteins with only
140    Here we show that a gene encoding protein disulfide isomerase P5 (PDI-P5) is expressed at high lev
141 ), ERdj4, and HEDJ, as well as EDEM, protein disulfide isomerase-P5, and ribosome-associated membrane
142 e; copper zinc superoxide dismutase; protein disulfide isomerase, pancreatic; tropomyosin 2 (TM2); an
143              Different inhibitors of protein disulfide isomerase (PDI) activity were able to inhibit
144 ng and to correct DSB errors through protein-disulfide isomerase (PDI) activity.
145 onstrated that the ER oxidoreductase protein disulfide isomerase (PDI) acts as a redox-dependent chap
146                                      Protein disulfide isomerase (PDI) and endoplasmic reticulum prot
147 on of two disulfide bond isomerases, protein disulfide isomerase (PDI) and ERdj5, in cell-cell fusion
148 oorly understood mechanism requiring protein disulfide isomerase (PDI) and ERO1.
149  endoplasmic reticulum (ER) requires protein disulfide isomerase (PDI) and Ero1p.
150 ion 1 (ERO1) transfers disulfides to protein disulfide isomerase (PDI) and is essential for oxidative
151 mation in eukaryotes is dependent on protein-disulfide isomerase (PDI) and its homologs, which contai
152 ported that monoclonal antibodies to protein-disulfide isomerase (PDI) and other membrane-impermeant
153  by accepting electrons from reduced protein disulfide isomerase (PDI) and passing them on to molecul
154  concentrate in the RER, and bind to protein disulfide isomerase (PDI) and prolyl 4-hydroxylase 1 (P4
155                                      Protein-disulfide isomerase (PDI) and related members of the PDI
156 hours in this model was dependent on protein disulfide isomerase (PDI) and TF expression by myeloid c
157 t GNA colocalizes with the ER marker protein disulfide isomerase (PDI) and the COPI coat protein beta
158 s also suggest that the catalysis by protein disulfide isomerase (PDI) and thiol-disulfide exchange i
159               Glutaredoxin (Grx) and protein-disulfide isomerase (PDI) are members of the thioredoxin
160  The folding assistant and chaperone protein-disulfide isomerase (PDI) catalyzes disulfide formation,
161                                      Protein-disulfide isomerase (PDI) catalyzes the formation and is
162                                      Protein-disulfide isomerase (PDI) catalyzes the formation of the
163                                      Protein disulfide isomerase (PDI) catalyzes the oxidation reduct
164                                      Protein disulfide isomerase (PDI) catalyzes the rearrangement of
165  This work investigates how QSOX and protein disulfide isomerase (PDI) cooperate in vitro to generate
166                                      Protein disulfide isomerase (PDI) derived from intravascular cel
167             Thiol isomerases such as protein-disulfide isomerase (PDI) direct disulfide rearrangement
168  TF is critical for coagulation, and protein disulfide isomerase (PDI) disables coagulation by target
169                        We found that protein disulfide isomerase (PDI) facilitates CT retrotranslocat
170                  Some members of the protein disulfide isomerase (PDI) family appear to facilitate ER
171                     We show that the protein disulfide isomerase (PDI) family member pancreatic prote
172  endoplasmic reticulum (ER)-resident protein-disulfide isomerase (PDI) family members in lumbar spina
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                   Agr2 is a putative protein disulfide isomerase (PDI) initially identified as an est
182                                      Protein disulfide isomerase (PDI) interacts with these early int
183                                      Protein-disulfide isomerase (PDI) is a catalyst of folding of di
184                                      Protein disulfide isomerase (PDI) is a chaperone protein in the
185                                      Protein disulfide isomerase (PDI) is a folding assistant of the
186  shows a 55% identity with mammalian protein-disulfide isomerase (PDI) is a high capacity low affinit
187                                      Protein disulfide isomerase (PDI) is a multifunctional protein c
188                                      Protein disulfide isomerase (PDI) is a multifunctional protein r
189                                      Protein-disulfide isomerase (PDI) is a ubiquitous dithiol-disulf
190                                      Protein-disulfide isomerase (PDI) is an essential catalyst of di
191                                      Protein disulfide isomerase (PDI) is an essential protein foldin
192                                      Protein disulfide isomerase (PDI) is an essential protein in Sac
193                                      Protein disulfide isomerase (PDI) is an oxidoreductase essential
194                                      Protein disulfide isomerase (PDI) is an oxidoreductase that has
195                                      Protein disulfide isomerase (PDI) is an oxidoreductase that medi
196                                      Protein disulfide isomerase (PDI) is one of the most abundant ER
197                                      Protein disulfide isomerase (Pdi) is reported to be an insulin-r
198                        Extracellular protein disulfide isomerase (PDI) is required for platelet throm
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                            Recently, protein disulfide isomerase (PDI), a protein that catalyzes thio
218          This enzyme cooperates with protein disulfide isomerase (PDI), a redox chaperone previously
219 alpha-granule and lysosome cargo and protein disulfide isomerase (PDI), all of which serve to stabili
220                                      Protein-disulfide isomerase (PDI), an endoplasmic reticulum (ER)
221                                      Protein disulfide isomerase (PDI), an endoplasmic reticulum chap
222 olves a regulatory molecule, such as protein disulfide isomerase (PDI), an enzyme that plays a role i
223 ry acidic protein (GFAP), NF-kappaB, protein disulfide isomerase (PDI), and Nissl staining.
224  novel regulator of the ER chaperone protein disulfide isomerase (PDI), and that through PDI, reticul
225 an inhibitory monoclonal antibody to protein disulfide isomerase (PDI), and the small-molecule PDI an
226 uribenzoates, or using inhibitors of protein disulfide isomerase (PDI), bacitracin or antibodies to P
227 the lumen of the ER by the action of protein disulfide isomerase (PDI), before being retrotranslocate
228  mass spectrometry to be composed of protein disulfide isomerase (PDI), calcium binding protein 1 (CA
229 1, ER luminal binding protein (BiP), protein disulfide isomerase (PDI), calreticulin (CRT), and calmo
230          Thiol isomerases, including protein disulfide isomerase (PDI), catalyze disulfide oxidation,
231 n as thiol isomerases, which include protein disulfide isomerase (PDI), endoplasmic reticulum protein
232                                      Protein disulfide isomerase (PDI), ERp5, and ERp57, among perhap
233 von Willebrand factor, multimerin-1, protein disulfide isomerase (PDI), ERp5, ERp57, and ERp72 eluted
234 th redox-isomerase activity, such as protein disulfide isomerase (PDI), facilitate Env conversion fro
235 s in Arabidopsis thaliana PDIL2-1, a protein disulfide isomerase (PDI), have reduced seed set, due to
236 cells, galectin-9 binds cell surface protein disulfide isomerase (PDI), increasing retention of PDI o
237 peptides, we sequenced and expressed protein-disulfide isomerase (PDI), peptidyl-prolyl cis-trans iso
238                                      Protein disulfide isomerase (PDI), secreted by platelets and end
239                                      Protein disulfide isomerase (PDI), secreted from platelets and e
240                                      Protein disulfide isomerase (PDI), the chief endoplasmic reticul
241 ulum (ER) oxido-reductases ERp57 and protein disulfide isomerase (PDI), the lectin chaperones calnexi
242           Surprisingly, we find that protein disulfide isomerase (PDI), the major protein oxidase of
243 y, purified preparations of platelet protein disulfide isomerase (PDI), vitronectin, alpha-thrombin,
244 differentially expressed genes was a protein disulfide isomerase (PDI), which is well known as a mole
245                                      Protein disulfide isomerase (PDI)-like proteins act as oxido-red
246 pattern was found for the ER luminal protein disulfide isomerase (PDI).
247 els of XBP1 and XBP1 targets such as protein disulfide isomerase (PDI).
248 most frequently recognized clone was protein disulfide isomerase (PDI).
249 vels of ER proteins calreticulin and protein disulfide isomerase (PDI).
250  expressing small interfering RNA to protein disulfide isomerase (PDI).
251 ive folding of proteins in the ER by protein disulfide isomerase (PDI).
252 s, Cys-Cys, and reduced and oxidized protein disulfide isomerase (PDI).
253 n oxidative folding was catalyzed by protein disulfide isomerase (PDI).
254 p.Tyr393Cys]), the gene that encodes protein disulfide isomerase (PDI).
255 al protein relay involving Ero1p and protein disulfide isomerase (PDI).
256 match those of the in vivo catalyst, protein disulfide isomerase (PDI).
257 tein Ero1p to secretory proteins via protein disulfide isomerase (PDI).
258 ssive posttranslational oxidation of protein disulfide isomerase (PDI).
259 its, and the beta subunits formed by protein disulfide isomerase (PDI).
260 d co-localization of Tom20/Nur77 and Protein Disulfide Isomerase (PDI)/Nur77.
261  canonical DsbA oxidase and the DsbC protein disulfide isomerase (PDI)/reductase of Escherichia coli.
262 ecular chaperones BiP; GRP94; CaBP1; protein disulfide isomerase (PDI); ERdj3, a recently identified
263  conserved FAD-dependent enzyme, and protein disulfide isomerase (PDI); Ero1 is oxidized by molecular
264                  Thus, inhibition of protein disulfide isomerases (PDI) required for protein folding
265 e activity of the major ER-localized protein disulfide isomerase, PDI.
266 lex of the mannosidase Htm1p and the protein disulfide isomerase Pdi1p (Htm1p-Pdi1p) acts as a foldin
267                            In vitro, protein disulfide isomerase (Pdi1p) introduces disulfides into p
268 oxidizing the soluble oxidoreductase protein disulfide isomerase (Pdi1p), which in turn can directly
269  putative interaction of VWF and the protein disulfide isomerase PDIA1, which has previously been use
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 rom BiP, the toxin is transferred to protein disulfide isomerase; this ER redox chaperone is known to
290 to associate with calnexin, BiP, and protein-disulfide isomerase to form large, inactive complexes; d
291 n B (apoB) 17, it was unable to bind protein disulfide isomerase, transfer lipids, and support apoB s
292 ng binding to the two CxxC motifs of protein disulfide isomerase using a mutant RNase in which As-Mal
293  to the epidermis, and expression of protein disulfide isomerase was found primarily in the subepider
294 main with a CxxC sequence typical of protein disulfide isomerase (WCGHC).
295 C1 interacts with the oxidoreductase protein-disulfide isomerase, we hypothesized that thioredoxin-1
296 xin and ERp57, whereas BiP/GRP78 and protein disulfide isomerase were only modestly affected.
297 aperones GRP94/gp96, BiP, ERp72, and protein disulfide isomerase were purified in parallel from B16/F
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

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