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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
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
25 ne activity is comparable to that of protein-disulfide isomerase, a well characterized chaperone.
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
30 esponse (UPR) proteins calreticulin, protein disulfide-isomerase A3, and glutathione-S-transferase P.
34 onectin, indicating that most of the protein-disulfide isomerase activity of fibronectin is localized
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
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
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
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
60 GHC) is characteristic of eukaryotic protein-disulfide isomerases, and not other members of the thior
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
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
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
81 membrane protein DsbD keeps the periplasmic disulfide isomerase DsbC reduced, using the cytoplasmic
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
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
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
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
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.
112 cles that contained calreticulin and protein-disulfide isomerase in activated RAW 264.7 macrophages.
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.
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
124 (ER) oxidoreductin (Ero1) oxidase to protein disulfide isomerase is an important pathway leading to d
128 as an alpha2beta2 tetramer in which protein disulfide isomerase is the beta subunit with two differe
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
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
145 onstrated that the ER oxidoreductase protein disulfide isomerase (PDI) acts as a redox-dependent chap
147 on of two disulfide bond isomerases, protein disulfide isomerase (PDI) and ERdj5, in cell-cell fusion
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
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
160 The folding assistant and chaperone protein-disulfide isomerase (PDI) catalyzes disulfide formation,
165 This work investigates how QSOX and protein disulfide isomerase (PDI) cooperate in vitro to generate
168 TF is critical for coagulation, and protein disulfide isomerase (PDI) disables coagulation by target
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
176 gen has been well characterized, and protein disulfide isomerase (PDI) has been suggested as a key pl
186 shows a 55% identity with mammalian protein-disulfide isomerase (PDI) is a high capacity low affinit
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
202 previously determined that ERp29, a protein disulfide isomerase (PDI) member, extrudes the Py VP1 C-
205 sulfide bond Cys186-Cys 209 and that protein disulfide isomerase (PDI) regulates TF coagulant and sig
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
212 is protein, the addition of 4 microM protein disulfide isomerase (PDI) was found to lead to catalysis
215 is revealed the 55-kDa protein to be protein disulfide isomerase (PDI), a member of the estrogen rece
219 alpha-granule and lysosome cargo and protein disulfide isomerase (PDI), all of which serve to stabili
222 olves a regulatory molecule, such as protein disulfide isomerase (PDI), an enzyme that plays a role i
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
231 n as thiol isomerases, which include protein disulfide isomerase (PDI), endoplasmic reticulum protein
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
241 ulum (ER) oxido-reductases ERp57 and protein disulfide isomerase (PDI), the lectin chaperones calnexi
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
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
266 lex of the mannosidase Htm1p and the protein disulfide isomerase Pdi1p (Htm1p-Pdi1p) acts as a foldin
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
271 erase (PDI) family member pancreatic protein disulfide isomerase (PDIp), previously considered exclus
275 estigation into the role of cellular protein disulfide isomerases (PDIs) by studying the effects of t
280 ctases such as thioredoxin (Trx) and protein disulfide isomerase, play an essential role in regulatin
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
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
295 C1 interacts with the oxidoreductase protein-disulfide isomerase, we hypothesized that thioredoxin-1
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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