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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 kDa glucose-regulated protein (Grp78/BiP) or protein disulfide isomerase.
8 RP78, GRP75, HSP70, HSP60, HSP54, HSP27, and protein disulfide isomerase.
9 y to increase the effectiveness of DsbG as a protein disulfide isomerase.
10 with the endoplasmic reticulum (ER) marker, protein disulfide isomerase.
11 no activity was observed for BiP, ERp72, and protein disulfide isomerase.
12 sbC is active both in vivo and in vitro as a protein disulfide isomerase.
13 e identified as the abundant reticuloplasmin protein disulfide isomerase.
14 gomerization in the ER lumen is prevented by protein disulfide isomerase.
15 oplasmic reticulum oxidoreductases ERp57 and protein disulfide isomerase.
16 heir active sites, including thioredoxin and protein-disulfide isomerase.
17 vesicles and correlated with the presence of protein-disulfide isomerase.
18 ular switch of ADAM17 activity operated by a protein-disulfide isomerase.
19 ed folding at pH 7.5 even in the presence of protein-disulfide isomerase.
20 resemble the Escherichia coli DsbC and DsbG protein disulfide isomerases.
21 reticulum oxidoreductin1 oxidoreductase and protein disulfide isomerases.
22 of rearranging disulfide bonds, and giardial protein-disulfide isomerase-2 also displayed oxidant and
24 L1 interacted with the endomembrane proteins protein disulfide isomerase 5 (PDI5) and NAI2, with the
25 elping hand from a resident ER enzyme called protein disulfide isomerase, a chaperone that has oxidor
27 ivity of the complex was higher than that of protein-disulfide isomerase, a well characterized chaper
28 chaperone activity is comparable to that of protein-disulfide isomerase, a well characterized chaper
30 formation and impaired Golgi delivery of the protein disulfide isomerase A3 (PDIA3), an enzyme that c
31 tate dehydrogenase B), redox regulation (eg, protein disulfide isomerase A3), contractile function (e
32 partners, including calnexin, calreticulin, protein disulfide isomerase A3, tapasin, TAP1, and TAP2.
33 rotein response (UPR) proteins calreticulin, protein disulfide-isomerase A3, and glutathione-S-transf
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
40 act fibronectin, indicating that most of the protein-disulfide isomerase activity of fibronectin is l
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,
48 to its EDTA-conformation in the presence of protein disulfide isomerase and the inability of thrombo
51 olding catalysts that include members of the protein-disulfide isomerase and peptidyl-prolyl isomeras
52 reticulum (ER) chaperones (GRP78/BiP, GRP94, protein disulfide isomerase) and induction of the stress
53 eticulin, immunoglobulin-binding protein and protein disulfide isomerase, and by increased rates of a
54 ER-resident chaperone proteins such as BiP, protein disulfide isomerase, and heat shock proteins.
55 teins (CGHC) is characteristic of eukaryotic protein-disulfide isomerases, and not other members of t
57 ogram, in part, through de-repression of the protein disulfide isomerase anterior gradient 2 (Agr2).
58 robenzoic acid) (DTNB), bacitracin, and anti-protein disulfide isomerase antibody--inhibited cell-cel
59 addition, we show that multiple isoforms of protein disulfide isomerase are major soluble proteins i
60 osol and the nucleus, and although GRP78 and protein-disulfide isomerase are located largely in the e
61 finding is confirmed by co-localization with protein-disulfide isomerase as determined by double indi
62 ied GRP78 (glucose-regulated protein 78) and protein-disulfide isomerase as putative physiological su
64 recombinant MTP and MTPv1 had an equivalent protein disulfide isomerase association, subcellular loc
65 cells up-regulate the ER proteins GRP94 and protein disulfide isomerase at both the transcript and p
66 s an internal salt bridge leading to loss of protein disulfide isomerase binding and lipid transfer a
67 erminal beta-sheet domains are important for protein disulfide isomerase binding and lipid transfer a
69 These data show that sulfhydryl oxidase and protein disulfide isomerase can cooperate in vitro in th
73 ing that this single thioredoxin-like domain protein disulfide isomerase could play a critical role i
75 nalogous aspartate (or glutamate) residue in protein disulfide isomerase, DsbA, and other thiol:disul
82 disulfide isomerase and named it endothelial protein-disulfide isomerase (EndoPDI) because of its hig
83 tin-1, protein-disulfide isomerase, probable protein-disulfide isomerase (ER60), beta- or gamma-cytop
85 2 (HMGB1, HMGB2), heat shock protein HSC70, protein disulfide isomerase ERp60, and glyceraldehyde 3-
86 including glucose-regulated protein 78 kDa, protein disulfide isomerase family A, member 6, ER prote
87 he heterodimer, and provided an example of a protein disulfide isomerase family member interacting wi
88 uminal H2O2 as driving force for reoxidizing protein disulfide isomerase family members, thus efficie
89 in cell surface F protein are reduced by the protein disulfide isomerase family of isomerases and tha
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
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
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
110 ticulum (ER) oxidoreductin (Ero1) oxidase to protein disulfide isomerase is an important pathway lead
112 cterized as an alpha2beta2 tetramer in which protein disulfide isomerase is the beta subunit with two
114 ent catalysis of disulfide rearrangements by protein-disulfide isomerase is found to involve an escap
116 l cloning strategy we identified variants of PROTEIN DISULFIDE ISOMERASE LIKE 5-1 (HvPDIL5-1) as the
117 ene silencing vector in maize indicated that protein disulfide isomerase-like and phosphoglycerate ki
118 verting deiodinase, two metabolic enzymes, a protein disulfide isomerase-like protein that may bind T
120 MICA levels and a high expression of ERp5, a protein disulfide isomerase linked to MICA shedding (sMI
121 ary and tertiary structures, associated with protein disulfide isomerase, localized to the endoplasmi
122 tor beta, ATP synthase, elongation factor 2, protein disulfide isomerase, nucleophosmin-1, chaperonin
123 four thioredoxin-like domains found in most protein disulfide isomerases, of which two contain an ac
124 lutathione reductase and was an inhibitor of protein disulfide isomerase, one of the components of th
125 by replacing all lumenal proteins with only protein disulfide isomerase or all cytosolic proteins wi
127 p58(IPK), ERdj4, and HEDJ, as well as EDEM, protein disulfide isomerase-P5, and ribosome-associated
128 a-amylase; copper zinc superoxide dismutase; protein disulfide isomerase, pancreatic; tropomyosin 2 (
130 yses demonstrated that the ER oxidoreductase protein disulfide isomerase (PDI) acts as a redox-depend
132 expression of two disulfide bond isomerases, protein disulfide isomerase (PDI) and ERdj5, in cell-cel
135 ) oxidation 1 (ERO1) transfers disulfides to protein disulfide isomerase (PDI) and is essential for o
136 ormation by accepting electrons from reduced protein disulfide isomerase (PDI) and passing them on to
137 olecules concentrate in the RER, and bind to protein disulfide isomerase (PDI) and prolyl 4-hydroxyla
138 over 6 hours in this model was dependent on protein disulfide isomerase (PDI) and TF expression by m
139 aled that GNA colocalizes with the ER marker protein disulfide isomerase (PDI) and the COPI coat prot
140 r results also suggest that the catalysis by protein disulfide isomerase (PDI) and thiol-disulfide ex
141 n TGases, but it has significant homology to protein disulfide isomerase (PDI) and, particularly, to
146 bond of TF is critical for coagulation, and protein disulfide isomerase (PDI) disables coagulation b
150 is a novel membrane protein belonging to the protein disulfide isomerase (PDI) family, and Eps1 co-lo
152 tal microscopy in mice generated by crossing protein disulfide isomerase (PDI) floxed mice with lysoz
154 roteins which share active-site homology wit protein disulfide isomerase (PDI) has been identified fr
155 procollagen has been well characterized, and protein disulfide isomerase (PDI) has been suggested as
158 nd the endoplasmic reticulum redox chaperone protein disulfide isomerase (PDI) in many cell types.
176 The aim of this study was to explain whether protein disulfide isomerase (PDI) is responsible for the
181 ndent on Eps1, a transmembrane member of the protein disulfide isomerase (PDI) oxidoreductase family.
182 f the disulfide bond Cys186-Cys 209 and that protein disulfide isomerase (PDI) regulates TF coagulant
184 ise, primary quail myotubes transfected with protein disulfide isomerase (PDI) short hairpin RNAs sho
185 the mammalian ER contains >20 members of the protein disulfide isomerase (PDI) superfamily, which ens
188 es of this protein, the addition of 4 microM protein disulfide isomerase (PDI) was found to lead to c
190 e analysis revealed the 55-kDa protein to be protein disulfide isomerase (PDI), a member of the estro
193 ease of alpha-granule and lysosome cargo and protein disulfide isomerase (PDI), all of which serve to
195 ding involves a regulatory molecule, such as protein disulfide isomerase (PDI), an enzyme that plays
196 fibrillary acidic protein (GFAP), NF-kappaB, protein disulfide isomerase (PDI), and Nissl staining.
197 ins is a novel regulator of the ER chaperone protein disulfide isomerase (PDI), and that through PDI,
198 thiols, an inhibitory monoclonal antibody to protein disulfide isomerase (PDI), and the small-molecul
199 or mercuribenzoates, or using inhibitors of protein disulfide isomerase (PDI), bacitracin or antibod
200 lded in the lumen of the ER by the action of protein disulfide isomerase (PDI), before being retrotra
201 y tandem mass spectrometry to be composed of protein disulfide isomerase (PDI), calcium binding prote
202 60), SKP1, ER luminal binding protein (BiP), protein disulfide isomerase (PDI), calreticulin (CRT), a
204 mes known as thiol isomerases, which include protein disulfide isomerase (PDI), endoplasmic reticulum
206 sterin, von Willebrand factor, multimerin-1, protein disulfide isomerase (PDI), ERp5, ERp57, and ERp7
207 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
214 ic reticulum (ER) oxido-reductases ERp57 and protein disulfide isomerase (PDI), the lectin chaperones
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
235 from the canonical DsbA oxidase and the DsbC protein disulfide isomerase (PDI)/reductase of Escherich
236 the molecular chaperones BiP; GRP94; CaBP1; protein disulfide isomerase (PDI); ERdj3, a recently ide
237 a novel conserved FAD-dependent enzyme, and protein disulfide isomerase (PDI); Ero1 is oxidized by m
240 o be reduced by a cell surface population of protein-disulfide isomerase (PDI) and its cytotoxicity w
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
244 ith the luminal endoplasmic reticulum marker protein-disulfide isomerase (PDI) and that was in a simi
250 ation of endoplasmic reticulum (ER)-resident protein-disulfide isomerase (PDI) family members in lumb
252 on and isomerization during protein folding, protein-disulfide isomerase (PDI) has two catalytic site
254 aSt/PDI) shows a 55% identity with mammalian protein-disulfide isomerase (PDI) is a high capacity low
261 de-rich peptides, we sequenced and expressed protein-disulfide isomerase (PDI), peptidyl-prolyl cis-t
263 rypsin, rendered nicked toxin susceptible to protein disulfide isomerase- (PDI-) mediated reduction.
264 the complex of the mannosidase Htm1p and the protein disulfide isomerase Pdi1p (Htm1p-Pdi1p) acts as
266 ctively oxidizing the soluble oxidoreductase protein disulfide isomerase (Pdi1p), which in turn can d
267 ined the putative interaction of VWF and the protein disulfide isomerase PDIA1, which has previously
269 ide isomerase (PDI) family member pancreatic protein disulfide isomerase (PDIp), previously considere
273 e an investigation into the role of cellular protein disulfide isomerases (PDIs) by studying the effe
278 xidoreductases such as thioredoxin (Trx) and protein disulfide isomerase, play an essential role in r
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
285 We have compared our results with those of protein disulfide-isomerase, the eukaryotic counterpart
287 e synthesis of some ER chaperones, including protein disulfide isomerase, their steady state levels d
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
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
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