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1 derived endoplasmic reticulum (ER) chaperone glucose-regulated protein 170 (grp170) elicits potent an
2                                We found that glucose-regulated protein 170 (Grp170), the largest stre
3 a chain (IFN-gammaRalpha), and the chaperone glucose-regulated protein 58 (GRP58/ER-60/ERp57).
4 t data to show that one such tether protein, glucose regulated protein 75 (GRP75), is essential in in
5  that the 74-78-kDa protein(s) is related to glucose-regulated protein 75 (GRP-75), a member of the h
6 the voltage-dependent anion channel (VDAC)-1/glucose-regulated protein 75 (Grp75)/inositol 1,4,5-trip
7 protein family A (HSP70) member 9 (HSPA9) or glucose-regulated protein 75 (GRP75)] is a mitochondrial
8 ndent anion channel 1), the GRP75 (chaperone glucose-regulated protein 75), and the IP3R1 (inositol-1
9                                              Glucose regulated protein 78 (GRP78) is a chaperone prot
10  peptide exhibiting high binding affinity to glucose regulated protein 78 (GRP78) overexpressed in gl
11 ion of cell surface heat shock protein (HSP) glucose regulated protein 78 kDa (GRP78) was utilized fo
12 rotein chaperones (heat shock protein 70 and glucose regulated protein 78), and the antioxidant enzym
13 ss pathway mediated by the protein chaperone glucose regulated-protein 78 (GRP78).
14         In contrast, the expression level of glucose-regulated protein 78 (GRP 78) in RAW and HARM ce
15 lation of X-box-binding protein 1 (XBP1) and glucose-regulated protein 78 (GRP 78), and nuclear trans
16 was evaluated by measuring the expression of glucose-regulated protein 78 (GRP78 [BiP]) and editing o
17  chaperones such as Ig binding protein (BiP)/glucose-regulated protein 78 (GRP78) and by attenuating
18 MT expression inhibited homocysteine-induced glucose-regulated protein 78 (GRP78) and C/EBP-homologou
19 er affinity binding of PST-297S peptide with glucose-regulated protein 78 (GRP78) and insulin recepto
20 fied as crucial fungal invasins that bind to glucose-regulated protein 78 (GRP78) and integrins of ho
21                                Specifically, glucose-regulated protein 78 (Grp78) and spliced X-box b
22 in L-like and B-like proteases, histone H2A, glucose-regulated protein 78 (grp78) and stress-inducibl
23             CRIPTO and its signaling partner glucose-regulated protein 78 (GRP78) are highly expresse
24   Previously, we identified endothelial cell glucose-regulated protein 78 (GRP78) as a receptor for M
25                     Here, we have identified glucose-regulated protein 78 (GRP78) as what we believe
26                                         High glucose-regulated protein 78 (GRP78) expression contribu
27 ors strongly induce the transcription of the glucose-regulated protein 78 (grp78) gene, which encodes
28        We investigated the potential role of glucose-regulated protein 78 (GRP78) in mediating estrog
29     This study is to investigate the role of glucose-regulated protein 78 (GRP78) in the pulmonary mi
30                                          The glucose-regulated protein 78 (GRP78) is a plasminogen (P
31                                              Glucose-regulated protein 78 (GRP78) is an endoplasmic r
32                                              Glucose-regulated protein 78 (GRP78) mRNA levels were co
33      It has been suggested that cell surface glucose-regulated protein 78 (GRP78) was involved in thi
34 ur post-OIR mice pups' retinas revealed that glucose-regulated protein 78 (GRP78) was one of the seve
35 50-kDa oxygen-regulated protein (ORP150) and glucose-regulated protein 78 (GRP78)) is induced by NSAI
36 s identified as the surface membrane form of glucose-regulated protein 78 (GRP78), a member of the he
37                                              Glucose-regulated protein 78 (GRP78), a molecular chaper
38     This screen led to our identification of glucose-regulated protein 78 (GRP78), an endoplasmic ret
39 psies, staining of 4-hydroxynonenal (4-HNE), glucose-regulated protein 78 (Grp78), and C/EBP-homologo
40 factor 6 (ATF6) and their downstream targets glucose-regulated protein 78 (GRP78), glucose-regulated
41  determined by mass spectrometry analysis as glucose-regulated protein 78 (Grp78), indicating the sur
42      Ig binding protein (BiP), also known as glucose-regulated protein 78 (GRP78), is a critical ER c
43  influence expression of ERSR genes, such as glucose-regulated protein 78 (GRP78), that contribute to
44 P1 induces certain ER-targeted proteins, eg, glucose-regulated protein 78 (GRP78), that help resolve
45 approach and cell biology techniques for the glucose-regulated protein 78 (GRP78), the spliced X-box-
46    Alpha2M* binds to cell surface-associated glucose-regulated protein 78 (GRP78), which activates do
47 uding serving as a cofactor of the chaperone glucose-regulated protein 78 (GRP78).
48 es, glucose-regulated protein 94 (GRP94) and glucose-regulated protein 78 (GRP78).
49 elial cells (MvEC) in a manner that requires glucose-regulated protein 78 (GRP78).
50 endoplasmic reticulum (ER) chaperone protein glucose-regulated protein 78 (GRP78)/binding immunoglobu
51                                              Glucose-regulated protein 78 (GRP78)/BiP is a multifunct
52 forms a complex with the molecular chaperone glucose-regulated protein 78 (GRP78, also known as BiP),
53 volved in protein quality control, including glucose-regulated protein 78 (GRP78/BiP), a regulator of
54 ol intragastrically exhibited an increase in glucose-regulated protein 78 and inositol-requiring enzy
55                                              Glucose-regulated protein 78 and protein disulfide isome
56  the voltage-dependent anion channel and the glucose-regulated protein 78 have been identified as pla
57                                              Glucose-regulated protein 78 is reduced in AT2 cells fro
58 ssion of heat shock protein 72 kDa (HSP-72), glucose-regulated protein 78 kDa (GRP-78), and GRP-94 in
59 e have previously demonstrated the role that glucose-regulated protein 78 kDa (GRP78) acetylation and
60             In such glioma cancer cells, the glucose-regulated protein 78 kDa (GRP78) is particularly
61                            Overexpression of glucose-regulated protein 78 kDa in the liver abolished
62 and genetic (overexpression of the chaperone glucose-regulated protein 78 kDa) approaches.
63 tion with the SR/ER-resident protein, GRP78 (glucose-regulated protein 78 kDa).
64 nvolved in adiponectin maturation, including glucose-regulated protein 78 kDa, protein disulfide isom
65                     The chaperone GRP78/BiP (glucose-regulated protein 78 kDa/binding immunoglobulin
66 did not induce HO-1 mRNA expression, whereas glucose-regulated protein 78 mRNA was increased.
67  between voltage-dependent anion channel and glucose-regulated protein 78 on the surface of 1-LN huma
68 ess response, the unfolded protein response (glucose-regulated protein 78 pathway), and the ER overlo
69 endoplasmic reticulum (ER) chaperones GRP78 (glucose-regulated protein 78) and GRP94 (glucose-regulat
70            In addition, we identified GRP78 (glucose-regulated protein 78) and protein-disulfide isom
71 ng autoantibody titers against citrullinated glucose-regulated protein 78, and reduced spontaneous ne
72 SERCA expression and increased expression of glucose-regulated protein 78, C/EBP homologous protein,
73                         Here, we report that glucose-regulated protein 78, exposed on cell surfaces o
74 n-containing protein 2, elongation factor 2, glucose-regulated protein 78, transketolase, and succiny
75 on localized in the N-terminal domain of the glucose-regulated protein 78, whereas microplasminogen d
76 caspase-7, consistent with the disruption of glucose-regulated protein 78-procaspase-7 complexes.
77 channel and microplasminogen does so via the glucose-regulated protein 78.
78 does so through the C-terminal domain of the glucose-regulated protein 78.
79 ild-type gB, gB deltaI, and gB KNPm, but the glucose-regulated proteins 78 (BiP) and 94 formed stable
80 R, the ER-targeted cytoprotective chaperones glucose-regulated proteins 78 and 94 (GRP78 and GRP94),
81 g immunoglobulin heavy chain-binding protein/glucose-regulated protein, 78 kDa and CCAAT/enhancer bin
82                                       GRP78 (glucose-regulated protein, 78 kDa) is a key regulator of
83 atrix identified several proteins, including glucose regulated protein-78 kDa (GRP-78), heterogeneous
84                                              Glucose-regulated protein-78 (GRP-78) is an endoplasmic
85  process is initiated by DMP1 binding to the glucose-regulated protein-78 (GRP-78) localized on the p
86 doplasmic reticulum stress signals including glucose-regulated protein-78 (GRP78), activating transcr
87 s by binding to the stress response protein, glucose-regulated protein-78 (GRP78), expressed at the s
88 surface complex with the HSP70 family member glucose-regulated protein-78 (GRP78).
89 sed expression of chaperone proteins such as glucose-regulated protein-78 and activation of caspase-1
90                   IR increases expression of glucose-regulated protein 78kDa (GRP78) on the surface o
91                                              Glucose regulated protein 94 (Grp94) is the endoplasmic
92 (ER)-resident heat shock protein 90 paralog, glucose regulated protein 94 (Grp94), but their co-aggre
93 ons of the utility of peptide complexes with glucose regulated protein 94 (GRP94, also known as gp96)
94  Here we show that NK-specific deficiency of glucose-regulated protein 94 (gp96) leads to decreased m
95 6 (ATF6) and induction of the ER chaperones, glucose-regulated protein 94 (GRP94) and glucose-regulat
96 argets glucose-regulated protein 78 (GRP78), glucose-regulated protein 94 (GRP94) and protein disulfi
97     Binding immunoglobulin protein (BiP) and glucose-regulated protein 94 (Grp94) are endoplasmic ret
98 roles of the endoplasmic reticulum chaperone glucose-regulated protein 94 (GRP94) are poorly understo
99   In this study, we investigated the role of glucose-regulated protein 94 (GRP94) in human beta cell
100 duction of both IGF-I and IGF-II, we ablated glucose-regulated protein 94 (GRP94) in murine striated
101                                              Glucose-regulated protein 94 (GRP94) is a major endoplas
102                                              Glucose-regulated protein 94 (GRP94) is an endoplasmic r
103 zed that the ER-resident molecular chaperone glucose-regulated protein 94 (GRP94) is part of this qua
104 sm by which N-glycosylation of the chaperone glucose-regulated protein 94 (GRP94) is regulated to con
105     Here, we have explored the importance of glucose-regulated protein 94 (GRP94), a prominent ER cha
106 pliced X-box-binding protein 1 (sXBP-1), the glucose-regulated protein 94 (GRP94), and the calreticul
107               The ER-resident Hsp90 isoform, glucose-regulated protein 94 (Grp94), promotes the aggre
108                     The human HSP90 isoform, glucose-regulated protein 94 (GRP94), resides in the end
109 ted knockdown strategies, we determined that glucose-regulated protein 94 (Grp94), the ER equivalent
110                                Tumor-derived glucose-regulated protein 94 (GRP94/gp96) has shown grea
111                                              Glucose-regulated protein 94 (GRP94/gp96), the endoplasm
112 78 (glucose-regulated protein 78) and GRP94 (glucose-regulated protein 94), and the ER lectins calnex
113                                GRP78 (78 kDa glucose-regulated protein), a key endoplasmic reticulum
114                                   The 78 kDa-glucose regulated protein, a chaperone molecule, was kno
115 and interactions with the cochaperone 78-kDa glucose-regulated protein (binding immunoglobulin protei
116                   Notably, ER stress markers glucose-regulated protein, C/EBP homolog protein, splice
117     For example, cancer progression requires glucose regulated protein (GRP) 78 for cancer cell survi
118                                              Glucose Regulated Protein (GRP) 94 and GRP78 are critica
119 s proteins, heat shock protein (hsp) 110 and glucose-regulated protein (grp) 170, have shown them to
120                                              Glucose-regulated protein (Grp) 94 depletion reduces mut
121 epend on the endoplasmic reticulum chaperone glucose-regulated protein (GRP) 94.
122     Another SDK activity was copurified with glucose-regulated protein (GRP) and heat shock proteins
123 ion of stress proteins or chaperones such as glucose-regulated protein (GRP) and protein-disulphide i
124 uding stress response genes belonging to the glucose-regulated protein (grp) family.
125 tion block, the transcription of a family of glucose-regulated protein (GRP) genes encoding endoplasm
126 (2+) store, the transcription of a family of glucose-regulated protein (GRP) genes encoding ER chaper
127 y, can constitutively induce the promoter of glucose-regulated protein (grp) genes through activation
128 nitiation factor-2alpha (phospho-eIF2alpha), glucose-regulated protein (GRP)-78, and GRP94; and (b) t
129  the recognition of native and citrullinated glucose-regulated protein (GRP)78 peptides by CD8(+) T c
130 ases in the mRNA levels of the ER chaperones glucose-regulated protein (grp)78/immunoglobulin-binding
131            Of 1176 toxicology-related genes, glucose-regulated proteins (GRP-78 and -94), growth arre
132                                  The 170 kDa glucose-regulated protein (grp170) is an endoplasmic ret
133 he other as its mitochondrial homologue, the glucose-regulated protein grp75.
134 tracts of irradiated glioma cells identified glucose-regulated protein GRP78 as the receptor target f
135                                          The glucose-regulated protein GRP78, a major endoplasmic ret
136    Upregulation of UPR proteins, such as the glucose-regulated protein Grp78, induced the formation o
137                                   The 78-kDa glucose-regulated protein GRP78/BiP is a key endoplasmic
138  that BIK selectively forms complex with the glucose-regulated protein GRP78/BiP, a major ER chaperon
139 he MDA-7/IL-24 and PERK chaperone BiP/78-kDa glucose regulated protein (GRP78), and overexpression of
140 with ER-protein processing chaperone, 78-kDa glucose regulated protein (GRP78), and with trafficking-
141 vidence that cancer cells overexpress 78-kDa glucose-regulated protein (GRP78) as a mechanism to acqu
142 ostate cancer patients identified the 78-kDa glucose-regulated protein (GRP78) as one such target.
143   This study is to explore the role of 78 kD glucose-regulated protein (GRP78) in the development of
144 c supplementation of the ER chaperone 78-kDa glucose-regulated protein (GRP78) in the SFO.
145                                       78 kDa glucose-regulated protein (Grp78) is a heat shock protei
146                                   The 78-kDa glucose-regulated protein (GRP78) is a well-established
147         We show that the cell surface 78-kDa glucose-regulated protein (GRP78), a receptor that binds
148 the heat shock protein 70 family, the 78-kDa glucose-regulated protein (GRP78), also referred to as B
149                                   The 78-kDa glucose-regulated protein (GRP78), an endoplasmic reticu
150  corresponded to a M(r) approximately 78,000 glucose-regulated protein (GRP78), was observed.
151 h resulted in the upregulation of the 78-kDa glucose-regulated protein (GRP78).
152 pha-2-macroglobulin, and for SNTRVAP, 78-kDa glucose-regulated protein (GRP78).
153                                              Glucose-regulated protein (GRP78)/BiP, a major chaperone
154 damage-inducible protein 34 (GADD34), 78-kDa glucose-regulated protein (GRP78)/BiP, inositol-requirin
155 -regulation of chaperones such as the 78-kDa glucose-regulated protein (GRP78, also referred to as Bi
156 erone calreticulin, but not calnexin, 78 kDa glucose-regulated protein (Grp78/BiP) or protein disulfi
157 , we report that the stress-inducible 78-kDa glucose-regulated protein (GRP78/HSPA5), a key regulator
158 plasmic reticulum (ER) homologue, the 94 kDa glucose regulated protein (Grp94).
159  complex between p185c-erbB-2 and the 94-kDa glucose-regulated protein, GRP94, to which geldanamycin
160                Although the induction of the glucose-regulated proteins (GRPs) is commonly used as an
161 s with binding immunoglobulin protein/78-kDa glucose-regulated protein, in drug combination-treated c
162 xpressed in the endoplasmic reticulum, is a "glucose-regulated protein" induced by stress responses t
163 es encoding adaptive functions including the glucose-regulated proteins is induced.
164                       PAS kinase (PASK) is a glucose-regulated protein kinase involved in the control
165 eptor-related protein (LRP) and cell surface glucose-regulated protein [Mr approximately 78000 (GRP78
166  ER also possesses a single large Hsp70, the glucose-regulated protein of 170 kDa (Grp170).
167  by the nucleotide exchange factors, Grp170 (glucose-regulated protein of 170kDa) and Sil1, both of w
168       Circulating autoantibodies against the glucose-regulated protein of 78 kDa (GRP78) are present
169 C/EBP-homologous protein), as well as GRP78 (glucose-regulated protein of 78 kDa) was examined in sev
170                                              Glucose-regulated protein of 94 kDa (GRP94), the endopla
171                      MTJ-1 associates with a glucose-regulated protein of Mr approximately 78,000(GRP
172 cluding protein di-sulfide isomerase, 78 kDa glucose-regulated protein precursor, heat shock protein
173 ithelial cells (A549), keratin 18, the 78-kD glucose-regulated protein, trans-1, 2-dihyrobenzene-1,2-
174 onitis exhibited increased expression of the glucose-regulated proteins upregulated during ER stress
175 ulator binding immunoglobulin protein/78-kDa glucose-regulated protein was down-regulated, activating
176  endoplasmic reticulum stress marker, 78 kDa glucose-regulated protein, was up-regulated, whereas ant

 
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