ライフサイエンスコーパス: MG132

1 r N-benzoyloxycarbonyl (Z)-Leu-Leu-leucinal (MG132).

2 r N-benzoyloxycarbonyl (Z)-Leu-Leu-leucinal (MG132).

3 upon chemical inhibition of the proteasome (MG132).

4 rom degradation by the proteasome inhibitor, MG132.

5 hich was blocked by the proteasome inhibitor MG132.

6 n effect blocked by the proteasome inhibitor MG132.

7 tion was blocked by the proteasome inhibitor MG132.

8 as able to counter the inhibitory effects of MG132.

9 pre-treatment with the proteasome inhibitor MG132.

10 was stabilized by the proteasomal inhibitor MG132.

11 re all abolished by the proteasome inhibitor MG132.

12 olide, as well as proteasome inhibition with MG132.

13 plants treated with the proteasome inhibitor MG132.

14 tion CaR mutants to proteasome inhibition by MG132.

15 ith the presence of the proteasome inhibitor MG132.

16 fragments) were stabilized by the action of MG132.

17 ent or treated with the proteasome inhibitor MG132.

18 in the presence of the proteasome inhibitor, MG132.

19 crosomal pellet) isolated in the presence of MG132.

20 s and stabilized by the proteasome inhibitor MG132.

21 as not inhibited by the proteasome inhibitor MG132.

22 y pretreatment with the proteosome inhibitor MG132.

23 ed fibroblasts with the proteasome inhibitor MG132.

24 ors lactacystin, proteasome inhibitor 1, and MG132.

25 y NFkappaB translocation and is sensitive to MG132.

26 ing treatment with the proteasome inhibitor, MG132.

27 re detected in cells treated with 17-AAG and MG132.

28 y increased by UPS inhibitors bortezomib and MG132.

29 in the presence of the proteasomal inhibitor MG132.

30 or 50 ng/mL), HGF (10 ng/mL) and 5 or 10 muM MG132.

31 AAG is inhibited by the proteasome inhibitor MG132.

32 al control levels, even after treatment with MG132.

33 ith the proteasome inhibitors bortezomib and MG132.

34 reversed utilizing the proteasome inhibitor MG132.

35 by treating cells with proteasome inhibitor MG132.

36 in the presence of the proteasome inhibitor, MG132.

37 on was magnified by the proteasome inhibitor MG132.

38 acid analogs or the 26S proteasome inhibitor MG132.

39 icities of bortezomib and another inhibitor, MG132.

40 ld be prevented by the proteasomal inhibitor MG132.

41 ted remnant clearance in the same fashion as MG132.

42 that was blocked by the proteasome inhibitor MG132.

43 ich were rescued by the proteasome inhibitor MG132.

44 n the stationary phase of cells treated with MG132.

45 ich is prevented by the proteasome inhibitor MG132.

46 by application of the proteasome inhibitor, MG132.

47 d in the presence of the proteasome inhbitor MG132.

48 ich was prevented by a proteasome inhibitor, MG132.

49 on was inhibited by the proteasome inhibitor MG132.

50 ed through inhibition of the proteasome with MG132.

51 n be neutralized by the proteasome inhibitor MG132.

52 urvival action, may antagonize the action of MG132.

53 in the presence of the proteasome inhibitor MG132.

54 eriments using proteasome inhibitors such as MG132.

55 V1 was abrogated by the proteasome inhibitor MG132.

56 by treatment with the proteasome inhibitor, MG132.

57 -L-cysteine largely prevented the effects of MG132.

58 mostly reversed by the proteasomal inhibitor MG132.

59 by either polyQ or the proteasome inhibitor MG132.

60 P3A stabilization, we examined the effect of MG132 (0-300 microM) concentration-dependent proteasomal

61 d, with and without the proteasome inhibitor MG132 (10 microM).

62 h 1 or 10 ng/mL TGF-beta(2), with or without MG132 (2.5 or 10 muM, respectively).

63 asome, and inhibition of the proteasome with MG132 (a proteasome inhibitor) prevented Bim degradation

64 80 (a specific inhibitor of p38 MAPK) and by MG132 (a specific inhibitor of NF-kappaB).

65 MG132, a peptide aldehyde that competitively inhibits th

66 gely suppressed by chronic administration of MG132, a potent cell permeable proteasome inhibitor.

67 inhibition was abolished in the presence of MG132, a potent inhibitor of the 26 S proteasome.

68 MG132, a potent proteasome inhibitor and activator of RO

69 MG132, a proteasomal inhibitor, rescued PC-1 knockdown-d

70 S1P1 degradation is blocked by MG132, a proteasomal inhibitor.

71 VSMC treatment with MG132, a proteasome inhibitor, indicated that PD184161 i

72 Treatment of cells with MG132, a proteasome inhibitor, inhibited eEF-2 kinase de

73 intermediate chain, a process suppressed by MG132, a proteasome inhibitor.

74 This decrease was inhibited by MG132, a proteasome inhibitor.

75 was partially reversed by pretreatment with MG132, a proteasome inhibitor.

76 mains, and their interaction was enhanced by MG132, a proteasome inhibitor.

77 lasts have strikingly different responses to MG132, a proteasome inhibitor; proliferating cells rapid

78 Depletion of ATP or the presence of MG132, a proteasome/lysosome inhibitor, resulted in stab

79 K3 null MEFs is stabilized by treatment with MG132, a proteosome inhibitor.

80 s from this patient following treatment with MG132, a specific proteasome inhibitor, and normal level

81 was dispersed throughout the cytoplasm when MG132, a specific proteasome inhibitor, was added.

82 The proteasome inhibitor MG132 abolished down-regulation of ERalpha by TPSF.

83 onsistently, inhibition of the proteasome by MG132 abolished high-glucose-induced reduction of GTPCH

84 ing the proteosomal degradation of MCPIP1 by MG132 abrogated HIV-1 production in phorbol 12-myristate

85 In parallel, MG132 also activated GCN2 [general control nonderepressi

86 at, in the presence of proteasomal inhibitor MG132, also contain proteasomal components.

87 anta stabilization assays in the presence of MG132, an inhibitor of proteasome activity, demonstrated

88 MG132, an inhibitor of proteasome function, prevented de

89 eostemin protein is completely stabilized by MG132, an inhibitor of the 26S proteasome, as are the le

90 The treatment with MG132, an inhibitor of ubiquitin proteasome system, resc

91 apII was blocked by the proteasome inhibitor MG132 and a Cullin5 (Cul5) dominant negative mutant.

92 tially inhibited by the proteasome inhibitor MG132 and a dominant negative form of ubiquitin, indicat

93 tially inhibited by the proteasome inhibitor MG132 and a dominant negative mutant of ubiquitin, K6W-U

94 eatment with the 26 S proteosome inhibitors, MG132 and ALLN, leads to detection of ubiquitinated HDAC

95 arably to treatment with protease inhibitors MG132 and ALLN.

96 A1 ZnBD is inhibited by proteosome inhibitor MG132 and also by E64 and EGTA, suggesting that proteoly

97 d by immunostaining, Endo H sensitivity, and MG132 and bafilomycin failed effect.

98 idenced by blocking with specific inhibitors MG132 and bafilomycin, respectively.

99 Here we show that the proteasome inhibitors MG132 and bortezomib activate the RIPK3-MLKL necroptotic

100 Treatment with the proteasome inhibitors MG132 and bortezomib increased WASP levels in T cells fr

101 hat well-known proteasome inhibitors such as MG132 and bortezomib, as well as the recently discovered

102 hypersensitive to the proteasome inhibitors MG132 and bortezomib.

103 LRP1-deficient fibroblasts was prevented by MG132 and chloroquine.

104 onation of pol II from cells co-treated with MG132 and cisplatin indicated that the undegraded ubiqui

105 Notably, MG132 and EerI (proteasomal and endoplasmic reticulum-as

106 ere we showed that the proteasome inhibitors MG132 and epoxomicin blocked a postentry step in vaccini

107 CMPG1 is stabilized by the inhibitors MG132 and epoxomicin, indicating that it is degraded by

108 ant of CIS, and by the proteasome inhibitors MG132 and epoxomicin, which prolong GHR signaling to STA

109 hat genome replication was inhibited by both MG132 and epoxomicin, which would account for the effect

110 by treatments with the proteasome inhibitors MG132 and lactacystin that did not affect NO production.

111 Proteasome inhibitors, MG132 and lactacystin, blocked the NO donor-induced redu

112 MG132 and lactacystin, inhibitors of the ubiquitin-prote

113 t is inhibited by the proteasome inhibitors, MG132 and lactacystin.

114 By contrast, MG132 and LC potentiated the activity of activator prote

115 Proteosome inhibitor MG132 and lentiviruses enabling inducible expression or

116 by the proteasome inhibitors bortezomib and MG132 and much reduced in top2beta(-/-) mouse embryonic

117 mbinations of the cell cycle inhibitors with MG132 and obtained data suggesting that MG132 may also b

118 NFkappaB translocation, it is not altered by MG132 and therefore is not likely to be regulated by NFk

119 IFN-gamma production that can be reversed by MG132 and/or chloroquine, and it inhibits cytolytic acti

120 Proteasome inhibitors (bortezomib and MG132) and depletion of 19S and 20S proteasome subunits

121 s N-benzoyloxycarbonyl (Z)-Leu-Leu-leucinal (MG132) and N-benzoyloxycarbonyl-Leu-Leu-Leu-B(OH)(2) (MG

122 s with the 26S proteasome-specific inhibitor MG132, and by expressing the FAD2-1A cDNA in yeast strai

123 Three proteasome inhibitors (NLVS, MG132, and clasto-lactacystin beta-lactone) were tested

124 inhibited by the proteasome inhibitors NLVS, MG132, and clasto-lactacystin beta-lactone.

125 hyposensitivity to the proteasome inhibitor MG132, and decreased 26S complex stability.

126 idly increased upon incubation of cells with MG132, and ectopic overexpression of c-Jun mimicked the

127 URF2 was blocked by the proteasome inhibitor MG132, and SMURF2 efficiently ubiquitinated both overexp

128 In contrast, MG132, another (less specific) proteasome inhibitor, str

129 ther heat shock treatment or the presence of MG132 are on a productive pathway, supporting a model in

130 Proteasome inhibitors (e.g., bortezomib, MG132) are known to enhance adeno-associated virus (AAV)

131 NAi and injection of anti-dynein antibody in MG132-arrested metaphase cells produced similar effects.

132 hat proteasome inhibition with bortezomib or MG132 attenuated overall ligand-induced degradation of E

133 Pretreatment with proteasome inhibitor MG132 blocked ischemia-induced degradation of PTEN and b

134 MG132 blocked SGI-1027-induced depletion of DNMT1, indic

135 r N-benzoyloxycarbonyl (Z)-Leu-Leu-leucinal (MG132) blocked SU9516-mediated Mcl-1 down-regulation, im

136 Bafilomycin A1, but not MG132, blocked TGF-beta1 down-regulation of p27, suggest

137 Pretreatment with the proteasome inhibitor MG132 blocks IL-1beta-mediated reductions in nuclear RXR

138 re partially blocked by proteasome inhibitor MG132 but not by the lysosome inhibitor chloroquine.

139 h N-benzoyloxycarbonyl-(Z)-Leu-Leu-leucinal (MG132) but not leptomycin B suppressed AhR loss.

140 some inhibitors (bortezomib, epoxomicin, and MG132), but not to proteotoxic or ER stress, caused a 2-

141 was not affected by the proteasome inhibitor MG132, but it was suppressed by bafilomycin A1, which le

142 ized in the presence of proteasome inhibitor MG132, but its instability was independent of a function

143 by inhibition with the proteasomal inhibitor MG132, but not by other protease inhibitors.

144 ting seedlings with the proteasome inhibitor MG132 (carbobenzoxy-Leu-Leu-Leu-al), strongly suggesting

145 MG132 caused a significant increase in p21 and p27 prote

146 MG132 caused no significant change in heat shock factor

147 At the mRNA level, the proteasome inhibitor, MG132, caused a >10-fold increase in HSP27 and a small i

148 Treatment of cells with MG132 causes an accumulation of the aberrant tubulins, i

149 ing P3HR1 cells with a proteasome inhibitor, MG132, causes the accumulation of SUMO-Rta and promotes

150 ed by TGF-beta(2) treatment and inhibited by MG132 co-treatment.

151 Although the proteasome inhibitor MG132 completely blocked K(b)-SIINFEKL complex generatio

152 The NF-kappaB inhibitor MG132 completely inhibited IBDV-induced DNA fragmentatio

153 We found a biphasic MG132 concentration effect on CYP3A turnover: Stabilizat

154 Because the MG132 concentration used in those studies was 10-fold hi

155 ed, we found a marked (approximately 4-fold) MG132 concentration-dependent PERK autophosphorylation,

156 At these high MG132 concentrations, such CYP3A suppression could be du

157 f polyubiquitination in proteasome-inhibited MG132 controls.

158 in levels; these increases were inhibited by MG132 cotreatment.

159 oss of opioid receptors was not prevented by MG132, demonstrating a different degradation pathway.

160 e loss of proteasome activity in response to MG132, demonstrating that it boosted protein homeostasis

161 s were treated with the proteasome inhibitor MG132, demonstrating that p14(ARF) augments proteasomal

162 on, we were unable to biochemically detect a MG132-dependent cohort of NA DRiPs relevant for Ag proce

163 Moreover, knockdown of Nrf1 attenuates the MG132-dependent increase in proteasome subunit expressio

164 The MG132-dependent loss of Bmi-1 and Ezh2 is associated wit

165 Exposure of cells early in infection to MG132 does not result in retention of ICP0 as in wild-ty

166 MG132 effectively blocked degradation of both pp27Thr187

167 nhibitor (Bay11), or a proteasome inhibitor (MG132) effectively inhibited their inflammatory response

168 MG132 elicited a robust increase in the folding chaperon

169 he presence of the proteasome inhibitor with MG132, endogenous and expressed betaAPP levels are signi

170 cells inhibition of proteasomal activity by MG132 enhances the level of hypophosphorylated, unmodifi

171 ure to 1 microM of the proteasomal inhibitor MG132 for 24 h nor RNA interference WSB-1 knockdown resu

172 lls incubated with the proteasomal inhibitor MG132 further confirmed that they were degraded via the

173 We found that both MG132 (>1 microM) and Bortezomib (>0.025 microM) induced

174 DNA damage, whereas the proteasome inhibitor MG132 had no effect.

175 However, MG132 has been reported to suppress P450s 3A as a result

176 In the presence of an NF-kappaB inhibitor MG132, IL-8 transcription was inhibited, but not that of

177 changes in IL-6 were largely insensitive to MG132 in astrocytes, but were largely MG132-sensitive in

178 dysfunction induced by proteasome inhibitor MG132 in both human lymphoblast cells and MCF7 cells.

179 absence of the proteasome activity inhibitor MG132 in infected cells.

180 ic inhibition of the proteasome activity via MG132 in postnatal mice could exacerbate glial TDP-43-me

181 preincubated with the proteasomal inhibitor MG132 in the absence of globin chain expression vector a

182 e embryos treated with proteasomal inhibitor MG132, in which intact sperm mitochondrial sheaths were

183 ince treatment with the proteasome inhibitor MG132 increased levels of NF-kappaB/p65 protein and decr

184 hat long-term incubation with PIs (PS-341 or MG132) increased NF-kappaB-regulated gene expression suc

185 of Panc-1 cells with a proteasome inhibitor, MG132, increased the HPK1 protein levels in a dose-depen

186 Proteasome inhibition by MG132 increases the occupancy of p53 protein at p53-resp

187 was stabilized in the HCMV-infected cells by MG132, indicating a shift from p53 to HDM2 ubiquitinatio

188 effect is partially reversed by leupeptin or MG132, indicating that both the lysosomal and proteasoma

189 nd is stabilized by the proteasome inhibitor MG132, indicating that it is degraded via the ubiquitin-

190 n can be completely blocked by 10 micromol/L MG132, indicating that the degradation is mediated by pr

191 high Pi is blocked in pho2 and inhibited by MG132, indicating the requirement of UBC24 and 26S prote

192 sensitized serum-starved quiescent cells to MG132-induced apoptosis.

193 Quercetin decreased MG132-induced expression of HSP27, -70, and -90 by more

194 ibition of cellular proteolysis by Z-L3VS or MG132 induces abnormal elongation of daughter centrioles

195 findings reveal that at high concentrations, MG132 is indeed cytotoxic and can suppress CYP3A synthes

196 The proteasome inhibitors MG132, lactacystin, and epoxomicin blocked PICT1 degrada

197 egradation with the 26S proteasome inhibitor MG132 largely restored c-Jun protein levels, suggesting

198 Finally, treating cells with MG132 leads to accumulation of polyubiquitinated SENP2,

199 In particular, proteasome inhibition with MG132 markedly stimulated PA28 binding to exposed 20S al

200 with MG132 and obtained data suggesting that MG132 may also boost transduction by causing G2/M cell c

201 [carbobenzoxy-L-leucyl-L-leucyl-L-leucinal (MG132), MG115 (carbobenzoxy-L-leucyl-L-leucyl-L-norvalin

202 ne impairment recovered upon the addition of MG132, mirroring the Boc-D-cmk response.

203 in the presence of the proteasomal inhibitor MG132; mutation of all putative intracellular loop and c

204 Stimulating without MG132, Myc peaked at 2.5 hrs, and at steady was ~8 +/- 1

205 The presence of the proteasome inhibitor MG132 [N-benzoyloxycarbonyl (Z)-Leu-Leuleucinal] increas

206 at inhibition of ET1-induced SRF activity by MG132 occurs at the level downstream of heterotrimeric G

207 8 activities and the antiapoptotic effect of MG132 on IFN-gamma-treated LECs.

208 erexpression of c-Jun mimicked the effect of MG132 on SRF activity.

209 were obtained with the proteasome inhibitor MG132, one of the most potent inhibitors of LT toxicity.

210 Finally, administration of MG132 or a superoxide dismutase mimetic, tempol, reverse

211 the same degree as the NF-kappaB inhibitors MG132 or BAY 11-7082, and there was no additive effect w

212 analyzed the proapoptotic activities of PIs (MG132 or Bortezomib) in NSCLC cells.

213 by treatment with the proteasome inhibitors MG132 or lactacystin or high concentrations of leupeptin

214 Blocking the proteasomal pathway with either MG132 or lactacystin prevented rapamycin from partially

215 We report here that the addition of MG132 or lactacystin, each a specific inhibitor of cellu

216 he presence of proteasome-specific inhibitor MG132 or MG115 and ubiquitinated in plant cells, suggest

217 and HEK293T cells with proteasome inhibitors MG132 or Omuralide increases Drosha protein levels.

218 Inhibition of the 26S proteasome with either MG132 or PR-11 prevented the high glucose-triggered redu

219 effects were prevented by pretreatment with MG132 or replacement of ATP with ATP-gamma-S, a nonhydro

220 Finally, either administration of MG132 or supplementation of l-sepiapterin normalized the

221 ild-type roots with the proteosome inhibitor MG132 or the gibberellic acid (GA) synthesis inhibitor p

222 RGS4 protein was observed in the presence of MG132 or the specific proteasome inhibitor lactacystin a

223 n proteasomal degradation was inhibited with MG132 or ubiquitination was prevented by the lysine-to-a

224 y N-benzoyloxycarbonyl (Z)-Leu-Leu-leucinal (MG132) or lactacystin (LC) did not enhance the levels of

225 sted at metaphase by a proteasome inhibitor, MG132, or by Cdc20 depletion.

226 tment of cells with the proteasome inhibitor MG132, or the IkappaB kinase inhibitor Bay 11-7085 befor

227 , which was further increased by exposure to MG132, or upon transfection with a dorfin dominant negat

228 es c-Jun protein, which was also restored by MG132 pre-exposure.

229 pathway by the chemical proteasome inhibitor MG132 prevented HIF-1alpha degradation in the presence o

230 nhibitor UBEI-41 or the proteasome inhibitor MG132 prevented IRF5 degradation, supporting the idea th

231 ethylisothiourea or the proteasome inhibitor MG132 prevented LPS-induced LKB1 degradation and improve

232 pretreatment with the proteasomal inhibitor MG132 prevented the degradation of the keratin IF networ

233 MG132 prevented the IFN-gamma-induced increase in caspas

234 The proteasome inhibitor MG132 prevents DNMT1 degradation and reduces hypomethyla

235 Application of the proteasome inhibitor, MG132, prevents blue-light-dependent degradation of HRT,

236 ZR75-1 cells inhibited apoptosis induced by MG132 proteasome inhibitor.

237 eated with 1 ng TGF-beta(2), with or without MG132 (proteasome inhibitor) or GM 6001 (MMP inhibitor).

238 h combinations of 100 U/mL IFN-gamma, 10 muM MG132 (proteasome inhibitor), and 100 muM quercetin (HSP

239 The proteasome inhibitor MG132 reduced CPT-induced Tra2 degradation and TAF1 alte

240 LLN, 2 micromol/L lactacystin, or 100 nmol/L MG132) reduced the BMK1-mediated effect on HIF1alpha exp

241 not treatment with the proteasome inhibitor MG132, reduced BST-2 downregulation by wild-type Vpu, th

242 oN degradation with the proteasome inhibitor MG132 reproduced the inhibitory action of BMP-7 on Smad3

243 However, the proteasome inhibitor MG132 rescued DeltaSIV INa, suggesting that the SIV moti

244 t of the cells with the proteasome inhibitor MG132 restored KPNA1 levels.

245 nfected leaves with the proteasome inhibitor MG132 resulted in higher GRIK1 and GRIK2 protein levels,

246 blastoma cells with the proteasome inhibitor MG132 resulted in reduced accumulation of SERCA levels c

247 Prolonged incubation with MG132 resulted in the increased expression of heat shock

248 ith nonboronated proteasome inhibitors (i.e. MG132) revealed a specificity of Tiron for bortezomib.

249 Proteosomal inhibition by MG132 reversed antisense-mediated decrease of S6K1 and 4

250 The proteasome inhibitor MG132 reversed caspase-2 down-regulation by rottlerin, w

251 Proteasome inhibitor MG132 reversed the effects of GSK3 inhibition and increa

252 or-related apoptosis-inducing ligand boosted MG132's proapoptotic activity through strengthening the

253 Elevated pressure also increased MG132-sensitive expression of IL-6 mRNA by microglia.

254 ive to MG132 in astrocytes, but were largely MG132-sensitive in microglia.

255 Bim degradation by the proteasome inhibitor MG132 sensitized resistant OV433 cells to cisplatin-indu

256 The proteasome inhibitors epoxomicin and MG132 significantly abrogated degradation of NS5A protei

257 The proteasome inhibitor MG132 significantly decreased oxyradicals, cytokine leve

258 xposure to the proteosome/lysosome inhibitor MG132, significantly reduced gemcitabine-induced cell de

259 protein, whereas proteasome inhibition with MG132 stabilized and maintained its DNA-binding function

260 n the 26S proteosome as a protease inhibitor MG132 stabilizes SNC1 and reverses the effect of CPR1 on

261 an be stabilized by the proteasome inhibitor MG132, suggesting that MKP1 is constitutively degraded t

262 insensitivity of gain-of-function mutants to MG132 suggests that receptor sensitivity to calcium infl

263 h N-benzoyloxycarbonyl (Z)-Leu-Leu-leucinal (MG132) suppresses CYP3A4 protein levels.

264 A proteasome inhibitor, MG132, suppresses secretion of AQP-1, implying that ubiq

265 This suggests that MG132 systemically perturbs the intracellular phosphopro

266 ying the time of the removal and addition of MG132, the adverse effect of the proteasome inhibitors w

267 dly, and degradation of IRF-8 was blocked by MG132, the proteasome inhibitor, but inhibitors of calpa

268 In the presence of the proteasome inhibitor MG132, TNF increased accumulation of ubiquitinated Smad1

269 l cells were incubated with leptomycin b and MG132 to block nuclear export and proteasome activity, r

270 Treatment with the proteasome inhibitor MG132 to prevent NF-kappaB activation dramatically reduc

271 hed an increase in ubiquitinated proteins in MG132-treated astrocytes.

272 normal levels of E1beta could be detected in MG132-treated cells.

273 ity of CRAG knockdown in polyQ-expressing or MG132-treated cells.

274 d by confocal immunofluorescence analyses of MG132-treated hepatocytes.

275 ggregates, and apoptotic cell death, whereas MG132-treated quiescent cells displayed fewer juxtanucle

276 g proteasome protein subunits in response to MG132 treatment and an increase in proteasome activity.

277 expression of G50C and G50A was rescued upon MG132 treatment as well as cyclosporine A, but not by FK

278 MG132 treatment did not result in ubiquitination or accu

279 MG132 treatment greatly reduced radiation-induced apopto

280 We also found that MG132 treatment had a broad affect on the NF-kappaB path

281 Moreover, MG132 treatment of proliferating fibroblasts led to incr

282 Here, we show that the effects of MG132 treatment on ERK signaling are more widespread, le

283 It has been proposed that MG132 treatment reduces growth factor-stimulated phospho

284 ked Ub polymers increased substantially upon MG132 treatment, revealing that they might be important

285 nd that this increase was more evident after MG132 treatment.

286 Proteasome inhibitor (MG132) treatment strongly inhibited the proliferation of

287 In the presence of the proteasome inhibitor MG132, virion-associated Vif increased dramatically.

288 sulted in disappearance of c-Fos protein and MG132 was able to prevent this loss.

289 This activity of Z-L3VS or MG132 was found to correlate with inhibition of intracel

290 Regulation of SRF by MG132 was not related to inhibition of nuclear factor-ka

291 Downregulation of alphaA-crystallin by MG132 was observed at both the mRNA and protein levels.

292 Previously, the proteasome inhibitor MG132 was reported to increase HIV infection-here we inv

293 The antiproliferative effect of MG132 was significantly reversed in samples transfected

294 rnover is blocked by treatment of cells with MG132, we provide evidence that such turnover is mediate

295 r N-benzoyloxycarbonyl (Z)-Leu-Leu-leucinal (MG132), whereas lysosome inhibitor chloroquine was witho

296 ened sensitivity to the proteasome inhibitor MG132, which induced p27(kip1) expression.

297 Treatment with the proteasome inhibitor MG132, which stabilizes repeats, confirms proteasome inv

298 After MG132 withdrawal, wild-type HPK1 protein expression was

299 rom the toxicity of the proteasome inhibitor MG132 without eliciting any increase in glutathione.

300 tion of proteasome-mediated degradation with MG132 yielded additional, but nonfunctional protein.