ライフサイエンスコーパス: MG132

1 upon chemical inhibition of the proteasome (MG132).

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

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

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

5 mostly reversed by the proteasomal inhibitor MG132.

6 by either polyQ or the proteasome inhibitor MG132.

7 rom degradation by the proteasome inhibitor, MG132.

8 hich was blocked by the proteasome inhibitor MG132.

9 tion was blocked by the proteasome inhibitor MG132.

10 as able to counter the inhibitory effects of MG132.

11 pre-treatment with the proteasome inhibitor MG132.

12 was stabilized by the proteasomal inhibitor MG132.

13 re all abolished by the proteasome inhibitor MG132.

14 olide, as well as proteasome inhibition with MG132.

15 c stress induced by the proteasome inhibitor MG132.

16 plants treated with the proteasome inhibitor MG132.

17 tion CaR mutants to proteasome inhibition by MG132.

18 ith the presence of the proteasome inhibitor MG132.

19 fragments) were stabilized by the action of MG132.

20 ent or treated with the proteasome inhibitor MG132.

21 in the presence of the proteasome inhibitor, MG132.

22 crosomal pellet) isolated in the presence of MG132.

23 as not inhibited by the proteasome inhibitor MG132.

24 y pretreatment with the proteosome inhibitor MG132.

25 ed fibroblasts with the proteasome inhibitor MG132.

26 ors lactacystin, proteasome inhibitor 1, and MG132.

27 y NFkappaB translocation and is sensitive to MG132.

28 ing treatment with the proteasome inhibitor, MG132.

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

30 s and stabilized by the proteasome inhibitor MG132.

31 in the presence of the proteasomal inhibitor MG132.

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

33 AAG is inhibited by the proteasome inhibitor MG132.

34 al control levels, even after treatment with MG132.

35 ith the proteasome inhibitors bortezomib and MG132.

36 by treating cells with proteasome inhibitor MG132.

37 in the presence of 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 n effect blocked by the proteasome inhibitor MG132.

43 y increased by UPS inhibitors bortezomib and MG132.

44 reversed utilizing the proteasome inhibitor MG132.

45 on was magnified by the proteasome inhibitor MG132.

46 in the presence of the proteasome inhibitor, MG132.

47 ich were rescued by the proteasome inhibitor MG132.

48 n the stationary phase of cells treated with MG132.

49 ich is prevented by the proteasome inhibitor MG132.

50 by application of the proteasome inhibitor, MG132.

51 d in the presence of the proteasome inhbitor MG132.

52 ich was prevented by a proteasome inhibitor, MG132.

53 on was inhibited by the proteasome inhibitor MG132.

54 ed through inhibition of the proteasome with MG132.

55 n be neutralized by the proteasome inhibitor MG132.

56 urvival action, may antagonize the action of MG132.

57 in the presence of the proteasome inhibitor MG132.

58 eriments using proteasome inhibitors such as MG132.

59 V1 was abrogated by the proteasome inhibitor MG132.

60 by treatment with the proteasome inhibitor, MG132.

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

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

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

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

65 80 (a specific inhibitor of p38 MAPK) and by MG132 (a specific inhibitor of NF-kappaB).

66 MG132, a peptide aldehyde that competitively inhibits th

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

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

69 MG132, a potent proteasome inhibitor and activator of RO

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

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

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

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

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

75 This decrease was inhibited by 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 K3 null MEFs is stabilized by treatment with MG132, a proteosome inhibitor.

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

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

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

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

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

84 eedlings exposed to the proteasome inhibitor MG132 accumulated assembly intermediates, reflecting par

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 n the presence of the proteasomal inhibitors MG132 and ALLN rather than the lysosomal inhibitors leup

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 bsence of LNPs as well as in the presence of MG132 and concanamycin A.

106 MG132 and DHB significantly blocked the MeHg-induced dec

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

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

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

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

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

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

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

114 MG132 and lactacystin, inhibitors of the ubiquitin-prote

115 d by treatment with the proteasome inhibitor MG132 and lactacystin.

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

117 Proteosome inhibitor MG132 and lentiviruses enabling inducible expression or

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

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

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

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

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

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

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

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

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

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

128 cells treated with the proteasome inhibitor MG132, and we further explore genome-wide effects of pro

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

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

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

132 rbates the occurrence of cohesion fatigue in MG132-arrested cells.

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

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

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

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

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

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

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

140 ificantly suppressed by proteasome inhibitor MG132/bortezomib at mRNA and protein levels in lung canc

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

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

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

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

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

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

147 MG132 caused a significant increase in p21 and p27 prote

148 MG132 caused no significant change in heat shock factor

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

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

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

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

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

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

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

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

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

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

159 f polyubiquitination in proteasome-inhibited MG132 controls.

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

161 nd increase the stability of ORE1 in vivo in MG132/cycloheximide-chase experiments.

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

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

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

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

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

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

168 MG132 effectively blocked degradation of both pp27Thr187

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

170 MG132 elicited a robust increase in the folding chaperon

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

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

173 Further investigation revealed that MG132 facilitated polyubiquitinated AGR2 degradation thr

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

203 MG132-mediated repression of AGR2 transcription was inde

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

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

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

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

208 8 activities and the antiapoptotic effect of MG132 on IFN-gamma-treated LECs.

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 Treatment of either a proteasome inhibitor MG132 or bortezomib, or with a p-ERK/MEK inhibitor U0126

214 yubiquitinated AGR2 clearance in response to MG132 or bortezomib.

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

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

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

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

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

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

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

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

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

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

225 hesis inhibitor (CHX), proteasome inhibitor (MG132), or proline hydroxylase inhibitor (DHB) were appl

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

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

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

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

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

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

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

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

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

235 omycin A1, but not the proteasomal inhibitor MG132, prevented the FAC-mediated decrease in TfR1 prote

236 The proteasome inhibitor MG132 prevents DNMT1 degradation and reduces hypomethyla

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

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

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

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

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

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

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

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

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

246 A proteasome inhibitor MG132 rescues PPM1A and PTEN expression, even in the pre

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

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

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

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

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

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

253 eatment of EMD with the proteasome inhibitor MG132 reversed its c-Myc-targeting effect, suggesting th

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

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

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

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

258 This binding induced MG132-sensitive reduction of AIF expression in the prese

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

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

261 The proteasome inhibitor MG132 significantly decreased oxyradicals, cytokine leve

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

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

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

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

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

267 ter application of 26S proteasomal inhibitor MG132, suggests that phosphorylation is essential to pro

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

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

270 This suggests that MG132 systemically perturbs the intracellular phosphopro

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

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

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

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

275 oprecipitation assay only in the presence of MG132 to prevent RLIM degradation.

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

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

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

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

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

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

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

283 MG132 treatment greatly reduced radiation-induced apopto

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

285 Moreover, MG132 treatment of proliferating fibroblasts led to incr

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

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

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

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

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

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

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

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

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

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

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

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.