ライフサイエンスコーパス: heat-shock protein 90

1 nd absence of functional molecular chaperone heat shock protein 90.

2 LAQ824 also induced acetylation of heat shock protein 90.

3 e rate is further accelerated on addition of heat shock protein 90.

4 a drug that blocks the chaperone activity of heat-shock protein 90.

5 y to gamma-enolase (8%); alpha-enolase (9%); heat-shock protein 90 (13%); osteopontin (4%); ubiquitin

6 /Zn-superoxide dismutase (SOD) but increased heat shock protein-90, a chaperone that facilitates prot

7 Heat shock protein 90 alpha (Hsp90 alpha)/p23 and Hsp90

8 Heat shock protein 90 alpha (Hsp90alpha) was immobilized

9 orms part of a protein complex that includes heat shock protein 90-alpha (HSP90-alpha), a molecular c

10 geldanamycin, an inhibitor of the chaperone heat shock protein 90, also increased both wild-type and

11 tigation revealed that SHP-2 interacted with heat shock protein 90, an important chaperone protein pr

12 ase 5 (PP5) has been found in complexes with heat shock protein 90 and glucocorticoid receptors and m

13 sing specific inhibitors revealed a role for heat shock protein 90 and glycogen synthase kinase 3 but

14 Emodin decreased the association of AR and heat shock protein 90 and increased the association of A

15 R-499 cardiomyopathy phenotype, including of heat shock protein 90 and protein serine/threonine phosp

16 90, which disrupted the interaction between heat shock protein 90 and TAp73 and thus promoted the pr

17 y, this conformational change was opposed by heat-shock protein 90 and did not require the MDM2 RING-

18 s a conformational change that is opposed by heat-shock protein 90 and precedes p53 ubiquitination.

19 The ATPase-driven dimeric molecular Hsp90 (heat shock protein 90) and its cofactor Cdc37 (cell divi

20 ajor tegument protein, and cofilin, tubulin, heat shock protein 90, and heat shock protein 70 were su

21 n combination with cytotoxics, inhibitors of heat shock protein 90, and inhibitors of proteasome func

22 protein inhibitor of NOS1 (PIN), calmodulin, heat shock protein 90, and NOS interacting protein.

23 kinase A, epidermal growth factor receptor, heat shock protein 90, and platelet-derived growth facto

24 Therefore, mitochondrial heat shock protein 90s are adaptive regulators of tumor

25 ls was prevented by geldanamycin, suggesting heat shock protein 90 as a binding partner.

26 A pull-down assay identified GAPDH and heat-shock protein 90 as potential substrates for SerB65

27 face expression of heat shock protein 60 and heat shock protein 90, as well as improve DC function, w

28 s known to inhibit the chaperone function of heat shock protein 90, as well as induce growth arrest a

29 perone complex with mutant GCase and reduced heat-shock protein 90-associated protein degradation.

30 Heat shock protein 90 beta (Hsp90 beta) is involved in m

31 those, we chose to focus on an inhibitor of heat shock protein 90 beta (HSP90beta).

32 ly revealed that the intracellular chaperone heat-shock protein 90 beta (HSP90beta) is present extrac

33 nts specifically reacted with the sumoylated heat-shock protein 90 beta isoform-alpha (HSP90-SUMO1, w

34 Here we show that the chaperone protein heat shock protein 90 beta1 (hsp90beta1) is required for

35 ial heat shock protein 90, but not cytosolic heat shock protein 90, binds and stabilizes the electron

36 33) pool formation required active cytosolic heat-shock protein 90 but not ER g96 and uniquely enable

37 Specifically, mitochondrial heat shock protein 90, but not cytosolic heat shock prot

38 shock protein 40, heat shock protein 70, and heat shock protein 90 by enzyme-linked immunosorbent ass

39 gulation of TAp73 protein stability by HDAC1-heat shock protein 90 chaperone complex, and our data su

40 ted by 17-beta-estradiol and interact within heat shock protein 90 chaperone complexes, together with

41 o reconstitution system whereby the cellular heat shock protein 90 chaperone system activates recombi

42 The heat shock protein 90 chaperone was nitrated in both tro

43 ng and that SNCG can replace the function of heat shock protein 90, chaperone ER-alpha36 activity, st

44 tudies suggest that EphA2 represents a novel heat shock protein 90 client protein and that the treatm

45 directly interacts with PIH1D1, a subunit of heat-shock protein 90 cochaperone R2TP complex, which is

46 Here we report that heat shock protein 90-directed protein folding in mitoch

47 Thus, heat shock protein 90-directed proteostasis in mitochond

48 Here, we show that heat-shock-protein-90-directed protein folding in mitoch

49 ch specifically inhibits the function of the heat shock protein 90 family.

50 Modulation of Hsp90 (heat shock protein 90) function has been recognized as a

51 We found that heat shock protein 90, glutathione S-transferase (GST),

52 oximately 30%, but addition of siRNA(Hsp90) (heat shock protein 90) had little effect.

53 thioredoxin 1), increased the expression of heat shock protein 90, heat shock protein 70, Bcl-2, Bcl

54 f RanBP9 to physically interact with tau and heat shock protein 90/heat shock cognate 70 (Hsp90/Hsc70

55 ed that small-molecule inhibitors, including heat-shock protein 90, histone deacetylase, PI3K/AKT, an

56 (17-AAG) inhibits the chaperone function of heat shock protein-90 (Hsp-90) and promotes the proteaso

57 ity of the auxin co-receptor TIR1, involving HEAT SHOCK PROTEIN 90 (HSP90) [9].

58 FKBP51 (the 51-kDa FKBP) associates with heat shock protein 90 (Hsp90) and appears in functionall

59 acts by modulating the chaperone activity of heat shock protein 90 (Hsp90) and blocking the binding o

60 was dependent on the chaperoning function of heat shock protein 90 (HSP90) and co-accompanied by the

61 By interacting with the TPR domain, heat shock protein 90 (Hsp90) and fatty acids including

62 This interaction was stabilized by heat shock protein 90 (HSP90) and followed by proteasoma

63 The chaperones heat shock protein 90 (HSP90) and heat shock cognate pro

64 Chemical proteomics showed that heat shock protein 90 (HSP90) and heterogeneous nuclear

65 otein via augmenting the interaction between heat shock protein 90 (Hsp90) and HIF-1alpha protein.

66 5C) is known to interact with the chaperonin heat shock protein 90 (HSP90) and is involved in the reg

67 (EC144), is a second generation inhibitor of heat shock protein 90 (Hsp90) and is substantially more

68 The molecular chaperone heat shock protein 90 (Hsp90) and its accessory cochaper

69 assistance of a host cell chaperone complex, heat shock protein 90 (Hsp90) and its co-chaperones, whi

70 lysosomal membrane, where it interacts with heat shock protein 90 (HSP90) and stabilizes binding of

71 s from inhibition of the molecular chaperone heat shock protein 90 (HSP90) and subsequent degradation

72 Disassociation between Kit and heat shock protein 90 (HSP90) and up-regulation of HSP70

73 with molecular targeted agents that inhibit heat shock protein 90 (Hsp90) and/or mammalian target of

74 se C (PKC) and Chk1 inhibitor UCN-01 and the heat shock protein 90 (Hsp90) antagonist 17-AAG have bee

75 tibodies targeting citrullinated isoforms of heat shock protein 90 (HSP90) are associated with rheuma

76 Inhibitors of the molecular chaperone heat shock protein 90 (Hsp90) are currently generating s

77 This screen identified heat shock protein 90 (HSP90) as a new binding partner o

78 The potential of heat shock protein 90 (Hsp90) as a therapeutic target fo

79 e identified previously topoisomerase II and heat shock protein 90 (Hsp90) as part of a complex.

80 Previous reports suggest heat shock protein 90 (hsp90) associates with endothelia

81 The chaperone heat shock protein 90 (hsp90) associates with signaling

82 Heat shock protein 90 (HSP90) binds directly to eNOS, au

83 quinoid ansamycin antibiotic, which binds to heat shock protein 90 (hsp90) causes destabilization of

84 ves correlated with increased binding to the heat shock protein 90 (HSP90) chaperone and with higher

85 n Cullin5 (Cul5) E3 ubiquitin ligase and the heat shock protein 90 (Hsp90) chaperone complex.

86 We found that the heat shock protein 90 (Hsp90) chaperone system of the ye

87 We have investigated mechanisms involved in heat shock protein 90 (Hsp90) chaperone-mediated cross p

88 is regulated via direct association with the heat shock protein 90 (HSP90) chaperone.

89 tein kinases are the most prominent group of heat shock protein 90 (Hsp90) clients and are recruited

90 of CK2 and EGFR also caused deactivation of heat shock protein 90 (Hsp90) co-chaperone Cdc37, which

91 In this report we show that the heat shock protein 90 (HSP90) co-chaperones p23 and FKBP

92 l division cycle 37 homolog (Cdc37) is a key heat shock protein 90 (Hsp90) cochaperone for protein ki

93 p23 is a heat shock protein 90 (Hsp90) cochaperone located in bot

94 Histone deacetylase 6 (HDAC6) is a heat shock protein 90 (hsp90) deacetylase.

95 Heat shock protein 90 (hsp90) drives heme insertion into

96 The molecular chaperone and heat shock protein 90 (Hsp90) exists mainly as a homodim

97 The heat shock protein 90 (Hsp90) family of heat shock prote

98 The heat shock protein 90 (Hsp90) family of molecular chaper

99 ecular chaperones, especially members of the heat shock protein 90 (Hsp90) family, are thought to pro

100 Akt phosphorylation via the dissociation of heat shock protein 90 (Hsp90) from its client protein 3-

101 of cells with geldanamycin, an inhibitor of heat shock protein 90 (Hsp90) function, also resulted in

102 ave demonstrated here that the inhibition of heat shock protein 90 (Hsp90) functions by small interfe

103 to determine whether the molecular chaperone heat shock protein 90 (HSP90) has an effect on both reco

104 The molecular chaperone heat shock protein 90 (HSP90) has emerged as an exciting

105 We demonstrate here a novel role of heat shock protein 90 (Hsp90) in control of the INrf2 an

106 We investigated a role for chaperone heat shock protein 90 (hsp90) in enabling heme insertion

107 Nitration of the pro-survival chaperone heat shock protein 90 (Hsp90) in position 33 and 56 indu

108 To explore the role of heat shock protein 90 (HSP90) in regulation of TSSKs, th

109 AhR is usually associated with heat shock protein 90 (Hsp90) in the cytoplasm.

110 estigated the role of the cellular chaperone heat shock protein 90 (Hsp90) in viral RNA replication c

111 Here we show that LRRK2 forms a complex with heat shock protein 90 (Hsp90) in vivo and that inhibitio

112 eins to characterize the mechanisms by which heat shock protein 90 (HSP90) increases eNOS activity at

113 We found that inhibitors of heat shock protein 90 (HSP90) induced apoptosis in BL ce

114 Heat shock protein 90 (Hsp90) inhibition by modulation o

115 Heat shock protein 90 (HSP90) inhibition inhibits cancer

116 Heat shock protein 90 (HSP90) inhibition is an attractiv

117 Here, we demonstrate that heat shock protein 90 (HSP90) inhibition using a purine-

118 We examined whether the heat shock protein 90 (HSP90) inhibitor 17-(dimethylamin

119 FDG PET for imaging of tumor response to the heat shock protein 90 (Hsp90) inhibitor 17-allylamino-17

120 Chk1 is depleted when cells are treated with heat shock protein 90 (Hsp90) inhibitor 17-allylamino-17

121 We found that the heat shock protein 90 (Hsp90) inhibitor ganetespib induc

122 Combination therapy with the heat shock protein 90 (HSP90) inhibitor PU-H71 and ruxol

123 trate that these tumors are sensitive to the heat shock protein 90 (Hsp90) inhibitor PU-H71.

124 n novologue (a novobiocin-based, C-terminal, heat shock protein 90 (Hsp90) inhibitor) that decreases

125 to kinase inhibition, an orally administered heat shock protein 90 (Hsp90) inhibitor, IPI-504, was ev

126 AUY922, a novel resorcinylic isoxazole amide heat shock protein 90 (HSP90) inhibitor.

127 The discovery and clinical development of heat shock protein 90 (Hsp90) inhibitors continue to pro

128 We reasoned that newer heat shock protein 90 (HSP90) inhibitors could overcome

129 We report that heat shock protein 90 (Hsp90) inhibitors selectively kil

130 hat the combination of glutaminase (GLS) and heat shock protein 90 (Hsp90) inhibitors selectively tri

131 A novel class of heat shock protein 90 (Hsp90) inhibitors was developed f

132 srupting client-chaperone interactions using heat shock protein 90 (Hsp90) inhibitors would result in

133 Heat shock protein 90 (HSP90) inhibitors, such as 17-all

134 Several hit structures were identified as heat shock protein 90 (Hsp90) inhibitors.

135 used to determine effects of LDL and L-4F on heat shock protein 90 (hsp90) interactions with eNOS.

136 In this study, we show that heat shock protein 90 (Hsp90) interacts directly with ea

137 Heat shock protein 90 (Hsp90) is a conserved and ubiquit

138 The heat shock protein 90 (Hsp90) is a dimeric molecular cha

139 Heat shock protein 90 (Hsp90) is a molecular chaperone e

140 Heat shock protein 90 (Hsp90) is a molecular chaperone i

141 Heat shock protein 90 (Hsp90) is a molecular chaperone p

142 Heat shock protein 90 (Hsp90) is a molecular chaperone r

143 Heat shock protein 90 (Hsp90) is a molecular chaperone t

144 Heat shock protein 90 (Hsp90) is a molecular chaperone t

145 Heat shock protein 90 (HSP90) is a molecular chaperone t

146 Heat shock protein 90 (Hsp90) is a molecular chaperone t

147 Heat shock protein 90 (Hsp90) is a molecular chaperone t

148 Heat shock protein 90 (HSP90) is a molecular chaperone t

149 Heat shock protein 90 (Hsp90) is a molecular chaperone t

150 Heat shock protein 90 (Hsp90) is an ATP-dependent molecu

151 Heat shock protein 90 (Hsp90) is an attractive cancer ta

152 Heat shock protein 90 (Hsp90) is an emerging target for

153 Heat shock protein 90 (Hsp90) is an emerging therapeutic

154 In eukaryotes, heat shock protein 90 (Hsp90) is an essential ATP-depend

155 Heat shock protein 90 (Hsp90) is an essential chaperone

156 Heat shock protein 90 (Hsp90) is an essential eukaryotic

157 Heat shock protein 90 (Hsp90) is an essential molecular

158 The molecular chaperone heat shock protein 90 (Hsp90) is an essential protein re

159 Heat shock protein 90 (Hsp90) is critical for the matura

160 Heat shock protein 90 (Hsp90) is essential for activatio

161 The molecular chaperone heat shock protein 90 (Hsp90) is involved in multiple ce

162 g tumorigenesis, the chaperoning activity of heat shock protein 90 (HSP90) is often exploited by canc

163 The molecular chaperone heat shock protein 90 (Hsp90) is overexpressed during he

164 We have previously shown that the heat shock protein 90 (Hsp90) is required for HIV-1 gene

165 The molecular chaperone heat shock protein 90 (HSP90) is required for the activi

166 The molecular chaperone heat shock protein 90 (Hsp90) is required for the foldin

167 The molecular chaperone heat shock protein 90 (Hsp90) is required for the stabil

168 s mediated by bortezomib-induced exposure of heat shock protein 90 (hsp90) on the surface of dying ce

169 We provide evidence that heat shock protein 90 (HSP90) phenotypically masks stand

170 Heat shock protein 90 (Hsp90) plays a central role in si

171 From yeast to vertebrates, heat shock protein 90 (HSP90) plays a unique role among

172 Heat shock protein 90 (Hsp90) protects cellular proteins

173 Heat shock protein 90 (HSP90) protects KIT oncoproteins

174 In eukaryotes, heat shock protein 90 (Hsp90) proteins are essential ATP

175 Acetylation of heat shock protein 90 (Hsp90) regulates downstream hormo

176 Previous studies suggest that heat shock protein 90 (Hsp90) regulates the stability an

177 Heat shock protein 90 (Hsp90) represents a promising the

178 The molecular chaperone heat shock protein 90 (Hsp90) serves essential roles in

179 sis from iNOS can be profoundly modulated by heat shock protein 90 (hsp90) through protein-protein in

180 ures of cyclin dependent kinase 2 (CDK2) and heat shock protein 90 (HSP90) to assess the performance

181 NMNAT2 complexes with heat shock protein 90 (HSP90) to refold aggregated prote

182 Recently the molecular chaperone heat shock protein 90 (Hsp90) was implicated as a major

183 (SF3B2 and ataxin-2) of a chaperone protein, heat shock protein 90 (Hsp90) when co-administered with

184 7-AAG) inhibits the chaperone association of heat shock protein 90 (hsp90) with the heat shock factor

185 Accordingly, levels of heat shock protein 90 (HSP90), a known ErbB2 protein sta

186 Na(+) and/or K(+) flux and the activation of heat shock protein 90 (HSP90), a protein required for th

187 recently shown that PPARalpha interacts with heat shock protein 90 (Hsp90), although the biological c

188 lls: telomerase-associated protein 1 (TEP1), heat shock protein 90 (HSP90), and topoisomerase IIalpha

189 ane potential, did not require the chaperone Heat Shock Protein 90 (Hsp90), and was inhibited by cyto

190 In search for an HDAC6 target, we found that heat shock protein 90 (Hsp90), another prominent substra

191 Here, we demonstrate that heat shock protein 90 (Hsp90), heat shock protein 70 (Hs

192 that could regulate the GR chaperone protein heat shock protein 90 (HSP90), in the synaptic action of

193 uces acetylation of histone H3 and H4 and of heat shock protein 90 (hsp90), increases p21 levels, as

194 tics, such as geldanamycin, potently inhibit heat shock protein 90 (Hsp90), promoting ubiquitin-media

195 ted protein 94 (Grp94), the ER equivalent of heat shock protein 90 (Hsp90), specifically recognizes m

196 nt phenethyl isothiocyanate (PEITC) inhibits heat shock protein 90 (Hsp90), the main negative regulat

197 Because eEF-2 kinase is chaperoned by heat shock protein 90 (Hsp90), we next determined if dis

198 82 colocalized and coimmunoprecipitated with heat shock protein 90 (HSP90), which increased upon alco

199 that RIP1 formed a complex with Triad3A and heat shock protein 90 (Hsp90), which is a chaperone prot

200 is required for the association of Ago2 with heat shock protein 90 (Hsp90), which is necessary for th

201 The chaperone HEAT SHOCK PROTEIN 90 (HSP90), which maintains phenotypi

202 Here, we report that heat shock protein 90 (Hsp90), which plays a critical ro

203 ivity of these inhibitors was tested against heat shock protein 90 (HSP90), which possesses a similar

204 ity of JAK2-dependent cells to inhibitors of heat shock protein 90 (HSP90), which promote the degrada

205 Heat shock protein 90 (HSP90), which regulates the funct

206 C-1-interacting proteins that are well-known heat shock protein 90 (Hsp90)-associated co-chaperones:

207 d inactivation of nNOS and the inhibition of heat shock protein 90 (hsp90)-based chaperones, which ar

208 ts binding to the N-terminal fragment of the heat shock protein 90 (Hsp90).

209 eutic agents predicated on the inhibition of heat shock protein 90 (Hsp90).

210 showed that WT1 is a novel client protein of heat shock protein 90 (Hsp90).

211 by inhibition of the HDAC6-regulated protein heat shock protein 90 (HSP90).

212 bilized when it associates with the cellular heat shock protein 90 (Hsp90).

213 ession, with concomitant hyperacetylation of heat shock protein 90 (hsp90).

214 d to a common site on the cellular chaperone heat shock protein 90 (Hsp90).

215 requires the interaction of the LBD with the heat shock protein 90 (Hsp90).

216 ddition, RUNX1-ETO physically interacts with heat shock protein 90 (HSP90).

217 /Akt, mitogen-activated protein kinases, and heat shock protein 90 (HSP90).

218 require the molecular chaperone complex, the heat shock protein 90 (Hsp90).

219 by association with the molecular chaperone heat shock protein 90 (Hsp90).

220 ctrometry revealed that GRK2 associates with heat shock protein 90 (Hsp90).

221 lic androgen receptor (AR) chaperone protein heat shock protein 90 (HSP90).

222 ed by rapid HDAC6-dependent deacetylation of heat shock protein 90 (HSP90).

223 protein 39 (WISp39) as a binding partner for heat shock protein 90 (Hsp90).

224 s depends on the dimeric molecular chaperone heat shock protein 90 (Hsp90).

225 ugh network construction, to be regulated by heat shock protein 90 (HSP90).

226 e, we have shown that selective targeting of heat shock protein-90 (Hsp90) chaperones in mitochondria

227 The identification of heat shock protein-90 (Hsp90) chaperones in mitochondria

228 Molecular chaperones of the heat shock protein-90 (Hsp90) family promote cell surviv

229 Both intracellular and extracellular heat shock protein-90 (Hsp90) family proteins (alpha and

230 ugh interference of cyclophilin-D binding to heat shock protein-90 (Hsp90) in mitochondria, rendering

231 Heat shock protein-90 (Hsp90) is an essential molecular

232 al proteins, such as the molecular chaperone heat shock protein-90 (Hsp90), in promoting cancer cell

233 onverted to kallikrein because of release of heat shock protein-90 (Hsp90).

234 othelium, potentially due to dissociation of heat shock proteins 90 (Hsp90), and cellular glucose hom

235 els of residual Activin-like activity and by Heat-Shock Protein 90 (HSP90) activity.

236 The heat-shock protein 90 (HSP90) acts as a chaperone by ens

237 Heat-shock protein 90 (Hsp90) acts as a molecular chaper

238 p-regulation of the folding machinery of the heat-shock protein 90 (Hsp90) chaperone protein is cruci

239 Heat-shock protein 90 (Hsp90) chaperones a key subset of

240 Here we investigated the role of cellular heat-shock protein 90 (HSP90) in AAV transduction becaus

241 Although STAT3 coprecipitated with heat-shock protein 90 (Hsp90) in control cells, coprecip

242 o address this need, we explored the role of heat-shock protein 90 (Hsp90) in opioid-induced MOR sign

243 Inhibition of the chaperone heat-shock protein 90 (HSP90) induces apoptosis, and it

244 Blocking heat-shock protein 90 (Hsp90) induces death of malignant

245 We present here that heat-shock protein 90 (Hsp90) inhibitor 17-(allylamino)-

246 We demonstrate that the heat-shock protein 90 (HSP90) inhibitor 17-allylamino-17

247 In this study we examined the effect of heat-shock protein 90 (HSP90) inhibitor, geldanamycin (G

248 ylamino]-17-demethoxygeldanamycin (17AAG), a heat-shock protein 90 (Hsp90) inhibitor, prevents UVR-in

249 Unlike most chaperones, heat-shock protein 90 (Hsp90) interacts with a select gr

250 The molecular chaperone heat-shock protein 90 (Hsp90) is an essential component

251 Heat-shock protein 90 (Hsp90) is an ubiquitous chaperone

252 Inhibition of heat-shock protein 90 (HSP90) leads to O(2)/PHD/VHL-inde

253 Heat-shock protein 90 (Hsp90) of Saccharomyces cerevisia

254 The molecular chaperone heat-shock protein 90 (HSP90) plays a key role in the ce

255 aperone UNC45B, in addition to the chaperone heat-shock protein 90 (HSP90) significantly increased th

256 Galpha12 mutants showed impaired binding to heat-shock protein 90 (Hsp90) while retaining binding to

257 d that ZAP-70+ CLL cells expressed activated heat-shock protein 90 (Hsp90) with high binding affinity

258 homeostasis, molecular chaperones, including heat-shock protein 90 (Hsp90), represent attractive drug

259 a novel, water-soluble, potent inhibitor of heat-shock protein 90 (Hsp90).

260 res formation of a complex between SGK-1 and heat-shock protein 90 (Hsp90).

261 buffer transformation has been attributed to heat-shock protein 90 (Hsp90).

262 rol interfered with the establishment of the heat-shock protein 90/Hsp90 cochaperone Cdc37/Hsp90-Hsp7

263 Chloroplast heat shock protein 90 (Hsp90C) represents a highly conse

264 e the role of the molecular chaperone hsp90 (heat shock protein 90) in excitatory synaptic transmissi

265 le, in response to replicative stress and on heat shock protein 90 inhibition, and that deregulation

266 V4-11 cells (containing a FLT-3 LM) with the heat shock protein 90 inhibitor 17-allylamino-demethoxy

267 HER2 protein on treatment of tumor mice with heat shock protein 90 inhibitor 17-N,N-dimethyl ethylene

268 ne, the JAK1/2 inhibitor ruxolitinib, or the heat shock protein 90 inhibitor 8-(6-iodobenzo[d][1.3]di

269 f EphA2(+) tumor cells with the irreversible heat shock protein 90 inhibitor, 17-dimethylaminoethylam

270 Inhibition of ErbB2 by either the HSP (heat shock protein) 90 inhibitor geldanamycin or the Erb

271 and pyridino- thiazolothiopurines as potent heat shock protein 90 inhibitors.

272 Several Hsp90 (heat shock protein 90) inhibitors are currently under cl

273 that the interactions of AID with eEF1A and heat-shock protein 90 kD (HSP90) are inversely correlate

274 is the endoplasmic reticulum resident of the heat shock protein 90 kDa (Hsp90) family of molecular ch

275 We identified the cellular heat shock protein 90 kDa alpha (cytosolic), class B mem

276 Next, we identified the heat-shock protein 90 kDa (HSP90) as the native antigen

277 doses (40 mg/kg) of 17-DMAG, an inhibitor of heat-shock protein 90, known to decrease HER2 expression

278 Addition of heat shock protein 90 leads to conversion of prekallikre

279 ck protein 70 were increased while placental heat shock protein 90 levels were decreased in hypoxic p

280 ancer cells is highly stabilized through the heat shock protein 90 machinery (HSP90).

281 processing mechanisms, as well as cytosolic heat shock protein 90-mediated chaperoning.

282 gly, alvespimycin, a potent inhibitor of the heat-shock protein 90 molecular chaperone, markedly inhi

283 Heat shock protein 90 (molecular weight, 90 kDa) (hsp90)

284 lity group box 1, heat shock protein 70, and heat shock protein 90; negatively regulates their stimul

285 aused NO-dependent dissociation of HSF1 from heat shock protein 90, nuclear translocation of HSF1, an

286 n 94 (GRP94/gp96), the endoplasmic reticulum heat shock protein 90 paralog, elicits both innate and a

287 The ERK/MEK signaling pathway, heat shock protein 90, PI3K, and an intact cytoskeleton

288 these inhibitors limit the deacetylation of heat shock protein 90, resulting in less recognition of

289 Interestingly, DARC- or heat shock protein 90 subunit alpha-deficient ASMCs resp

290 h, in turn, was dependent on the presence of heat shock protein 90 subunit alpha.

291 ed the chaperone association of Bcr-Abl with heat shock protein 90, thereby promoting the proteasomal

292 itro; and enhanced the binding of acetylated heat shock protein 90 to lymphocyte-specific protein tyr

293 c, 17AAG functions to modulate the action of heat shock protein 90, ultimately affecting a multitude

294 dehydrogenase, alpha-enolase, filamin-A, and heat shock protein 90, were identified in samples of api

295 (required for Mla12 resistance), and Hsp90 (heat shock protein 90), which are known to participate e

296 lted in hyperacetylation and inactivation of heat shock protein 90, which disrupted the interaction b

297 by inhibiting its chaperone association with heat shock protein 90, which induced the poly-ubiquityla

298 inase induces its complexing with 14-3-3 and heat shock protein 90, which is facilitated by the longe

299 Disruption of heat shock protein 90 with 17-AAG significantly reduced

300 and autolytimycin (2) were shown to bind the heat shock protein 90 with enhanced binding activity (ap