ライフサイエンスコーパス: chaperone protein

1 gand-mediated conformational changes of this chaperone protein.

2 ost DEAD box helicases and the viral p33 RNA chaperone protein.

3 at matches contemporary understanding of the chaperone protein.

4 identified BAG1, which encodes a prosurvival chaperone protein.

5 in a free (hydrated) form but is bound to a chaperone protein.

6 al to swo1(+) and encodes the S. pombe Hsp90 chaperone protein.

7 hway and support a role for torsinA as an ER chaperone protein.

8 ral potential binding targets for the La RNA chaperone protein.

9 volved through immune selection on the groEL chaperone protein.

10 n their fusion protein and membrane-anchored chaperone protein.

11 ised by an overexpression of contractile and chaperone proteins.

12 argeted for export with the help of specific chaperone proteins.

13 d to an increase in the expression of the ER chaperone proteins.

14 17p/Sec18p, the vacuolar tethering and SNARE chaperone proteins.

15 ion-independent manner by means of dedicated chaperone proteins.

16 ression responses involving cytoskeletal and chaperone proteins.

17 d-type plants, as is the accumulation of BiP chaperone proteins.

18 the heat shock protein 70 (Hsp70) family of chaperone proteins.

19 substrates of this class of protein-folding chaperone proteins.

20 ations (PTMs) and assisted by a number of co-chaperone proteins.

21 f neurodegenerative processes using modified chaperone proteins.

22 ulfide bonds, modulates redox responses, and chaperones proteins.

23 metrically with the hetero-octameric Tubulin Chaperone Protein-1 (TCP-1) complex, with the hetero-hex

24 rylation and enhanced complex formation with chaperone protein 14-3-3.

25 ing and facilitation of interaction with the chaperone protein 14-3-3zeta.

26 d the inability of S32T Prdx6 to bind to the chaperone protein, 14-3-3, that is required for LB targe

27 Here we identify the mitochondrial targeting chaperone protein, 14-3-3epsilon, as a RIG-I-binding par

28 of how mutant CALR, an endoplasmic reticulum chaperone protein, activates the JAK/STAT signaling path

29 vity can be improved by agents that increase chaperone protein activity.

30 chemical chaperones or overexpression of ER chaperone proteins alleviates hepatic steatosis.

31 The chaperone proteins, alpha-crystallins, also possess anti

32 st is regulated by the interaction between a chaperone protein and a heat shock transcription factor,

33 -length and p95-HER2 interact with the HSP90 chaperone protein and are degraded in tumor cells expose

34 The chaperone protein and guanine nucleotide exchange factor

35 C depends on its interaction with a cellular chaperone protein and in which cyclosporine inhibits HCV

36 This is a novel role for a cdc48-related chaperone protein and indicates that TgNoAP1 may be part

37 in, telatinib] bind selectively to the Hsp90 chaperone protein and inhibit its function.

38 Q/N-rich disordered domain, is modulated by chaperone proteins and leads to altered function of the

39 e ATP, which is tightly regulated both by co-chaperone proteins and post-translational modifications

40 ritic cells and elicit an immune response to chaperoned proteins and peptides.

41 Heat shock protein 27 (Hsp27) is a chaperone protein, and its expression is increased in re

42 Binding of sigmaR1 to BiP, an ER chaperone protein, and sigmaR1 phosphorylation status we

43 NK cells basally expressed the AHR, relevant chaperone proteins, and the AHR nuclear translocator, wh

44 volved in ameliorating the oxidative stress, chaperone proteins, anti-apoptotic factors, and DNA repa

45 Chaperone proteins are considered to be fairly ubiquitou

46 Emerging evidence strongly suggests that chaperone proteins are cytoprotective in neurodegenerati

47 Chaperone proteins are effective antitumor vaccines when

48 bon receptor-interacting protein (AIP), a co-chaperone protein, as required for response to DNMDP.

49 We conclude that histone chaperone protein Asf1 maintains a subset of replication

50 sis, folding, oligomerization, and turnover; chaperone proteins assist with all of these processes.

51 Clusterin is a chaperone protein associated with treatment resistance a

52 , a proteomics approach was used to identify chaperone proteins associated with K(ATP) channels.

53 Furthermore, several chaperone proteins associated with the responses to osmo

54 The co-chaperone protein, BAG3, which belongs to the BAG protei

55 refore constitute an improved formulation of chaperone protein-based tumor vaccine.

56 nd can direct the ubiquitination of the host chaperone protein BAT3.

57 e with cardiac-specific deficiency of the co-chaperone protein BCL2-associated athanogene 3 (BAG3) de

58 In cells, soluble chaperone proteins bind and distribute cytoplasmic Cu(+)

59 smic reticulum where it colocalized with the chaperone protein BIP and inhibited secretion of adipone

60 supraoptic nuclei revealed induction of the chaperone protein BiP and progressive loss of AVP-produc

61 B), which cleaves endoplasmic reticulum (ER) chaperone protein BiP, inducing ER stress and apoptotic

62 determining the expression levels of the ER chaperone protein BiP, the spliced form of X-box binding

63 cific site on the endoplasmic reticulum (ER) chaperone protein BiP/GRP78, leading to ER stress, and i

64 response to sleep deprivation involving the chaperone protein BiP/GRP78.

65 r response, which is mediated through the ER chaperone protein, BiP, three known ER transmembrane str

66 GRP94) is a major endoplasmic reticulum (ER) chaperone protein, but its in vivo function is still eme

67 LOX-PP interacted with the Hsp70 chaperoned protein c-Raf.

68 We have now identified the ER chaperone protein calnexin as an interacting protein for

69 L-6, could associate stably with ER-resident chaperone protein calnexin.

70 the interaction of hERG channels with the ER chaperone protein calnexin.

71 lular functions of the endoplasmic reticulum chaperone protein calreticulin (CRT) are emerging.

72 t demonstrate that the endoplasmic reticulum chaperone protein calumenin is associated with gamma-car

73 nd heat shock protein 90 (Hsp90), which is a chaperone protein capable of maintaining the stability o

74 de isomerase (PDI), an endoplasmic reticulum chaperone protein, catalyzes disulfide bond breakage, fo

75 2 (CCT2), a gene that encodes the molecular chaperone protein, CCTbeta.

76 led Gp53 was shown to interact with the AAA+ chaperone protein ClpC of the ClpCP protease of B. subti

77 toprotective intracellular and extracellular chaperone protein clusterin (CLU) interacts with MMP-9 b

78 empty MSP1D1 nanodisc and the tetradecameric chaperone protein complex GroEL) analyzed under native-M

79 wed as components of distinct oxidoreductase-chaperone protein complexes.

80 In this report, we show that cellular chaperone proteins, components of the 26S proteasome, an

81 Hsp90 encodes a ubiquitous molecular chaperone protein conserved among species which acts on

82 Cu chaperones, proteins containing a Cu-binding domain(s),

83 se that is known to ubiquitylate other hsp90-chaperoned proteins, could act as an ubiquitin ligase fo

84 ersistent posttranslational modifications in chaperone proteins, coupled with protein cross-linking a

85 Calreticulin (CRT), an intracellular chaperone protein crucial for the proper folding and tra

86 esence of a gene encoding a potential export chaperone protein, CsaA, adjacent to the AC hydrolase ge

87 Mutations in the co- chaperone protein, CSPalpha, cause an autosomal dominant

88 t study, we show for the first time that the chaperone protein cyclophilin A (CyPA) acts as a Ca(2+)

89 ns invest considerable cellular resources in chaperones, protein degradation, autophagy and mitophagy

90 that HDAC6 is associated physically with the chaperone protein dHsc4/Hsc70 to maintain the proteostas

91 tion of a complex of AKT, PDK1 and the GRP78 chaperone protein, directing phosphorylation of AKTThr30

92 oxidases and the endoplasmic reticulum redox chaperone protein disulfide isomerase (PDI) in many cell

93 y of proteins is a novel regulator of the ER chaperone protein disulfide isomerase (PDI), and that th

94 The oxidation-sensitive chaperone protein DJ-1 has been implicated in several hu

95 A human molecular chaperone protein, DnaJ heat shock protein family (Hsp40

96 The human molecular chaperone protein DNAJB6 was recently found to inhibit t

97 tress response proteins, including the major chaperone proteins, five ATP-dependent protease complexe

98 ich codes for the glucocorticoid receptor co-chaperone protein FKBP51, was consistently upregulated i

99 discoveries that coalesced into the field of chaperones, protein folding, and protein quality control

100 Strikingly, HSPA2, a chaperone protein for CDC2A kinase, is absent in mutant

101 en shown, and CFP-10 has been described as a chaperone protein for ESAT-6.

102 SNCG functions as a molecular chaperone protein for estrogen receptor (ER)-alpha36, a

103 eal the unique ability of tAFP to serve as a chaperone protein for LMM molecules, both endogenous and

104 srupted the interaction of LRP5 with Mesd, a chaperone protein for LRP5/6 that is required for transp

105 MESD encodes an endoplasmic reticulum (ER) chaperone protein for the canonical Wingless-related int

106 cells also have overexpression of molecular chaperone proteins for promoting survival from stress re

107 , we will focus on the function of molecular chaperone proteins for the regulation of cell death in d

108 ial type III secretion (T3S) systems require chaperone proteins for translocation into host cells.

109 al phosphoprotein P that plays the role of a chaperone protein, forming a soluble N(0)-P complex.

110 ray crystal structure of an Atx1-like copper chaperone protein from Bacillus subtilis containing a no

111 DnaK is the canonical Hsp70 molecular chaperone protein from Escherichia coli.

112 ions are destabilizing; agents that modulate chaperone protein function improve STAT3 stability and a

113 e power of reprogramming to examine GRP78, a chaperone protein generally restricted to the endoplasmi

114 The endoplasmic reticulum (ER) chaperone protein glucose-regulated protein 78 (GRP78)/b

115 Here, we found that ablation of the Wnt chaperone protein Gpr177 (also known as Wntless) in mous

116 s identified by N-terminal sequencing as the chaperone protein GroEL.

117 e to the association of RNAP with the global chaperone protein GroEL.

118 sion protein in BL21 star cells coexpressing chaperone proteins GroEL and GroES.

119 The chaperone protein GRP78 serves as a master UPR regulator

120 Targeting its primary mediator, the chaperone protein GRP78, through specific, proteolytic c

121 The subsequent upregulation of ER chaperone proteins GRP78 and GRP58 may contribute to res

122 C directly binds the cell membrane-localized chaperone protein, GRP78, associated with its cofactor,

123 g yeast homologue of the Escherichia coli co-chaperone protein GrpE, which stimulates initiation at b

124 age protein ferritin, and for heme iron, the chaperone proteins haptoglobin and hemopexin.

125 me effect, it seems that the influence these chaperone proteins have on invasion is mediated, at leas

126 f the HDAC family that could regulate the GR chaperone protein heat shock protein 90 (HSP90), in the

127 tion of the cytosolic androgen receptor (AR) chaperone protein heat shock protein 90 (HSP90).

128 Here we show that the chaperone protein heat shock protein 90 beta1 (hsp90beta

129 We report that chaperone proteins heat-shock protein (Hsp)90, heat-shoc

130 nase (citron Rho-interacting kinase [CRIK]), chaperone proteins (heat shock 90-kDa protein [Hsp90], H

131 ion of MMP-9, interactions between MMP-9 and chaperone proteins (heat shock protein [Hsp] 70 and Hsp6

132 wo client proteins (SF3B2 and ataxin-2) of a chaperone protein, heat shock protein 90 (Hsp90) when co

133 As key molecular chaperone proteins, heat shock proteins (HSPs) represent

134 olved the X-ray crystal structure of the RNA chaperone protein Hfq from the alpha-proteobacterium Cau

135 usly, our lab identified a role for the sRNA chaperone protein Hfq in the regulation of components of

136 The RNA chaperone protein Hfq is required for the function of al

137 Additionally, the RNA chaperone protein Hfq was found to be necessary for GcvB

138 target mRNAs, and it is thought that the RNA chaperone protein Hfq, known to be involved in MicA regu

139 In collaboration with the chaperone protein Hfq, SgrS interferes with the interact

140 airing, and this regulation requires the RNA chaperone protein Hfq.

141 on by CDK1 inhibits its association with the chaperone protein HJURP and that the removal of this mod

142 IscU functions through interactions with a chaperone protein HscA and a cochaperone protein HscB.

143 le than unmodified GFP and induces the small chaperone protein HSP-16, which co-localizes and co-immu

144 found that DJ-1 turned on production of the chaperone protein Hsp-70 without affecting glutathione s

145 Overproduction of the chaperone protein Hsp104 results in loss of [PSI+].

146 In this report, we show that a fission yeast chaperone protein Hsp16 inhibits HIV-1 by suppressing th

147 The stress chaperone protein Hsp70 (DnaK) (abbreviated DnaK) and it

148 The stress-inducible chaperone protein HSP70 (HSPA1) is implicated in melanom

149 The stress-induced chaperone protein Hsp70 enables the initiation and progr

150 d LOX-PP in HEK293T cells and the heat shock/chaperone protein Hsp70 identified.

151 degeneration, whereas overexpression of the chaperone protein HSP70 suppressed this toxicity.

152 Our results suggest that the chaperone protein Hsp70, encoded by the SSA family of ge

153 Coexpression of the chaperone protein Hsp70, which can block alpha-synuclein

154 teraction between IRF3 kinase IKKepsilon and chaperone protein HSP70, which is required for the activ

155 rt protein domains (Kunitz and WW), one long chaperone protein (Hsp70), and synthetic lattice protein

156 In addition, inhibition of a cytosolic chaperone protein Hsp90 also induces IRE1alpha oligomeri

157 However, the chaperone protein HSP90 can stabilize Akt and cPKC, part

158 eta dimerization is regulated by DNA and the chaperone protein Hsp90 is poorly understood.

159 In mice, the chaperone protein Hsp90 mediates MOR signaling within th

160 nthesized and evaluated as inhibitors of the chaperone protein Hsp90 using two assays: competition fo

161 plexes in lipid rafts and by segregating the chaperone protein Hsp90, an essential cofactor for IKK,

162 (PP5), which binds to the C terminus of the chaperone protein Hsp90.

163 ion, but instead involved the stress-induced chaperone protein HSP90.

164 Nod2 is constitutively associated with a chaperone protein, Hsp90, which is required for Nod2 sta

165 involving direct binding of EGCG to the AhR chaperone protein, hsp90.

166 1 to the outer mitochondrial membrane by the chaperone protein HSP90beta.

167 Heat shock protein 90 (Hsp90) is a molecular chaperone protein implicated in stabilizing the conforma

168 igma-1Rs) are endoplasmic reticulum resident chaperone proteins implicated in many physiological and

169 tors (sigma(1)Rs) are intracellularly mobile chaperone proteins implicated in several disease process

170 The heat shock protein HSP90 chaperones proteins implicated in breast cancer progress

171 Protein disulfide isomerase (PDI) is a chaperone protein in the endoplasmic reticulum that is u

172 BiP is the predominant DnaK/Hsp70-type chaperone protein in the ER.

173 These data indicate that SNCG is a new chaperone protein in the Hsp-based multiprotein chaperon

174 bacteria and the surprising involvement of a chaperone protein in this process.

175 To counteract this damage, antioxidants and chaperone proteins in muscle cells can prevent oxidation

176 f transcripts encoding endoplasmic reticulum chaperone proteins in neurons.

177 ordinated synthesis of interacting cytosolic chaperone proteins in the absence of a wider stress resp

178 aA- and alphaB-crystallin, the most abundant chaperone proteins in the eye lens.

179 en identified a paralogous group of secreted chaperone proteins in the HSP-90 family that contained t

180 for the first time, we examined the role of chaperone proteins in the viral lifecycle of BTV.

181 of extracellular calreticulin (eCRT), an ER chaperone protein, in animal models enhances wound heali

182 Yeast prions require a core set of chaperone proteins including Sis1, Hsp70 and Hsp104 to g

183 Several chaperone proteins, including hsp90 and p23, have demons

184 in-bound histones are complexed with storage chaperone proteins, including nucleoplasmin.

185 Numerous chaperone proteins, including RbcX, are essential for pr

186 cytiotrophoblast cells) and several forms of chaperone proteins, including, for nonheme iron, the tra

187 al rationale to combine mTOR inhibitors with chaperone protein inhibitors to treat human blood cancer

188 occur through estrogen-induced changes in ER-chaperone protein interactions, which alter the DNA acce

189 the connecting cilium without lipid binding chaperone protein interactions.

190 roundwork for strategies to target essential chaperone-protein interactions in Mtb, the leading cause

191 Curiously, proteolytic removal of the chaperone protein Invariant chain from MHC-II, degradati

192 gma-1R) is an endoplasmic reticulum resident chaperone protein involved in a plethora of cellular fun

193 quired the presence of functional UNC93B1, a chaperone protein involved in signaling by endosomal TLR

194 are a ubiquitous, highly conserved family of chaperone proteins involved in signal transduction, regu

195 chinery of the heat-shock protein 90 (Hsp90) chaperone protein is crucial for cancer progression.

196 We conclude that the GP96 chaperone protein is involved in the otolith formation d

197 The Hsp90 chaperone protein is required for cellular survival unde

198 f haem means that a network of intracellular chaperone proteins is required to avert the cytotoxic ef

199 ne of the fundamental functions of molecular chaperone proteins is to selectively conjugate cellular

200 ptor (Sig-1R), an endoplasmic reticulum (ER) chaperone protein, is an interorganelle signaling modula

201 stantiate the important function of CDC37 in chaperoning protein kinases.

202 ein binding protein 1 (GPIHBP1) and with its chaperone protein lipase maturation factor 1 (LMF1), we

203 The sigma 1 receptor (S1R) is a molecular chaperone protein located in the endoplasmic reticulum a

204 sing target of METH is the sigma receptor, a chaperone protein located on the membrane of the endopla

205 Different histone chaperone proteins mediate the storage and chromatin dep

206 essor screen identified the budding yeast co-chaperone protein Mge1p as a high copy suppressor of the

207 eved by pretreatment with 4-phenylbutrate, a chaperone protein mimic.

208 mitochondria via an N-terminal motif and the chaperone protein mitochondrial heat shock protein 70 (m

209 mouse splenocytes incubated without or with chaperone protein modulators-HSF1A, a small-molecule TRi

210 mer toxicity significantly, even at very low chaperone/protein molar ratios, provided that they were

211 g in glioma cells is regulated by a specific chaperone protein, namely Hsc70.

212 hicken erythrocyte core histones and histone chaperone protein Nap1 under constant low force.

213 This allowed the mapping of a chaperone-protein network consisting of 1,227 unique int

214 ated with elevated steady state levels of ER chaperone proteins, nor does it block cellular activatio

215 e product exhibited similarity to molybdenum chaperone proteins of the DMSO reductase family members

216 18 proteins including cytoskeletal proteins, chaperones, proteins of the translational machinery, ves

217 Chaperone proteins often facilitate the folding and mult

218 With this nucleoside, the effect of a viral chaperone protein on DNA base stacking was site-selectiv

219 strong favorable effect of the co-expressed chaperone proteins on PCC folding, assembly, and activit

220 nteractions of the E fusion proteins and prM chaperone proteins on the virus envelope are reorganized

221 , nucleocytoplasmic shuttling, the effect of chaperone proteins on these properties, and differences

222 ction albeit non-enzymatic like serving as a chaperone protein or an interactive platform between pro

223 appears distinct from that observed in Cu(+) chaperone proteins or catalytic/redox metal binding site

224 AIL binds to the co-chaperone protein p23 and prevents AR's interaction with

225 As rOATP1A1 binds to the chaperone protein, PDZK1, rOATP1A4 functionally hitchhik

226 ure virions lacking an uncleaved form of the chaperone protein prM, unlike most flavivirus-specific a

227 , the PI3K-Akt signaling pathway, hemoglobin chaperone, protein processing in endoplasmic reticulum,

228 promoting an interaction between Syk and the chaperone protein, prohibitin.

229 factor-Y, inhibits its association with the chaperone protein promoter, as well as the promoter acti

230 of discrete nuclear foci containing cellular chaperone proteins, proteasomal components, and ubiquiti

231 ted with heat shock protein 90, an important chaperone protein protecting p210 from proteasome-mediat

232 The histone chaperone protein RBBP4, has previously been shown to bi

233 s are consistent with a model in which small chaperone proteins reduce Abeta toxicity by interacting

234 Co-chaperone proteins regulate the ATP-driven Hsp90 client

235 toskeletal proteins, enzymes, heat shock and chaperone proteins, regulatory proteins, and a fatty aci

236 for the interaction between 5-HT(3A) and the chaperone protein resistance to inhibitors of choline es

237 heat shock protein 70 kDa (Hsc70) is a major chaperone protein responsible for maintaining proteostas

238 receptor expression can be inhibited by the chaperone protein RIC-3.

239 ity in RNA regulatory networks involving RNA chaperone proteins, RNases, sRNAs, and mRNAs.

240 Cyclophilin A (CyPA) is a 20-kDa chaperone protein secreted from vascular smooth muscle c

241 rg, Sip, Spa, Ssa and Sse operons along with chaperone protein SicA.

242 presence of cocaine via interaction with the chaperone protein sigma-1 receptor (Sig-1R).

243 The chaperone protein SmgGDS promotes cell-cycle progression

244 sphorylation-dependent interactions with the chaperone protein SmgGDS-607.

245 by their interaction with the network of co-chaperone proteins, some of which contain tetratricopept

246 likely requirement of periplasmic partner Cu-chaperone proteins specific for each Cu(+) -ATPase.

247 se genes that increase the synthesis of many chaperone proteins specific to individual organelles.

248 c reticulum (ER), bound with the ER-resident chaperone proteins such as BiP, protein disulfide isomer

249 n factor, eIF2alpha, increased expression of chaperone proteins such as glucose-regulated protein-78

250 owever, the properties of other nucleic acid chaperone proteins, such as retrotransposon Ty3 NC, a li

251 The periplasmic molecular chaperone protein SurA facilitates correct folding and m

252 aMCI brain suggesting that alteration in the chaperone protein systems might contribute to the pathog

253 Hsp90 is a chaperone protein that allows cancer cells to tolerate t

254 Cdc37 is one such co-chaperone protein that also has a role in client protein

255 umerous functions, NC is a nucleic acid (NA) chaperone protein that catalyzes NA rearrangements leadi

256 the production of an efflux pump and a metal chaperone protein that confer resistance to Au salts.

257 Hsp90 is a chaperone protein that controls the folding of proteins

258 of the viral RNA and is also a nucleic acid chaperone protein that facilitates nucleic acid restruct

259 Mature NCp7 is a chaperone protein that facilitates remodeling of nucleic

260 ERp44 is an ER lumenal chaperone protein that favors the maturation of disulfid

261 tein-78 (GRP-78) is an endoplasmic reticulum chaperone protein that has been implicated in functional

262 liferation, including Tom70, a mitochondrial chaperone protein that interacts with both SARS-CoV-1 an

263 tocytes lacking collectrin, an intracellular chaperone protein that localizes within the endoplasmic

264 ynthesis, acting both as a catalyst and as a chaperone protein that mediates substrate channeling int

265 Caenorhabditis elegans known as UNC93B1 is a chaperone protein that mediates translocation of the nuc

266 Thus, frataxin is an iron chaperone protein that protects the aconitase [4Fe-4S]2+

267 Hsp90, a chaperone protein that regulates several oncoproteins, i

268 Wls/Gpr177 is a newly identified chaperone protein that specifically escorts Wnt ligands

269 Sigma1 receptors (Sigma1R) are intracellular chaperone proteins that bind psychotropic drugs and also

270 neuronal stomatin-like proteins are putative chaperone proteins that can modify volatile anesthetic s

271 bers of evolutionarily conserved families of chaperone proteins that inhibit the aggregation of unfol

272 Hsp90 cooperates with a set of co-chaperone proteins that modulate Hsp90 activity and/or t

273 stead, it appears that some bacteria utilize chaperone proteins that stabilize periplasmic proteins,

274 in which surveillance pathways compete with chaperone proteins that transiently protect nascent ncRN

275 r complexes of Kv4 channels with a family of chaperone proteins, the potassium channel-interacting pr

276 transcription factor that requires a second chaperone protein to activate the output promoter.

277 store vision by binding to alphaB-crystallin chaperone protein to dissolve or disaggregate lenticular

278 t on the unfolded protein response (UPR) and chaperone proteins to ensure correct protein folding and

279 ound: the periplasmic protein, bp26, and the chaperone protein, trigger factor (TF).

280 ly trafficked to dendrites by binding to the chaperone protein TRIP8b.

281 We demonstrate a role for cytosolic chaperones, proteins typically associated with folding n

282 t proteins by covalent ligation of the small chaperone protein ubiquitin.

283 +)] as a model to investigate the effects of chaperone proteins upon prion variant determination.

284 We identify a protease and several chaperone proteins upregulated under aminoglycoside stre

285 rom immunization studies using tumor-derived chaperone protein vaccines, which lead to antigen-specif

286 FABP4, a lipid chaperone protein, was identified as the critical regula

287 a point mutation in ureD, encoding a urease chaperone protein, was identified, resulting in a substi

288 To understand how OS-9 interacts with ER chaperone proteins, we mapped its interaction with Grp94

289 Because CRCL contain a variety of heat shock/chaperone proteins, we theorized that CRCL obtained from

290 and alterations in the binding of MMP-9 with chaperone proteins were also observed in the retina from

291 ive stress-regulated mitochondrial aconitase chaperone protein, were markedly reduced in Epas1(-)(/)(

292 , which binds to other endoplasmic reticulum chaperone proteins, were sufficient for the suppression

293 s of the transporters are often supported by chaperone proteins, which scavenge the metal ions from t

294 ss II HDACs creates binding sites for 14-3-3 chaperone proteins, which trigger nuclear export of thes

295 n elevated expression of stress response and chaperone proteins, while fast growth in nitrogen-defici

296 sigma-1 receptor is an endoplasmic reticulum chaperone protein, widely expressed in central and perip

297 e and that one of its substrates is Hsp90, a chaperone protein with both intra- and extracellular cli

298 Hsp90 is a chaperone protein with important roles in maintaining tr

299 ied the 90-kDa heat shock protein (Hsp90), a chaperone protein with novel signaling functions, as a C

300 Candidal Hsp70 proteins are classical chaperone proteins with two discrete functional domains