ライフサイエンスコーパス: chaperone protein

1 at matches contemporary understanding of the chaperone protein.

2 identified BAG1, which encodes a prosurvival chaperone protein.

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

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

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

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

7 anscriptional levels of GRP78, an ER luminal chaperone protein.

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

9 gand-mediated conformational changes of this chaperone protein.

10 volved through immune selection on the groEL chaperone protein.

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

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

13 17p/Sec18p, the vacuolar tethering and SNARE chaperone proteins.

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

15 ations (PTMs) and assisted by a number of co-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 rmation in the bacterial cytosol by specific chaperone proteins.

21 ation of genes such as Grp78/BiP encoding ER chaperone proteins.

22 eptide shows differences in association with chaperone proteins.

23 lysis of ATP and also by association with co-chaperone proteins.

24 f neurodegenerative processes using modified chaperone proteins.

25 ised by an overexpression of contractile and chaperone proteins.

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

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

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

29 from its sequestered site with the molecular chaperone protein 14-3-3 and displace proapoptotic BAX (

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

31 creates docking sites for the intracellular chaperone protein 14-3-3.

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

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

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

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

36 We now report that five cellular chaperone proteins, all known cofactors of Hsp90, were s

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

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

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

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

41 The chaperone protein and guanine nucleotide exchange factor

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

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

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

45 d to a highly conserved pocket in the hsp 90 chaperone protein and inhibit its function.

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

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

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

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

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

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

52 Chaperone proteins are considered to be fairly ubiquitou

53 Chaperone proteins are crucial for the maintenance of na

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

55 Chaperone proteins are effective antitumor vaccines when

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

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

58 Clusterin is a chaperone protein associated with treatment resistance a

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

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

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

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

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

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

65 eins, antioxidant defense enzymes, molecular chaperones, protein biosynthesis enzymes, and traffickin

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

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

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

69 localize with endoplasmic reticulum resident chaperone protein BiP.

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

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

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

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

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

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

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

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

78 The chaperone protein, calreticulin, was found to undergo cl

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

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

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

82 2 (CCT2), a gene that encodes the molecular chaperone protein, CCTbeta.

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

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

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

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

87 BiP is a chaperone protein containing a polypeptide binding site

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

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

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

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

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

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

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

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

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

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

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

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

100 The folding assistant and chaperone protein-disulfide isomerase (PDI) catalyzes di

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

102 the cysteine-rich zinc-binding domain of the chaperone protein DnaJ.

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

104 inding domain of the bacterial heat shock 70 chaperone protein DnaK was studied in its apo form and w

105 entified a role for an endoplasmic reticulum chaperone protein family member, zebrafish GP96.

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

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

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

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

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

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

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

113 f the invariant chain (Ii), a human-specific chaperone protein for MHC class II normally generated by

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

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

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

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

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

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

120 -combs; 41.2%), and an endoplasmic reticulum chaperone protein gene SEC63 (37.5%).

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

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

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

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

125 The chaperone protein GRP78 serves as a master UPR regulator

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

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

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

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

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

131 to being an abundant and pivotal cytoplasmic chaperone protein, has been shown to be a weak ATPase.

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

133 onstrated several mechanisms where defective chaperone proteins have pathogenic consequences.

134 ormed to monitor farnesylation status of the chaperone protein HDJ-2.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

149 ng persistence (NRP) is the alpha-crystallin chaperone protein homologue (Acr).

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

171 1 to the outer mitochondrial membrane by the chaperone protein HSP90beta.

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

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

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

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

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

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

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

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

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

181 f transcripts encoding endoplasmic reticulum chaperone proteins in neurons.

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

183 ncreased levels of binding protein and other chaperone proteins in the endosperm.

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

185 To study the possible role of chaperone proteins in the regulation of PPARalpha activi

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

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

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

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

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

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

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

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

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

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

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

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

198 The Hsp90 chaperone protein is required for cellular survival unde

199 RT activation by the chaperone proteins is a dynamic process dependent on ATP

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

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

202 Hsp90, which often cooperates with Cdc37 in chaperoning protein kinases, does not affect Spc1 SAPK.

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

204 GRP94 is a chaperone protein localized in the endoplasmic reticulum

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

206 Retention is dependent upon chaperone proteins, many of which require Ca(++) for opt

207 Different histone chaperone proteins mediate the storage and chromatin dep

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

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

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

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

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

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

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

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

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

217 Calreticulin has long been recognized as a chaperone protein of the endoplasmic reticulum (ER) and

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

219 18 proteins including cytoskeletal proteins, chaperones, proteins of the translational machinery, ves

220 Chaperone proteins often facilitate the folding and mult

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

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

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

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

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

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

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

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

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

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

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

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

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

234 n receptor, was identified as the heat shock/chaperone protein receptor of APC.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

259 haracterized by increased levels of HSP70, a chaperone protein that has been shown to counteract para

260 nucleocapsid protein (NC) is a nucleic acid chaperone protein that has been shown to greatly facilit

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

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

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

264 Cdc37 is a co-chaperone protein that recruits several immature client

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

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

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

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

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

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

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

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

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

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

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

276 he contributions of endotoxin and heat shock/chaperone proteins to the stimulation of innate immune r

277 t CPE may require another integral membrane "chaperone" protein to insert through the lipid bilayer i

278 Unexpected clusters included genes for chaperones, protein trafficking, ubiquitin/26 S proteaso

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 pitate with A beta has identified six likely chaperone proteins: two members of the HSP70 family, thr

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

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

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

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

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

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

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

289 Neither E2 nor chaperone proteins were detected in unwinding complexes.

290 Remarkably, a set of proteins identified as chaperone proteins were found to be highly abundant on t

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