ライフサイエンスコーパス: molecular chaperone

1 , a class of ubiquitous and highly conserved molecular chaperone.

2 tructural requirements for its function as a molecular chaperone.

3 ealed that HdeB indeed works as an effective molecular chaperone.

4 and maintains muscle function by acting as a molecular chaperone.

5 rotein 90 (Hsp90) is an essential eukaryotic molecular chaperone.

6 of hRes subunits pointed to resistin being a molecular chaperone.

7 p90alpha, the two cytosolic paralogs of this molecular chaperone.

8 multimeric form of Prdx-1 with activity as a molecular chaperone.

9 r protein homeostasis and requires effective molecular chaperones.

10 controlled by various mechanisms, including molecular chaperones.

11 equires assistance by a complex machinery of molecular chaperones.

12 ins can only be achieved by interaction with molecular chaperones.

13 ition, celastrol modulated the expression of molecular chaperones.

14 ck response (HSR) for balanced expression of molecular chaperones.

15 d other stresses to induce the expression of molecular chaperones.

16 inhibited by the presence of ATP-independent molecular chaperones.

17 s) critically depend on a complex network of molecular chaperones.

18 and highly conserved family of ATP-dependent molecular chaperones.

19 heat shock protein 90 kDa (Hsp90) family of molecular chaperones.

20 proteasome subunits, antioxidant enzymes and molecular chaperones.

21 The molecular chaperone 4-phenylbutyric acid attenuates citr

22 PR silencing or by the addition of the small molecular chaperone 4-phenylbutyric acid, implicating a

23 a D21N 14-3-3zeta mutant exhibited enhanced molecular chaperone ability that prevented amorphous pro

24 w that a reduction in the expression of this molecular chaperone accelerates prion pathogenesis in vi

25 ate genes with assorted functions, including molecular chaperones, acid resistance, stress response a

26 Molecular chaperones act on non-native proteins in the c

27 rsity in the microscopic mechanisms by which molecular chaperones act to suppress amyloid formation.

28 re highly relevant to the emerging view that molecular chaperone action is intimately involved in the

29 nistically, both LOAD mutations impaired the molecular chaperone activity of ADAM10 prodomain.

30 he highly efficacious mode of action of this molecular chaperone against protein aggregation, and dem

31 protein beta2-microglobulin (beta2m) and the molecular chaperone alphaB-crystallin was investigated b

32 We hypothesized that treatment with the molecular chaperone ambroxol hydrochloride would improve

33 uman wild-type, N370S and L444P GBA with the molecular chaperones ambroxol and isofagomine.

34 HSP70 is a molecular chaperone and a key component of the heat-shoc

35 in cells and regulates G proteins as both a molecular chaperone and GEF.

36 The Hsp90 molecular chaperone and its Cdc37 cochaperone help stabi

37 Hsp90 is a dimeric molecular chaperone and its function is modulated by its

38 bination in a fragment screening against the molecular chaperone and oncology target Hsp90, for which

39 by transcriptionally inducing mitochondrial molecular chaperone and protease genes.

40 ase and other genetic disorders by modifying molecular chaperone and protein degradation pathways.

41 aracterized an interplay between the Hsp90Ec molecular chaperone and the ClpQ protease involved in co

42 heat shock proteins (HSPs), which are often molecular chaperones and are under the control of heat s

43 tegies used to tune the PN through targeting molecular chaperones and assess the potential of the che

44 Molecular chaperones and chaperone-sorting factors, such

45 Proteostasis depends on a network of molecular chaperones and clearance pathways involved in

46 Molecular chaperones and cytosolic and vacuolar degradat

47 that considers pairwise interactions between molecular chaperones and different protein species to id

48 hin the endoplasmic reticulum is assisted by molecular chaperones and folding catalysts that include

49 in the rough endoplasmic reticulum, and many molecular chaperones and folding enzymes are involved in

50 culum (ER) orthologue of the Hsp70 family of molecular chaperones and is intricately involved in most

51 ostasis (or proteostasis) network comprising molecular chaperones and other factors.

52 eotoxic stress by inducing the expression of molecular chaperones and other heat shock response genes

53 ngs thus highlight an intricate interplay of molecular chaperones and protein disorder in the evolvab

54 ated Protein (GRP) 94 and GRP78 are critical molecular chaperones and regulators of signaling.

55 asmic sites in a manner that is regulated by molecular chaperones and requires TORC1 activity signali

56 ostasis is achieved by a delicate network of molecular chaperones and various proteolytic processes s

57 rovide a comparative discussion of the Ric-8 molecular chaperoning and GEF activities, and support th

58 endoplasmic reticulum (ER) membrane protein, molecular chaperone, and a component of the translocon.

59 The sigma-1 receptor (sigma1R) is a molecular chaperone, and its ligands have been shown to

60 responses, including cyp1a (up to 560-fold), molecular chaperones, and antioxidant enzymes.

61 elial cells, its interactome is enriched for molecular chaperones, and it interacts with the cytoplas

62 Many enzymes, molecular chaperones, and post-translational modifiers f

63 began with the study of protein folding and molecular chaperones, and she went on to show that prote

64 nd molecular stress responses (expression of molecular chaperones, antioxidants, bioenergetic and pro

65 Molecular chaperones are an essential part of the machin

66 Molecular chaperones are essential molecules for cell gr

67 Hsp70 molecular chaperones are implicated in a wide variety of

68 Molecular chaperones are pivotal in folding and degradat

69 Molecular chaperones are responsible for managing protei

70 We have investigated the potential role of molecular chaperones as modulators of the immune respons

71 Metazoan molecular chaperones assist native folding and block pol

72 in a murine model using a recently developed molecular chaperone-based vaccine that specifically targ

73 iously, we have shown that a cysteine in the molecular chaperone BiP, a Hsp70 molecular chaperone wit

74 drophobic N terminus and adenylylates the ER molecular chaperone, BiP, at Ser-365 and Thr-366.

75 Thus EMC1 acts as a molecular chaperone, bracing the destabilized SV40 in a

76 We propose that ThT functions as a molecular chaperone by end stacking on terminal G4-quart

77 90 (Hsp90) clients and are recruited to the molecular chaperone by the kinase-specific cochaperone c

78 protein 90 (HSP90) plays a unique role among molecular chaperones by promoting the evolution of herit

79 e turnover of receptors associating with the molecular chaperone calnexin (CNX) was significantly slo

80 eir rebinding to the carbohydrate-binding ER molecular chaperones calnexin and calreticulin.

81 tk in apoptotic cell uptake, identifying the molecular chaperone calreticulin (CRT) as a novel substr

82 chanism by which binding interactions from a molecular chaperone can be used to overcome protein aggr

83 Thus, molecular chaperones can contribute to functional mainte

84 ggregation, and demonstrate that the role of molecular chaperones can involve interactions with multi

85 ctin requires assistance from the oligomeric molecular chaperone CCT.

86 s in the evolutionarily conserved AAA-ATPase molecular chaperone, CDC48A, homologous to yeast Cdc48 a

87 rial cell wall and inhibits SlyD, which is a molecular chaperone, cis/trans peptidyl prolyl isomerise

88 The molecular chaperone ClpB/Hsp104, a member of the AAA+ su

89 The molecular chaperone ClpC/Hsp93 is essential for chloropl

90 We characterized some effects of the molecular chaperone clusterin, providing new and more de

91 f cytoprotective heat shock proteins (HSPs), molecular chaperones/cochaperones constituting a major c

92 N-linked glycans and carbohydrate-binding molecular chaperones contribute to the efficient folding

93 Molecular chaperones control a multitude of cellular fun

94 Molecular chaperones control the cellular folding, assem

95 In the cytosol, different classes of molecular chaperones cooperate in evolutionarily conserv

96 (core 1 beta3-galactosyltransferase) and its molecular chaperone Cosmc regulate the biosynthesis of m

97 d by knocking-out Core 1 beta3Gal-T Specific Molecular Chaperone (COSMC), N-glycans by targeting the

98 Core 1 beta3GalT-specific molecular chaperone (Cosmc), which encodes an X-linked c

99 ock protein 47 (HSP47) is a single-substrate molecular chaperone crucial for collagen biosynthesis.

100 TRAP1 is a HSP90 molecular chaperone deregulated in human tumors and resp

101 y structures, suggesting a means to generate molecular chaperone diversity.

102 -terminal domain of DNAJB1, a homolog of the molecular chaperone DNAJ, fused in frame with PRKACA, th

103 hese results emphasize the diverse action of molecular chaperones during CytoQC.

104 Several studies suggest a role for molecular chaperones during these processes.

105 eat shock protein 70 (Hsp70) is a ubiquitous molecular chaperone essential for maintaining cellular p

106 The human AAA ATPase p97 is a molecular chaperone essential in cellular proteostasis.

107 e heat shock protein 90 (Hsp90) is a dimeric molecular chaperone essential in numerous cellular proce

108 ic reticulum and requires a large numbers of molecular chaperones, foldases, and post-translational m

109 s issue, Chai et al. find that Munc18-1 is a molecular chaperone for alpha-synuclein and that aggrega

110 dings suggest that BuGZ not only serves as a molecular chaperone for Bub3 but also enhances its loadi

111 Thioflavin T (ThT) functions as a molecular chaperone for gelation of water by guanosine a

112 any signaling proteins, depends on the Hsp90 molecular chaperone for in vivo function.

113 HSP90 is a molecular chaperone for several signaling proteins that

114 s an important regulator of EMT, acting as a molecular chaperone for SMAD4 and as its potential thera

115 ed by E. coli GroEL and GroES, are essential molecular chaperones for protein folding.

116 l heat-shock protein Hsp27 are linked to its molecular chaperone function and influenced by post-tran

117 In addition, several molecular chaperone genes were overexpressed in the pres

118 t has been hypothesized that the ER-resident molecular chaperone glucose-regulated protein 94 (GRP94)

119 Molecular chaperones govern protein homeostasis, being a

120 sY, ftsH, ftsE, mreB, mreC, mreD, rodA), and molecular chaperones (grpE, dnaK, dnaJ, hsp20, hsp90), e

121 Molecular chaperones have central roles in each of the a

122 Here, we identify the molecular chaperone heat shock cognate protein 70 (Hsc70

123 aggregate-driven sequestration of the major molecular chaperone heat shock cognate protein 70 (HSC70

124 The molecular chaperone heat shock protein 70 (Hsp70) plays

125 Molecular chaperone Heat Shock Protein 70 (Hsp70) plays

126 s nucleotide exchange factors (NEFs) for the molecular chaperone heat shock protein 70 (Hsp70).

127 The molecular chaperone heat shock protein 90 (Hsp90) is an

128 The molecular chaperone heat shock protein 90 (Hsp90) is ove

129 The molecular chaperone heat shock protein 90 (HSP90) is req

130 d cellular signaling by association with the molecular chaperone heat shock protein 90 (Hsp90).

131 rmal and cancer cells depends on the dimeric molecular chaperone heat shock protein 90 (Hsp90).

132 The molecular chaperone heat shock protein A2 (HSPA2), a mem

133 The molecular chaperone heat-shock protein 90 (Hsp90) is an

134 hippocampal excitatory synaptic markers, and molecular chaperones (heat shock proteins (HSPs)) involv

135 es, including antioxidants, detoxicants, and molecular chaperones (heat shock proteins).

136 Another set of molecular chaperones helps to maintain proteins in their

137 ng Protein, a 70 kDa homodimer) binds to the molecular chaperone Hsc70 (a 70 kDa monomer), and this c

138 The molecular chaperone Hsc70 assists in the folding of non-

139 erative disease-associated proteins with the molecular chaperone Hsc70 is well known, and we hypothes

140 , we observed that addition of the mammalian molecular chaperone Hsc70, abundantly associated with G8

141 which leads to Parkinson's disease, and the molecular chaperone Hsc70.

142 ly associated with Huntington's disease, and molecular chaperone Hsc70.

143 LC-1 biosynthesis is also facilitated by the molecular chaperones Hsc70 and Hsp90beta.

144 rone Hsp70, and its interaction with another molecular chaperone Hsp104 on [SWI(+) ] maintenance.

145 disassembled at elevated temperatures by the molecular chaperone Hsp104.

146 rm of the Sup35 protein, is dependent on the molecular chaperone Hsp104.

147 nt FUS is implicated in this process, as the molecular chaperone Hsp110 mitigated these toxic effects

148 Most striking, the addition of the molecular chaperone Hsp110, in a concentration substoich

149 Here, we report that the molecular chaperone Hsp27 (HSPB1) drives EMT in prostate

150 Highly conserved molecular chaperone Hsp70 heat shock proteins play a key

151 f Sse1 - a nucleotide exchange factor of the molecular chaperone Hsp70, and its interaction with anot

152 of alpha-syn aggregation is dependent on the molecular chaperone Hsp70, which is consistent with the

153 and HSP90 inhibitors or heat shock, was the molecular chaperone HSP70.

154 Maintenance of protein homeostasis by molecular chaperones Hsp70 and Hsp90 requires their spat

155 The stress-inducible molecular chaperone, HSP72, is an important therapeutic

156 eadily accessible to the bud neck (including molecular chaperone Hsp82 and glycolytic enzyme Pgk1).

157 lation of ATPase and closure kinetics in the molecular chaperone Hsp90 by allosteric modulators throu

158 The function of the molecular chaperone Hsp90 depends on large conformationa

159 tify compounds that discriminate between the molecular chaperone Hsp90 of the protozoan pathogen Plas

160 TPase) stimulates the ATPase activity of the molecular chaperone Hsp90 to accelerate the conformation

161 pecific co-chaperone that interacts with the molecular chaperone HSP90 to facilitate the stable assem

162 Hsf1 activation depends upon the molecular chaperone Hsp90 under basal and heat shock con

163 ell-known cellular RNA binding proteins, the molecular chaperone Hsp90 was identified as a component

164 Here, we identify one such protein, the molecular chaperone Hsp90, as an important factor requir

165 ) is the bacterial homolog of the eukaryotic molecular chaperone Hsp90, which is involved in the prot

166 et that should receive more attention is the molecular chaperone Hsp90.

167 receptor, an effect that is dependent on the molecular chaperone HSP90.

168 on of 20S proteasome components requires the molecular chaperone Hsp90.

169 nnel in HeLa cells and identified ER lumenal molecular chaperone immunoglobulin heavy-chain-binding p

170 ort that alphaB-crystallin, an antiapoptotic molecular chaperone implicated in the pathogenesis of di

171 The heat shock protein 70s (HSP70s) are molecular chaperones implicated in many cancers and of s

172 ith MEC-6, an endoplasmic reticulum-resident molecular chaperone in Caenorhabditis elegans MEC-6 modu

173 eat shock protein-90 (Hsp90) is an essential molecular chaperone in eukaryotes involved in maintainin

174 biological role of this abundantly expressed molecular chaperone in health and disease.

175 ted peroxidase activity, AnPrx6 can act as a molecular chaperone in its dimeric state, contrary to ot

176 ntribute to the fundamental understanding of molecular chaperones in assisting protein folding in liv

177 longation pausing, suggesting a dual role of molecular chaperones in facilitating polypeptide elongat

178 h preproteins and mediate the recruitment of molecular chaperones in the intermembrane space to facil

179 f full-length TRAP1, the mitochondrial Hsp90 molecular chaperone, in a catalytically active closed st

180 portance in maintaining protein homeostasis, molecular chaperones, including heat-shock protein 90 (H

181 Hsp90 is a molecular chaperone involved in the activation of numero

182 Proteases and molecular chaperones involved in plastid protein quality

183 are highlighted in the context of studies of molecular chaperones involved in protein disaggregation.

184 The ATPase cycle of the Hsp90 molecular chaperone is essential for maintaining the sta

185 and toward that end, modulation of cellular molecular chaperones is a potential therapeutic target.

186 udy, we found that HSP90, a highly conserved molecular chaperone, is overexpressed in CLL compared wi

187 SJ1 (DNAJB2), a member of the DNAJ family of molecular chaperones, is a key player in neuronal proteo

188 in the production of heat shock proteins or molecular chaperones, is triggered by elevated temperatu

189 Hsp90 is a conformationally dynamic molecular chaperone known to promote the folding and act

190 deling of the inhibited complexes by diverse molecular chaperones known as rubisco activases (Rcas).

191 , fully mapping an allosteric landscape of a molecular chaperone like DnaK will facilitate the develo

192 uce disulfide bridges but possesses a strong molecular chaperone-like activity.

193 t that, in some settings, this mitochondrial molecular chaperone may act as a tumor suppressor.

194 t intriguing results showing that "designer" molecular chaperones may hold the key to an evolutionari

195 tor class due to interactions with different molecular chaperones, mediated in part by strict spatial

196 that rational development of drugs targeting molecular chaperones might help in future control of pat

197 Molecular chaperones monitor protein homeostasis and def

198 In eukaryotic cells a molecular chaperone network associates with translating

199 The molecular chaperone network protects against the toxic m

200 Especially in the field of molecular chaperones, NMR has recently provided the firs

201 TL4 was previously described as an unfolding molecular chaperone of LPL that catalytically converts a

202 We show that the disaggregase Hsp101, a molecular chaperone of the Hsp100 family, dissolves heat

203 ATP-binding nonglycosylated ligand-regulated molecular chaperone of unknown three-dimensional structu

204 sis network coordinates these processes with molecular chaperones of different classes and their regu

205 gely unknown, its sequence domains suggest a molecular chaperone or protein quality control function.

206 interaction of Isu with the J-protein/Hsp70 molecular chaperone pair, Jac1 and Ssq1.

207 It is increasingly recognized that molecular chaperones play a key role in modulating the f

208 Heat shock protein 70 (Hsp70) molecular chaperones play critical roles in protein home

209 Molecular chaperones play key roles during growth, devel

210 Hsp70 molecular chaperones play key roles in cellular protein

211 The HSP90 molecular chaperone plays a key role in the maturation,

212 Molecular chaperones prevent aggregation and misfolding

213 Molecular chaperones prevent the aggregation of polyQ-co

214 s, the translation machinery and a number of molecular chaperones promote correct de novo folding of

215 The human molecular chaperone protein DNAJB6 was recently found to

216 1, subunit 2 (CCT2), a gene that encodes the molecular chaperone protein, CCTbeta.

217 One of the fundamental functions of molecular chaperone proteins is to selectively conjugate

218 discusses current understanding of how Hsp70 molecular chaperones recognize and act on their substrat

219 The results show how molecular chaperones recognize unfolded polypeptides and

220 P), encoding a heat shock protein 70 (HSP70) molecular chaperone, reduced autophagy.

221 omain (NBD) of heat shock protein 70 (Hsp70) molecular chaperones reduces the affinity of their C-ter

222 The heat shock protein 90 (Hsp90) family of molecular chaperones regulates protein homeostasis, fold

223 Furthermore, BAG family molecular chaperone regulator 3 assisted protein folding

224 the heat shock protein 70 (Hsp70) family of molecular chaperones rely on allosteric interactions bet

225 r Galphai, Galphaq, and Galpha12/13 and as a molecular chaperone required for the initial association

226 t constantly be engaged and remodeled by the molecular chaperone Rubisco activase (Rca).

227 understand how low concentrations of passive molecular chaperones, such as small heat-shock proteins,

228 Molecular chaperones, such as the small heat shock prote

229 In vivo, molecular chaperones, such as the small heat-shock prote

230 OM protein insertase (the Bam complex) and a molecular chaperone (SurA) are both necessary and suffic

231 ating the ability of these enzymes to act as molecular chaperones, surpassing the redox effect.

232 embly intermediates or evidence that another molecular chaperone system was used for antibody product

233 Moreover, by analysing several protein-molecular chaperone systems, we reveal the striking dive

234 LRP1 requires a molecular chaperone, termed the receptor-associated prot

235 cial as a cosubstrate, but can also act as a molecular chaperone that activates and stabilizes enzyme

236 ck protein of 90 kDa (Hsp90) is an essential molecular chaperone that adopts different 3D structures

237 in (alphaHb)-stabilizing protein (AHSP) is a molecular chaperone that assists hemoglobin assembly.

238 ein 90 (Hsp90) is an essential ATP-dependent molecular chaperone that associates with numerous client

239 k protein alphaB-crystallin is an oligomeric molecular chaperone that binds aggregation-prone protein

240 res the receptor-associated protein (RAP), a molecular chaperone that binds LRP1 and other low densit

241 a-Hemoglobin stabilizing protein (AHSP) is a molecular chaperone that binds monomeric alpha-subunits

242 Hsp90 is a molecular chaperone that facilitates the maturation of s

243 DnaK is a molecular chaperone that has important roles in protein

244 In bacteria, trigger factor (TF) is the molecular chaperone that interacts with the ribosome to

245 Heat shock protein 90 (HSP90) is a molecular chaperone that is up-regulated in cancer and i

246 Thus, DAXX uses a novel strategy as a molecular chaperone that paradoxically couples its own f

247 (Hsp90) is a widely conserved and ubiquitous molecular chaperone that participates in ATP-dependent p

248 novel role for the N terminus of hTLR7 as a molecular chaperone that provides processed hTLR7 with t

249 p58(IPK) is a molecular chaperone that regulates protein homeostasis t

250 Hsp90 is a highly conserved molecular chaperone that remodels hundreds of client pro

251 Hsp90 is a homodimeric ATP-dependent molecular chaperone that remodels its substrate 'client'

252 eins (sHsps) are a family of ATP-independent molecular chaperones that are important for binding and

253 ck proteins (sHsps) are virtually ubiquitous molecular chaperones that can prevent the irreversible a

254 ation, living cells maintain a population of molecular chaperones that ensure the solubility of the p

255 malian small heat-shock proteins (sHSPs) are molecular chaperones that form polydisperse and dynamic

256 Small heat shock proteins are ubiquitous molecular chaperones that form the first line of defence

257 job description: organizing a small team of molecular chaperones that keep the proteome moving.

258 i HscA and HscB, the specialized Hsp70/Hsp40 molecular chaperones that mediate iron-sulfur cluster tr

259 Tumor cells display on their surface several molecular chaperones that normally reside in the endopla

260 70-kDa Heat shock proteins are ATP-driven molecular chaperones that perform a myriad of essential

261 oteins such as HSP70 and HSP90 are important molecular chaperones that play critical roles in biotic

262 Heat shock protein 70 (Hsp70) and Hsp90 are molecular chaperones that play essential roles in tumor

263 1 is to regulate a network of genes encoding molecular chaperones that protect proteins from damage c

264 e induced by cellular stress and function as molecular chaperones that regulate protein folding.

265 proteins (sHsps) are a ubiquitous family of molecular chaperones that suppress the unspecific aggreg

266 ular components involved, including the H2-M molecular chaperone, the proteasome and gamma-interferon

267 Cells express a family of molecular chaperones, the heat shock proteins, during ti

268 orchestrated action of conserved families of molecular chaperones, the Hsp70 and Hsp90 systems.

269 essed by blocking the proteasome, Hsp70-type molecular chaperones, the Pib1 E3 ubiquitin-protein liga

270 involve enzyme replacement therapy (ERT) and molecular chaperone therapy.

271 , when exposed to conditions that compromise molecular chaperones, these proteins aggregate and becom

272 Unlike other Hsp70 molecular chaperones, those of the eukaryotic cytosol ha

273 ergic neurons activates HSF1 and upregulates molecular chaperones through the metabotropic serotonin

274 proteins use a second membrane protein as a molecular chaperone to assist their folding and to ensur

275 results suggest that CBFbeta may serve as a molecular chaperone to enable Vif to adopt an appropriat

276 support the notion that CBFbeta serves as a molecular chaperone to facilitate Vif-E3 ligase assembly

277 Organisms use molecular chaperones to combat the unfolding and aggrega

278 ck factor (Hsf1) regulates the expression of molecular chaperones to maintain protein homeostasis.

279 The ability of molecular chaperones to overcome the misfolding and aggr

280 his problem, cells have evolved a network of molecular chaperones to prevent protein aggregation and

281 HSPs) are well documented to act in vitro as molecular chaperones to prevent the irreversible aggrega

282 ay, codon optimization, and co-expression of molecular chaperones to promote expressed SrtA secretion

283 Bacterial secretion systems often employ molecular chaperones to recognize and facilitate export

284 es in stress protection; (3) accumulation of molecular chaperones to restore protein homeostasis toge

285 Molecular chaperones triage misfolded proteins via actio

286 gated the effects of the ribosome-associated molecular chaperone trigger factor (TF) on alphaSyn stru

287 of protein L in presence of the prototypical molecular chaperone trigger factor over the range of phy

288 The molecular chaperone UNC-45B is required for the folding

289 Specifically, constitutive downregulation of molecular chaperones was observed, which may impact resp

290 mitochondrial 2-Cys peroxiredoxins to act as molecular chaperones when forming decamers.

291 We propose that TRAP1 is a ligand-activated molecular chaperone, which couples ATP binding to dramat

292 hsc-70 (HSPA8) is a cytosolic molecular chaperone, which plays a central role in cellu

293 Similarly, whether and how molecular chaperones, which have been shown to buffer de

294 y conserved subfamily of the Hsp90 family of molecular chaperones whose function has not been defined

295 Glucose-regulated protein 78 (GRP78), a molecular chaperone widely elevated in human cancers, is

296 Hsp70s are allosteric molecular chaperones with conformational landscapes that

297 ck proteins (sHSPs) are a conserved group of molecular chaperones with important roles in cellular pr

298 ke proteins, and enhanced the association of molecular chaperones with the aggregates.

299 eine in the molecular chaperone BiP, a Hsp70 molecular chaperone within the ER, is susceptible to oxi

300 and through a co-expression strategy with a molecular chaperone, yields of one engineered thaumatin