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 and maintains muscle function by acting as a molecular chaperone.

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

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

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

6 tructural requirements for its function as a molecular chaperone.

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

8 ain indicating that YcjX might function as a molecular chaperone.

9 a cell and requires the action of effective molecular chaperones.

10 equires assistance by a complex machinery of molecular chaperones.

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

12 proteasome subunits, antioxidant enzymes and molecular chaperones.

13 r protein homeostasis and requires effective molecular chaperones.

14 controlled by various mechanisms, including molecular chaperones.

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

16 sHsps) compose the most widespread family of molecular chaperones.

17 peptidylprolyl isomerases, a superfamily of molecular chaperones.

18 (Hsp70s) are ubiquitous and highly conserved molecular chaperones.

19 uitous and ancient family of ATP-independent molecular chaperones.

20 uires the action of cotranslationally acting molecular chaperones.

21 The molecular chaperone 4-phenylbutyric acid attenuates citr

22 The molecular chaperone 90-kDa heat-shock protein (Hsp90) as

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 g-of-war between cis/trans isomerization and molecular chaperone activity.

29 e previously obtained evidence that OsmY has molecular chaperone activity.

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

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

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

33 How BiP operates as a molecular chaperone and as an ER stress sensor is unknow

34 iSyTE-bioinformatics analysis identified the molecular chaperone and cytoskeletal modulator, HSPB1, a

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

36 nctional switch between UgpB's activity as a molecular chaperone and its activity as a G3P transporte

37 The Hsp90 molecular chaperone and its Cdc37 cochaperone help stabi

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

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

40 by transcriptionally inducing mitochondrial molecular chaperone and protease genes.

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

42 ansmembrane-spanning proteins which serve as molecular chaperones and allosteric modulators of G-prot

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 cochaperones are the most abund

47 Molecular chaperones and cytosolic and vacuolar degradat

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

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

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

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

52 trols basal and stress-induced expression of molecular chaperones and other targets.

53 Even with an elaborate network of molecular chaperones and protein folding facilitators, m

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

55 This suggests that competition between molecular chaperones and the LBD for the FQNLF motif reg

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

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

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

64 Hsp70 molecular chaperones are abundant ATP-dependent nanomach

65 The molecular chaperones are central mediators of protein ho

66 Molecular chaperones are essential molecules for cell gr

67 Members of the Hsp90 and Hsp70 families of molecular chaperones are imp\ortant for the maintenance

68 Hsp70 molecular chaperones are implicated in a wide variety of

69 rs an alternative response in which specific molecular chaperones are induced.

70 Molecular chaperones are known to maintain protein homeo

71 Molecular chaperones are pivotal in folding and degradat

72 Molecular chaperones are responsible for managing protei

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

74 Metazoan molecular chaperones assist native folding and block pol

75 These results on a molecular chaperone at the nuclear pore suggest that Sig

76 o can be rescued from this inhibited form by molecular chaperones belonging to the ATPases associated

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

78 We found positive reactivity of the molecular chaperone BiP/GRP78 in conjunctival epithelium

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

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

81 Here we report that the Hsp90 molecular chaperone broadly regulates the transcription

82 n to contain a number of proteins, including molecular chaperones, but the consequences of these entr

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

84 90 (Hsp90) clients and are recruited to the molecular chaperone by the kinase-specific cochaperone c

85 reveal that the sequestration of cytoplasmic molecular chaperones by tau aggregates interferes with t

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

87 Thus, molecular chaperones can contribute to functional mainte

88 ctin requires assistance from the oligomeric molecular chaperone CCT.

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

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

96 ycan biosynthesis is regulated by a specific molecular chaperone Cosmc through assisting of the corre

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 Hsp70 is a highly conserved molecular chaperone critical for the folding of new and

100 Here, we delineate a molecular chaperone-dependent pathway for relocating act

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

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

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

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

105 arkinson's disease pathogenesis, acting as a molecular chaperone for alpha-synuclein.

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

107 lammasome activation, as well as acting as a molecular chaperone for intracellular proteins.

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

109 its prolyl isomerase activity and acted as a molecular chaperone for type III collagen.

110 ce of intracellular recycling of ER-resident molecular chaperones for collagen type I and bone metabo

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

112 quires the assistance of helper factors, the molecular chaperones, for quality control and the mainte

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

114 ction of proteins in the cell that carry out molecular chaperoning functions.

115 Molecular chaperones govern protein homeostasis, being a

116 Here, we present evidence that mitochondrial molecular chaperone GRP75, also known as mortalin/mthsp7

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

118 Molecular chaperones have central roles in each of the a

119 To counter this threat to cell viability, molecular chaperones have evolved to help nascent polype

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

121 The molecular chaperone heat shock protein (HSP) 101 is a pr

122 ssays), we studied the potential role of the molecular chaperone heat shock protein 70 (HSP70) in pri

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

124 Molecular chaperone Heat Shock Protein 70 (Hsp70) plays

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

126 cs are essential for function of the dimeric molecular chaperone heat shock protein 90 (Hsp90), inclu

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

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

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

130 ent tau aggregation, we demonstrate that the molecular chaperones heat-shock cognate 71-kDa protein (

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

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

133 The molecular chaperone Hsc70 performs essential tasks by fo

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

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

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

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

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

139 disassembled at elevated temperatures by the molecular chaperone Hsp104.

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

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

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

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

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

145 The major heat shock proteins and molecular chaperones Hsp70 and Hsp90, in turn, participa

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

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

148 The molecular chaperone Hsp90 affords a promising target bec

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

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

151 The molecular chaperone HSP90 facilitates the folding of sev

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

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

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

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

156 The molecular chaperone Hsp90, essential in all eukaryotes,

157 h highly conserved regulators, including the molecular chaperone Hsp90, the protein phosphatase calci

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

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

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

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

162 Molecular chaperones HSP90 and HSP70 are essential regul

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

164 HSP90 is a ubiquitously expressed molecular chaperone implicated in the correct folding an

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

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

167 Hsp90 is a highly conserved molecular chaperone important for the activity of many c

168 ll heat shock protein alphaA-crystallin is a molecular chaperone important for the optical properties

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

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

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

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

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

174 We investigated the role of molecular chaperones in both preventing and disaggregati

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

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

177 ock protein 90 (Hsp90) is a highly conserved molecular chaperone involved in ATP-dependent client pro

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

179 ses from the Hsp100/Clp family are a type of molecular chaperones involved in disassembling protein a

180 ) immunoglobulin binding proteins (BiPs) are molecular chaperones involved in normal protein maturati

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

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

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

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

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

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

187 The inhibition is counteracted by diverse molecular chaperones known as Rubisco activases (Rcas).

188 Loss of the Hsp104 molecular chaperone leads to the growth of prion particl

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

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

191 his transaction along with recently proposed molecular chaperone-like functions for CCS1 remain undef

192 The molecular chaperone machinery is important for the maint

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

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

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

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

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

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

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

200 Molecular chaperones often work collaboratively with the

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

202 el system to decipher the mechanism by which molecular chaperones overcome the multiple challenges du

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

204 Hsp70 molecular chaperones play key roles in cellular protein

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

206 Molecular chaperones prevent the aggregation of polyQ-co

207 Similarly, how the ribosome and molecular chaperones promote efficient folding remains o

208 tienzyme complex in lysosomes along with the molecular chaperone, protective protein cathepsin A (PPC

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

210 1, subunit 2 (CCT2), a gene that encodes the molecular chaperone protein, CCTbeta.

211 A human molecular chaperone protein, DnaJ heat shock protein fam

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

213 Here we show that these molecular chaperones recognize a region of the AR N-term

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

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

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

217 results help resolve the mechanisms by which molecular chaperones regulate the balance between AR agg

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

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

220 found that the sigma-1 receptor (Sig-1R), a molecular chaperone, reverses the pathological effects o

221 hotosynthesis the AAA+ protein and essential molecular chaperone Rubisco activase (Rca) constantly re

222 f carbon fixation into the biosphere, by its molecular chaperone Rubisco activase (Rca) is essential

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

224 highly polymorphic set of MHC-I alleles and molecular chaperones shapes the repertoire of peptide an

225 ps) are a family of ubiquitous intracellular molecular chaperones; some sHsp family members are upreg

226 Molecular chaperones such as Hsp40 and Hsp70 hold the an

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 volution is the expression of well-conserved molecular chaperones, such as those that are part of the

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 Here, we demonstrate that the molecular chaperone TAP-binding protein related (TAPBPR)

235 Here, using the molecular chaperone TAPBPR, we develop a robust method f

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

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

238 Hsp90 is a conserved molecular chaperone that assists in the folding and func

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

240 in the absence of its substrate, as a potent molecular chaperone that exhibits anti-aggregation activ

241 (HSP47) is an endoplasmic reticulum-resident molecular chaperone that facilitates collagen maturation

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

243 proline isomerase and turns it into a potent molecular chaperone that inhibits protein misfolding.

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

245 Hsp90 is a dimeric molecular chaperone that is essential for the folding an

246 UNC-45B is a multidomain molecular chaperone that is essential for the proper fol

247 eat-shock protein HSP27 is a redox-sensitive molecular chaperone that is expressed throughout the hum

248 in 90 (Hsp90) is an evolutionarily conserved molecular chaperone that is involved in the stability an

249 lated protein 75 (GRP75)] is a mitochondrial molecular chaperone that is often up-regulated and mislo

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

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

252 Heat shock protein 90 (Hsp90) is a molecular chaperone that plays an important role in tumo

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

254 eat shock protein 70 (Hsp70) is an important molecular chaperone that regulates oncoprotein stability

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

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

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

258 for the 90-kDa heat shock protein (HSP90), a molecular chaperone that suppresses the aggregation and

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

260 t shock proteins (Hsps) are highly conserved molecular chaperones that are ubiquitously expressed in

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

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

263 Small heat-shock proteins (sHsps) are molecular chaperones that facilitate the folding of prot

264 o families of highly conserved ATP-dependent molecular chaperones that fold and remodel proteins.

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

266 proteins (sHSPs) are ubiquitously expressed molecular chaperones that inhibit amyloid fibril formati

267 this approach, we have identified the known molecular chaperones that interact with human Heat Shock

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

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

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

271 teins (sHSPs) are a class of ATP-independent molecular chaperones that play vital roles in maintainin

272 roteins, but in other cases, they can act as molecular chaperones that prevent protein aggregation, e

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

274 Small heat-shock proteins (sHSPs) are molecular chaperones that respond to cellular stresses t

275 membrane chaperones might exist, akin to the molecular chaperones that stabilize and direct the assem

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

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

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

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

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

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

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

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

284 Organisms use molecular chaperones to combat the unfolding and aggrega

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

286 ellular proteins, viral proteins depend upon molecular chaperones to mediate their stabilization and

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

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

289 gulated by stress and are proposed to act as molecular chaperones to protect other proteins from stre

290 through downregulation of the mitochondrial molecular chaperone TRAP1, which subsequently increased

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

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

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

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

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

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

297 Hsp70s are allosteric molecular chaperones with conformational landscapes that

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

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