ライフサイエンスコーパス: chaperone

1 on and involved non-canonical regions of the chaperone.

2 ization and thus the acid activation of this chaperone.

3 formation normally attained by the ATP-bound chaperone.

4 ins muscle function by acting as a molecular chaperone.

5 etion is dependent on CpaB, a membrane-bound chaperone.

6 (Hsp90) is an essential eukaryotic molecular chaperone.

7 l changes and a population shift in the DnaK chaperone.

8 g polyphosphate, a newly recognized chemical chaperone.

9 of ubiquitous and highly conserved molecular chaperone.

10 inds in the amino acid 393-537 region of the chaperone.

11 sistance by a complex machinery of molecular chaperones.

12 eins), and that the rProtein and rRNA are co-chaperones.

13 ded polypeptide subunits, without biological chaperones.

14 he cysteine-rich zinc-binding domain of DnaJ chaperones.

15 ress response with up-regulation of cellular chaperones.

16 they constitute a second major class of RNA chaperones.

17 most recent affinity determinations of Cu(I) chaperones.

18 2A-H2B dimers without any additional histone chaperones.

19 targets, as well as to other crystallization chaperones.

20 ess rates of Fabs as structure determination chaperones.

21 We have previously shown that the chemical chaperone 4-phenylbutyrate (4-PBA) promotes the maturati

22 8 was blocked by treatment with the chemical chaperone 4-phenylbutyrate, uncovering the involvement o

23 Two chemical chaperones, 4PBA and TUDCA, were used to ameliorate the

24 further show that overexpression of certain chaperones abrogates protein aggregation and protects a

25 eduction in the expression of this molecular chaperone accelerates prion pathogenesis in vivo.

26 tes of SlyD, which suppresses its PPIase and chaperone activities.

27 e, we show that GIGANTEA has general protein chaperone activity and can act to specifically facilitat

28 egulation of the BiP chaperone cycle and its chaperone activity by subtle local perturbations at SBD

29 these mutations lead to modulation of their chaperone activity in vitro, the in vivo functions of al

30 interactions negatively regulate Npm histone chaperone activity in vitro.

31 Key to the chaperone activity is an ATP-induced allosteric regulati

32 The mechanism underlying the chaperone activity of AIPL1 is largely unknown, but invo

33 lity of the dimer contribute to the enhanced chaperone activity of phosphorylated Hsp27.

34 lin) are promiscuous chaperones, whereas the chaperone activity of the other sHsps is more substrate-

35 Here we report the effect of chaperone activity on the functional conformation of the

36 steine during stress beneficially alters BiP chaperone activity to cope with suboptimal folding condi

37 d by coiled-coil MDs to tightly control AAA+ chaperone activity.

38 eating additional complexity that may affect chaperone activity.

39 lated ASF1b and does not require its histone chaperone activity.

40 ds to the H2A-H2B dimer and exhibits histone chaperone activity.

41 Domains related to the chaperones activity were also found up-regulated in SP a

42 hat stabilize ribozyme folding; the apparent chaperoning activity of these ubiquitous proteins signif

43 e Hsp90 dimer and prevents the activating co-chaperone Aha1 from binding the middle domain of Hsp90.

44 of the interaction between Hsp90 and its co-chaperone Aha1, which accelerates the ATPase activity of

45 Strikingly, TIPRL and the latency chaperone, alpha4, coordinate to disassemble active holo

46 eria, separate genes encode a copper binding chaperone and a copper efflux pump, but in some the chap

47 ted by the addition of a naturally occurring chaperone and a nanobody designed to bind to the Abeta p

48 Thus, in addition to serving as a histone chaperone and transcription elongation factor, Spt6 coun

49 hallenging macromolecules as crystallization chaperones and as molecular fiducial marks for single pa

50 itochondria, where it recruits mitochondrial chaperones and assists in the folding of alpha-ketogluta

51 other in general, but whereas inhibitors of chaperones and cell cycle kinases induce similar transcr

52 Overproduction or deficiency of many chaperones and other cellular components cure the yeast

53 r proteostasis) network comprising molecular chaperones and other factors.

54 ress by inducing the expression of molecular chaperones and other heat shock response genes.

55 asmic Cu(+) sensor CueR controls cytoplasmic chaperones and plasma membrane transporters, whereas Cop

56 s in a manner that is regulated by molecular chaperones and requires TORC1 activity signaling through

57 This is likely a consequence of inefficient chaperoning and accumulation of alpha7 subunits in the E

58 ts as a polymerase cofactor, a viral protein chaperone, and an antagonist of the innate immune respon

59 protein complexes with HIRA, a histone H3.3 chaperone, and stabilizes the protein levels of HIRA com

60 Amongst these proteins are many Hsp40 co-chaperones, and a single Hsp70.

61 is abundant, selected transcription factors, chaperones, and heat shock proteins) were highly express

62 that has remained elusive for other histone chaperones, and it advances our understanding of how nuc

63 Many enzymes, molecular chaperones, and post-translational modifiers facilitate

64 h the study of protein folding and molecular chaperones, and she went on to show that protein folding

65 The histone chaperone anti-silencing factor 1a (ASF1a) interacts wit

66 Histone chaperones are a non-catalytic group of proteins that ar

67 his display is unique to cancer cells, these chaperones are attractive targets for drug development.

68 sequence-based predictions show that histone chaperones are highly enriched in intrinsically disorder

69 Molecular chaperones are pivotal in folding and degradation of the

70 Histone chaperones are responsible for binding the highly basic

71 servations establish BiP and its J domain co-chaperones as key regulators of the UPR.

72 SecB chaperones assist protein export in bacteria.

73 Thus, chaperone-assisted eviction of linker histones and Shugo

74 We show that the copper chaperone Atox1, which delivers copper to ATP7B, and the

75 Additionally, NAP1 histone chaperones, ATP-dependent chromatin remodeling factors,

76 work informs future studies about functional chaperone balance and cautions against therapeutic chape

77 epair in vitro Subsequent restoration of the chaperone-BER complex in cell, presumably after completi

78 e endoplasmic reticulum (ER)-localized Hsp70 chaperone BiP contributes to protein folding homeostasis

79 Most of the mutants interact with the ER chaperone BiP, while only mutants with aberrant glycosyl

80 s and reduced interactions with the ER HSP70 chaperone BiP.

81 into and through the lipid-binding pocket is chaperoned by sets of PITPalpha residues conserved throu

82 CO release is chaperoned by turn-on fluorescence and can be triggered

83 Golgi due to prolonged association with the chaperone calnexin.

84 ed exosomal release of the immunostimulatory chaperones calreticulin, Gp96, and ORP150; and increased

85 ailable evidence suggests that even a single chaperone can use many mechanisms to aid in protein fold

86 ulosis as a model to investigate how generic chaperones can specialize toward the control of TA syste

87 Actin-related proteins include chaperones, carbohydrate kinases, and other enzymes, as

88 ical SAM protein family HemW/RSAD1 is a heme chaperone catalyzing the insertion of heme into hemoprot

89 An emerging class of chaperones, chaperone-like amyloid binding proteins (CLA

90 wall and inhibits SlyD, which is a molecular chaperone, cis/trans peptidyl prolyl isomerise (PPIase)

91 sure efficient folding, members of different chaperone classes receive the nascent protein chain emer

92 ective heat shock proteins (HSPs), molecular chaperones/cochaperones constituting a major component o

93 catalytic mechanism constraints and required chaperone complementarity that hinder Rubisco biogenesis

94 leus as naked DNA, we asked whether the HIRA chaperone complex affects herpesvirus infection.

95 that identifies MLF as a member of a nuclear chaperone complex containing a DnaJ protein, BCL2-associ

96 The HIRA histone chaperone complex deposits histone H3.3 into nucleosomes

97 We propose that the HIRA chaperone complex represses incoming naked viral DNAs th

98 ssembly factor 1 (CAF1), a conserved histone chaperone complex that deposits H3-H4 during DNA replica

99 R constituents are present in a multi-client chaperone complex with HSP90.

100 arily studied because of its dependence on a chaperone complex, IcmSW, for translocation through the

101 a complementary conserved R2TP-like HSP90 co-chaperone complex, the loss of which affects assembly of

102 doxin Glrx3 and BolA2 function as a [2Fe-2S] chaperone complex.

103 hieve a more selective targeting of Hsp90-co-chaperone complexes.

104 sickest proteins use the most ATP-expensive chaperones), comprehensive (it can handle any type of pr

105 le any type of protein), and economical (the chaperone concentrations are just high enough to keep th

106 ric KhpA/B may function as a pleiotropic RNA chaperone controlling pneumococcal cell division.

107 Both CopZ chaperones could bind Cu(+) with high affinity.

108 ual post-translational regulation of the BiP chaperone cycle and its chaperone activity by subtle loc

109 ions of Hsp70 are independent of its protein chaperone cycle but also provide potential mechanical ex

110 We present methyl NMR analysis of the BiP chaperone cycle that reveals surprising conformational h

111 the polypeptide-binding pocket in the Hsp70 chaperone cycle.

112 function of PTEN in complex with the histone chaperone DAXX and the histone variant H3.3.

113 Exported substrates are chaperone-delivered to the translocase, EscV in enteropa

114 Here, we show that STUB1, a chaperone-dependent E3 ubiquitin ligase, modulates TFEB

115 sidues in the GERAMT-binding site for proper chaperone-dependent regulation of SOD2 antioxidant funct

116 p90Ec and Hsp70, DnaK, requires that the two chaperones directly interact.

117 has against itself, which depends on the co-chaperone, DnaJ-1.

118 70-interacting protein (CHIP), if freed from chaperones during acute stress, can dock on cellular mem

119 Finally, our data emphasize that sHsp chaperone efficiency depends on oligomerization and that

120 ne and a copper efflux pump, but in some the chaperone encoding gene has been elusive.

121 Ring-forming AAA+ chaperones exert ATP-fueled substrate unfolding by threa

122 Inhibition of chaperone expression, autophagy or the proteasome, in ad

123 , this study provides direct support for non-chaperone, extracellular Hsp90alpha as a potential drive

124 t replisome progression requires the histone chaperone FACT (facilitates chromatin transcription).

125 uggesting that it might physically bring the chaperone families together into a complex.

126 ds to a model wherein DDX1 can act as an RNA chaperone, folding stem IIB into a proper Rev binding co

127 -RAC further revealed that endogenous copper chaperone for SOD1 (CCS) is S-acylated in both human and

128 The copper chaperone for superoxide dismutase (Ccs1) activates imma

129 ex onto the nucleocapsid, but also acts as a chaperone for the nucleoprotein.

130 oli GroEL and GroES, are essential molecular chaperones for protein folding.

131 linositol-4-phosphate enhance association of chaperone-free CHIP with liposomes.

132 mation is required for understanding of this chaperone-free metal-cluster assembly.

133 of the UPR initiated by the ER-localized co-chaperone from Arabidopsis thaliana, AtBAG7.

134 ing that IDRs are often critical for histone chaperone function and play key roles in chromatin assem

135 y of mtHsp70 for its protein clients and its chaperone function are regulated by binding of ATP/ADP t

136 dules collaborated with GroEL(SR) to perform chaperone function in vivo: three GroES(7) variants func

137 We conclude that the Ub-binding pocket has a chaperone function involved in bud initiation.

138 echanism of CTD auto-inhibition predicts the chaperone function of Hfq in bacterial genera and illumi

139 hat it is possible to abrogate a specific co-chaperone function of Hsp90 without inhibiting the entir

140 r dynamics and may play a role in conferring chaperone function to 14-3-3zeta protein.

141 attributed to their N-terminal ATPase-driven chaperone function.

142 c translocation of MTA1 was dependent on the chaperoning function of heat shock protein 90 (HSP90) an

143 ver, these mutations disrupted multiple MeaB chaperone functions, including cofactor editing, loading

144 ), GTPase-activating proteins (GAPs), or the chaperone/GEF Ric-8A], while favoring high-affinity bind

145 4-fold increase in the expression of class I chaperone genes including GroEL and GroES.

146 ered class-I small heat-shock protein (sHSP) chaperone genes, SlHSP17.6, SlHSP20.0 and SlHSP20.1, in

147 the mammalian endoplasmic reticulum-resident chaperone gp96.

148 We now find that the ER chaperone Grp170 participates in the degradation process

149 ce in which both Apc and ER stress repressor chaperone Grp78 can be conditionally deleted from the in

150 n known in Escherichia coli, no gene for its chaperone had been identified.

151 assic role in maintaining protein stability, chaperones have additional roles in transport, chaperoni

152 Although Hsc70 and other co-chaperones have been shown to play a role in nuclear tra

153 B present in control DCs, covalently bind to chaperone heat shock protein 70.

154 report that a radical SAM protein, the heme chaperone HemW from bacteria, is required for the insert

155 Immunoprecipitation with the RNA chaperone Hfq drafts an unexpectedly large post-transcri

156 In bacteria, the RNA chaperone Hfq enables pairing of small regulatory RNAs w

157 combination with mutants of the histone H3.3 chaperone HIRA (Histone Regulator A) results in impaired

158 The histone chaperone HIRA is involved in depositing histone variant

159 P-A (centromere protein A), deposited by its chaperone, HJURP (Holliday junction recognition protein)

160 Ste11, and also, remarkably, the main Hsp90 chaperone (Hsc82) itself.

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

162 nucleotide exchange factor of the molecular chaperone Hsp70, and its interaction with another molecu

163 yn aggregation is dependent on the molecular chaperone Hsp70, which is consistent with the well-known

164 tion, Hsp104 cooperates with Hsp70 and Hsp40 chaperones (Hsp70/40) to form a bi-chaperone system.

165 The function of the molecular chaperone Hsp90 depends on large conformational changes,

166 -chaperone that interacts with the molecular chaperone HSP90 to facilitate the stable assembly of the

167 inases PKCbeta, PAK2, Lck, and CDK1, and the chaperone HSPA5.

168 ocessing through its interaction with the ER chaperone HSPA5/BiP.

169 an endoplasmic reticulum-resident molecular chaperone in Caenorhabditis elegans MEC-6 modulates the

170 dase activity, AnPrx6 can act as a molecular chaperone in its dimeric state, contrary to other Prxs.

171 BiP is the only Hsp70 chaperone in the endoplasmic reticulum (ER) and similar

172 ics (LC-MS/MS) to elucidate the role of this chaperone in the physiology and virulence of Yersinia en

173 deposition and emphasize the role of histone chaperones in adjusting genome expression.

174 Nap1 and Chz1 and a redundant role for these chaperones in H2A.Z deposition.

175 which is guided by at least four RP assembly chaperones in mammals: PAAF1, p28/gankyrin, p27/PSMD9, a

176 tifunctional adaptors that serve as iron ion chaperones in the cytosolic/nuclear compartment, binding

177 R-C complex, which relies on several histone chaperones including Nap1 and Chz1 to deliver H2A.Z-H2B

178 en proposed to coordinate with ATP-dependent chaperones, including heat shock protein 70 (Hsp70).

179 hibiting topoisomerases or depleting histone chaperones increased unwrapping, whereas inhibiting rele

180 expression of nAChR-specific and resident ER chaperones, indicating increased ER stress.

181 ng with the established mitochondrial matrix chaperone inhibitor gamitrinib-TPP.

182 Strikingly, NAP1-like histone chaperones interact with CSB and greatly enhance CSB-med

183 The ATPase cycle of the Hsp90 molecular chaperone is essential for maintaining the stability of

184 Our results indicate that subunit self-chaperoning is a robust mechanism for heteromeric protei

185 ygous for CK2alpha' shows increased HSF1 and chaperone levels, maintenance of striatal excitatory syn

186 pping an allosteric landscape of a molecular chaperone like DnaK will facilitate the development of s

187 POTRA2-3 also was found to have chaperone-like activity in an insulin aggregation assay,

188 ide bridges but possesses a strong molecular chaperone-like activity.

189 An emerging class of chaperones, chaperone-like amyloid binding proteins (CLABPs), has be

190 d complex, signifying a potential regulatory chaperone-like function for RavA-ViaA during bacterial a

191 at the core of the ATPase regulation of the chaperone machinery that maintains protein homeostasis.

192 s into adulthood and induces a select set of chaperones, many of which have been implicated in lifesp

193 al pathway and also suggest a mechanism that chaperones may exploit to prevent misfolding.

194 ich can be cleared through an HSF1-dependent chaperone mechanism that disaggregates the protein.

195 Chaperone-mediated autophagy (CMA) serves as quality con

196 Here we find that ER disturbance activates chaperone-mediated autophagy (CMA).

197 hoehorn-like fashion in the last step of the chaperone-mediated proteasome assembly.

198 f their central cellular function, bacterial chaperones might be potential candidates for drug target

199 oviding direct evidence against a sequential chaperone model.

200 one balance and cautions against therapeutic chaperone modifications without a thorough examination o

201 As force hinders the folding transition, chaperones must play a role in this scenario, although t

202 ar how these two important components of the chaperone network are linked.

203 Especially in the field of molecular chaperones, NMR has recently provided the first-ever hig

204 F1), that are particularly dependent on this chaperone, no equivalent clients for Hsp70 have been rep

205 -related proteins, such as puroindolines and chaperones, notably involved in the gluten-protein foldi

206 Our data reveal that Munc18-2 is not just a chaperone of STX11 but also directly contributes to comp

207 k coordinates these processes with molecular chaperones of different classes and their regulators fun

208 This concept may also hold true for other co-chaperones of Hsp90.

209 Chaperones of the HSP100 family help with substrate unfo

210 magnetic tweezers to study the influence of chaperones on protein folding and show that the ribosoma

211 ein permitting it to act as a potential haem chaperone or transporter.

212 ium between bound and unbound CENH3 (and its chaperones or binding proteins).

213 It has been shown that chaperones or karyopherins responsible for import can ma

214 tors, but not other antipsychotics, chemical chaperones, or VPA structural analogues.

215 by a proteostasis network containing protein chaperones, peptidases, and their substrate recognition

216 Although most histone chaperones perform these common functions, recent struct

217 dings suggest that MLF and the associated co-chaperones play a direct role in modulating gene transcr

218 Hsp70 molecular chaperones play key roles in cellular protein homeostasi

219 glustat) and a preliminary evaluation of its chaperoning potential are herein reported.

220 The chaperones presented herein enable direct access to imid

221 The chaperone protein and guanine nucleotide exchange factor

222 Clusterin is a chaperone protein associated with treatment resistance a

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

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

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

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

227 volved through immune selection on the groEL chaperone protein.

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

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

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

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

232 s a stable complex with GroES, arresting the chaperoning reaction cycle.

233 LRP1 is direct, and is modulated by the LRP chaperone, Receptor-Associated Protein (RAP).

234 aperones, their roles in histone binding and chaperoning remain unclear.

235 which an "epigenetic addiction" to the HJURP chaperone represents an Achilles' heel in p53-deficient

236 ), a master transcriptional regulator of the chaperone response, has been coopted from its role as a

237 -43 aggregation is targeted by a coordinated chaperone response.

238 tin assembly factor 1 (CAF-1) is the histone chaperone responsible for histone (H3-H4)2 deposition fo

239 expression of RovM caused by the loss of Hfq chaperone resulted in extended growth defect, alteration

240 structural studies of many different histone chaperones reveal that there are few commonalities in th

241 a bacterial Lsm family RNA-binding protein, chaperones RNA-RNA interactions between regulatory small

242 y, Bcp1 is a novel 60S biogenesis factor via chaperoning Rpl23 in the nucleus.

243 Previous work has shown that the chaperones Rpn14, Nas6, Hsm3, and Nas2 each bind a speci

244 ly be engaged and remodeled by the molecular chaperone Rubisco activase (Rca).

245 Here, we used both the export chaperone SecB of Escherichia coli and the tripartite TA

246 completion of repair, suggests that histone chaperones sequester the repair complex for oxidized bas

247 Here the authors show that cytosolic chaperones shift the F508del channel conformation to the

248 -vacuolar junction, and it utilizes cellular chaperones similarly to the aggregation of toxic or misf

249 thickness, the Escherichia coli periplasmic chaperones Skp and SurA, and BamA, the central subunit o

250 carrying the I4895T mutation with a chemical chaperone, sodium 4-phenylbutyrate (4PBA), reduces ER st

251 models derived from ExoU in complex with its chaperone, SpcU.

252 The yeast Hsp70 chaperone Ssb interacts with ribosomes and nascent polyp

253 c stem cell transplantation, pharmacological chaperones, substrate reduction therapy, or stop codon r

254 rotein at different sites results in a fuzzy chaperone-substrate ensemble and suggests a mechanism fo

255 amentally differs from canonical promiscuous chaperone-substrate interactions.

256 vitro degradation of two intermembrane space chaperone subunits, Tim9 and Tim10.

257 We propose that chaperones such as trigger factor can work as foldases u

258 Treatment with chemical chaperones, such as sodium 4-phenylbutyrate (PBA), reduc

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

260 The 90-kDa heat shock protein (Hsp90) chaperone system affects the accumulation of these toxic

261 discuss these findings in the context of the chaperone system of the lens, which we hypothesize seque

262 We propose that the HSP90/R2TP chaperone system promotes the assembly of a key module o

263 and Hsp40 chaperones (Hsp70/40) to form a bi-chaperone system.

264 the function of ER-associated and cytosolic chaperone systems in protein quality control.

265 In such tripartite TA-chaperone (TAC) systems, the chaperone was shown to assi

266 The chemical chaperones tauroursodeoxycholate (TUDCA) and 4-phenylbut

267 assembly factor 1 (CAF-1) is a H3-H4 histone chaperone that associates with the replisome and orchest

268 PL1 functions as a photoreceptor-specific co-chaperone that interacts with the molecular chaperone HS

269 Ank4 interacts with Bat3, a eukaryotic chaperone that is essential for ERAD, and is transiently

270 HdeA is a periplasmic chaperone that is rapidly activated upon shifting the pH

271 a widely conserved and ubiquitous molecular chaperone that participates in ATP-dependent protein rem

272 endoplasmic reticulum (ER)-targeted HSP40 co-chaperone that performs multifaceted functions involved

273 p90 is a homodimeric ATP-dependent molecular chaperone that remodels its substrate 'client' proteins,

274 are an evolutionarily conserved family of co-chaperones that are linked to disease states in mammals

275 clude biogenesis of iron-sulfur proteins and chaperones that deliver iron cofactors in cells.

276 s display on their surface several molecular chaperones that normally reside in the endoplasmic retic

277 terest are radical SAM enzymes, such as heme chaperones, that insert heme into respiratory enzymes.

278 and could be mechanistically important in co-chaperoning the assembly of the ribosome.

279 aperones have additional roles in transport, chaperoning the assembly site, and dissociation of ribos

280 locking the proteasome, Hsp70-type molecular chaperones, the Pib1 E3 ubiquitin-protein ligase, and th

281 disordered regions are common among histone chaperones, their roles in histone binding and chaperoni

282 region of PulG, we propose that PulM acts as chaperone to promote pseudopilin recruitment and coordin

283 olding, most likely due to the need for most chaperones to bind clients promiscuously.

284 cert with ferrireductases, ferroxidases, and chaperones to direct the movement of iron into, within,

285 optimization, and co-expression of molecular chaperones to promote expressed SrtA secretion into the

286 d expands the arsenal of the crystallization chaperone toolkit, which may be applicable to crystalliz

287 protein folding and show that the ribosomal chaperone trigger factor acts as a mechanical foldase by

288 h tripartite TA-chaperone (TAC) systems, the chaperone was shown to assist folding and to prevent deg

289 ly, constitutive downregulation of molecular chaperones was observed, which may impact response to co

290 m, although deletion of hfq, encoding an RNA chaperone, was defective in both LB and YESCA.

291 h nitrogen metabolism, energy production and chaperones were less abundant.

292 and HspB5/alphaB-crystallin) are promiscuous chaperones, whereas the chaperone activity of the other

293 ed reduction in expression of this essential chaperone which so far has been studied primarily in you

294 cially between the peptide substrate and its chaperone, which functions either as a stand-alone prote

295 MeaB is a multifunctional G-protein chaperone, which gates loading of the active 5'-deoxyade

296 id binding protein 4 (FABP4) is a fatty acid chaperone, which is induced during adipocyte differentia

297 or large-scale dynamics in a substrate-bound chaperone, which provides an effective mechanism to reta

298 This approach employs a radical relay chaperone, which serves as a traceless director that fac

299 cilitate the access of Hsp70 and ClpB/Hsp104 chaperones, which in ATP-dependent reactions disentangle

300 Hsp70s are allosteric molecular chaperones with conformational landscapes that involve l