ライフサイエンスコーパス: chaperone

1 one H3 and perform the function of a histone chaperone.

2 ts different faces of the PPE protein to the chaperone.

3 s (Galpha) and serves as an essential Galpha chaperone.

4 and up-regulation of an ER stress-responsive chaperone.

5 of nuclear myosin was dependent on the Hsp90 chaperone.

6 asomal degradation and required intact HSP90 chaperone.

7 esidues form a critical interaction with the chaperone.

8 a-spectrin, and may reduce its dependence on chaperones.

9 p from other proteins such as isomerases and chaperones.

10 is an Hsp90 client protein stabilized by the chaperones.

11 pose the most widespread family of molecular chaperones.

12 ly drive the expression of non-ATP-dependent chaperones.

13 by the loss of Hsp70/Hsp90 chaperones and co-chaperones.

14 gically active alkylcobalamins by downstream chaperones.

15 ferential interactions of the HSP70s with co-chaperones.

16 ing an evolutionary convergence with protein chaperones.

17 these pathways require the activity of Hsp70 chaperones.

18 porters, signaling molecules, scaffolds, and chaperones.

19 sassembly and reassembly mediated by histone chaperones.

20 re ubiquitous and highly conserved molecular chaperones.

21 manner reminiscent of the action of protein chaperones(16).

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

23 trom resolution, with the aid of an antibody chaperone acting as a fiducial marker.

24 e fluorescence-based approach to observe the chaperone action of human alphaB-crystallin (alphaBc, HS

25 The molecular mechanism underlying this chaperone activation is unclear.

26 composition of the sHsp ensembles and their chaperone activities depends strongly on the respective

27 ions of these three regions, we compared the chaperone activities of various constructs of human alph

28 7 is an abundant protein exhibiting opposing chaperone activities on different substrates, indicating

29 domains contribute additional and important chaperone activities, both in delaying amyloid formation

30 solated alpha-crystallin domain retains some chaperone activity against amyloid formation, the flanki

31 the mechanisms by which sHSPs achieve their chaperone activity against amyloid-forming clients and h

32 Their chaperone activity has been proposed to require several

33 chanistic model points to ways in which sHSP chaperone activity may be increased, either by native fa

34 s made it difficult to explain the efficient chaperone activity of Hsp70s.

35 The chaperone activity of HspB1-HspB6 hetero-oligomers, howe

36 In vitro, recombinant MANF exhibited chaperone activity that depended on its conserved cystei

37 trinsic ACD-NTR interactions greatly enhance chaperone activity toward tau.

38 TR from a binding groove on the ACD enhances chaperone activity toward tau.

39 ers are ATP-sensitive, regulated by helicase/chaperone activity, and exhibit the hallmarks of maturat

40 tary biophysical assays (circular dichroism, chaperone activity, and small-angle x-ray scattering) an

41 As SRRP1 is known to harbor RNA chaperone activity, we postulate that SRRP1 mediates the

42 etween cis/trans isomerization and molecular chaperone activity.

43 and stimulates antioxidant, proteasome, and chaperone activity.

44 utics that specifically bind and inhibit its chaperone activity.

45 eat stress, likely through a redox-dependent chaperone activity.

46 omers, which leads to significantly enhanced chaperone activity.

47 olecular details of this PPIase with histone chaperoning activity, we have solved the crystal structu

48 ture or structural stability but reduced its chaperoning activity.

49 r protein-chaperone complex rather than with chaperones alone, in line with the release of the chaper

50 cular complexes, it is considered a chemical chaperone and has found numerous practical applications.

51 witch between UgpB's activity as a molecular chaperone and its activity as a G3P transporter.

52 n that they interact with their cognate EspG chaperone and that this chaperone determines the designa

53 ts can be rescued by the loss of Hsp70/Hsp90 chaperones and co-chaperones.

54 Molecular chaperones and cochaperones are the most abundant cellul

55 up-regulation of cellular components such as chaperones and folding catalysts.

56 Moreover, we examined histone chaperones and found that the FACT complex recognized AD

57 TORC1 and liberates proteasomes, ribosomes, chaperones and metabolic enzymes from non-membrane bound

58 creased protein turnover by sequestration of chaperones and proteases or formation of stable protein

59 ticular, increase the levels and activity of chaperones and the proteasome system in the cytosol.

60 d strong PPIase activity, no role in histone chaperoning and revealed a monomeric five-beta palm-like

61 cleosomes is dependent upon the FACT histone chaperone, and FACT is recruited to these regions when e

62 le to bind G3P is constitutively active as a chaperone, and its crystal structure shows that it conta

63 lum (ER) stress, (2) decreased protective ER chaperones, and (3) greater cell death and liver injury.

64 ound clients is regulated by ATP binding, co-chaperones, and post-translational modifications.

65 idomain proteins, folding in the presence of chaperones, and the ability to investigate real-time cot

66 wnregulation of genes associated with stress chaperones, and the induction of gene families involved

67 ling pathway involving the liver synthesized chaperone ApoM as a circulating pro-regenerative mediato

68 gan adaptation that involves circulating S1P chaperone ApoM(+) high density lipoprotein (HDL), which

69 The CblC and CblD chaperones are involved in early steps in the cobalamin

70 Holdase chaperones are known to be central to suppressing aggreg

71 Molecular chaperones are known to maintain protein homeostasis.

72 During protein synthesis, ER luminal chaperones are swept along the secretory pathway and mus

73 The retina-specific chaperone aryl hydrocarbon interacting protein-like 1 (A

74 r, this is just one function of this histone chaperone, as FACT also functions in DNA replication.

75 Posttranslational protein targeting requires chaperone assistance to direct insertion-competent prote

76 r ESX-3 heterotrimer is interacting with its chaperone at a drastically different angle and presents

77 found that cytoplasmic Antioxidant 1 copper chaperone (Atox1), which is up-regulated in breast cance

78 The Intramolecular Chaperone Auto-processing (ICA) domain of Myrf forms a h

79 an be achieved by differential expression of chaperones-balancing foldases (which accelerate folding)

80 by allosteric regulation of its chaperone/co-chaperone based client relationships can be used to adju

81 escued from this inhibited form by molecular chaperones belonging to the ATPases associated with dive

82 e two quality control sensors control lectin chaperone binding and glycoprotein egress from the ER.

83 onal protein that serves as a cytosolic iron chaperone, binding and transferring iron to recipient pr

84 E35/PPE68_1 version that carried the EspG(5) chaperone-binding domain, previously shown to redirect t

85 1, an evolutionarily distinct CENP-A histone chaperone, binds both CENP-A and the centromere receptor

86 e found positive reactivity of the molecular chaperone BiP/GRP78 in conjunctival epithelium of patien

87 Whereas most co-chaperones bound equally well to these two HSP70s, Hsp70

88 a complex cellular process often assisted by chaperones, but it can also be facilitated by interactio

89 icate that CYT-19 functions as a general RNA chaperone by using a stochastic, energy-intensive mechan

90 to caspase-8 inflammasome activation, GSDMD, chaperoned by Cdc37/Hsp90, recruits the E3 ligase, NEDD4

91 Chaperones can mediate both protein folding and degradat

92 ases (CcmF and SirE) and two apocytochrome c chaperones (CcmI and SirG).

93 Here, we show that the putative HSP-90 co-chaperone CHP-1 acts as a regulator of EGFR trafficking

94 lycation under physiological conditions, the chaperone-client complexes underwent greater extents of

95 Bacterial chaperones ClpB and DnaK, homologs of the respective euk

96 Hsp70 system by allosteric regulation of its chaperone/co-chaperone based client relationships can be

97 bitor JG98, that targets the cytosolic Hsp70 chaperone/co-chaperone complex, can significantly improv

98 how quantitatively how JG98 alters the Hsp70 chaperone/co-chaperone system to adjust the spatial cova

99 chaperone function, a phenomenon termed the "chaperone code."

100 the scoop loop to the stability of the MHC I-chaperone complex and to peptide editing.

101 imaging to reveal a key role for the histone chaperone complex FACT (SPT16 and SSRP1) in governing Ca

102 processing complex RIXC and with the histone chaperone complex FACT.

103 onarily conserved H2A.Z via the SWR1 histone chaperone complex has been extensively studied, in plant

104 on of PscN with secreted proteins or protein-chaperone complex rather than with chaperones alone, in

105 Here, we identified an HDAC6-chaperone complex that targets aberrantly modified tau.

106 stress caused by defects in the ATRX-histone chaperone complex, and that induced by MYCN-mediated met

107 hat targets the cytosolic Hsp70 chaperone/co-chaperone complex, can significantly improve the traffic

108 port the discovery of novel membrane protein chaperone complexes for the biogenesis of multi-pass mem

109 uctures of class I and class II effector TMD-chaperone complexes from Salmonella Typhimurium and Pseu

110 eficiency alters the distributions of ATZ-ER chaperone complexes, increasing ATZ-BiP binding and incl

111 genes including cytochrome C oxidase copper chaperone (COX17) and ATP Synthase, H(+) transporting, M

112 t to the curli pore, CsgG, and the secretion chaperone, CsgE.

113 Here, we delineate a molecular chaperone-dependent pathway for relocating activated gen

114 scavengers, sensors, signal transducers, and chaperones, depending on conditions and context.

115 h their cognate EspG chaperone and that this chaperone determines the designated secretion pathway.

116 ratus and to participate in the recognition, chaperone dissociation and unfolding of exported T3SS pr

117 d the feasibility of inhibiting the Hsp70 co-chaperone DNAJA1 as a novel anticancer strategy.

118 9 hours because of the von Willebrand factor chaperone effect.

119 iflunisal (1) or Tafamidis (2), an analogous chaperoning effect could not be observed.

120 asable misfolded protein to obviate possible chaperone effects on substrate physical state or transpo

121 f this site, with potential costs to overall chaperone efficiency but also advantages with respect to

122 o nuclear domains called VICE (Virus Induced Chaperone Enriched) domains and that this recruitment is

123 m tuberculosis virulence factor EsxA and its chaperone EsxB are secreted as a heterodimer (EsxA:B) an

124 ly, their presence inversely correlated with chaperone expression.

125 tuberculosis (Mtb), the protective effect of chaperones extends to survival in the presence of host s

126 s egg extract identified the dimeric histone chaperone facilitates chromatin transcription (FACT) as

127 The histone chaperone FACT is upregulated during mammary tumorigenes

128 tilized germ cells by recruiting the histone chaperone FACT, displacing histones, and initiating prot

129 ently isolate the complex interactome of HSP chaperone family proteins under normal and stress condit

130 ent involving the yeast cytoplasmic Hsp70 co-chaperone Fes1.

131 escorted to centromeres by a CENP-A-specific chaperone for deposition.

132 olecules that bring "clients" to the primary chaperone for efficient folding.

133 hough CHP-1 has been proposed to act as a co-chaperone for HSP90, our data indicate that CHP-1 plays

134 ven that GAPDH displays properties of a heme chaperone for inducible NO synthase, here we investigate

135 DEAD-box protein that functions as a general chaperone for mitochondrial group I introns.

136 STIP1 is a co-chaperone for the heat-shock protein, HSP90, and has bee

137 acellular recycling of ER-resident molecular chaperones for collagen type I and bone metabolism and a

138 tream role in elevation of stress-responsive chaperones for cytoskeletal maintenance in post-nuclear

139 h require a member of the Eag family of T6SS chaperones for export.

140 ding proteins (FABPs) serve as intracellular chaperones for fatty acids and other hydrophobic ligands

141 Whereas they are known as crystallization chaperones for membrane proteins or as simple alternativ

142 s of sialin and help develop pharmacological chaperones for Salla disease.

143 Our findings suggest that tissue-specific chaperone function contributes to the selective neuropat

144 In addition to its chaperone function for ENZ, PRO substantially contribute

145 Modulation of ER stress and chaperone function may offer a promising therapeutic app

146 ed across all kinetoplastids, and describe a chaperone function of the TbPRMT1 prozyme, which represe

147 binatorial array of PTMs that modulate Hsp90 chaperone function, a phenomenon termed the "chaperone c

148 EMC, and constrain models of EMC's proposed chaperone function.

149 reservoirs for active monomers or exhibit a chaperoning function themselves, understanding the mecha

150 on and consequent loss of its synaptic SNARE-chaperoning function.

151 e in its solution conformation and a reduced chaperoning function.

152 Chaperone gene induction was reduced in such cells, whic

153 AML) that captures the TA from a cytoplasmic chaperone (Get3 or TRC40, respectively).

154 ith tamoxifen (Tmx)-inducible deletion of ER chaperone Grp78, a key regulator of ER homeostasis, in a

155 Although Hsp70 family chaperones have been extensively examined for the last 5

156 sp70 activities by altered transcription, co-chaperone "helper" proteins, and ATP binding and hydroly

157 h in P. aeruginosa We also find that the RNA chaperone Hfq targets a subset of those nascent transcri

158 he up-regulation of the global regulator RNA chaperone hfq.

159 holdases and dispels the notion of a strict chaperone hierarchy.

160 topic deposition of CENP-A in cancer by H3.3 chaperones HIRA and DAXX may fortuitously result in hybr

161 ne two novel members of the Escherichia coli chaperone holdase family, RidA and CnoX, whose thiol-ind

162 eat shock protein Hsp33 into a highly active chaperone holdase that binds unfolded proteins and preve

163 astic spatial reorganization of the cellular chaperone Hsc70 into nuclear domains called VICE (Virus

164 ression of the mitochondria-specific protein chaperones, HSP60 and HSP10, suggesting that Akt3 is req

165 The protein chaperone HSP70 is overexpressed in many cancers includi

166 The molecular chaperone Hsp90, essential in all eukaryotes, plays a mu

167 onserved regulators, including the molecular chaperone Hsp90, the protein phosphatase calcineurin, an

168 ne protein biogenesis faces the challenge of chaperoning hydrophobic transmembrane helices for faithf

169 Hsp90 is a highly conserved molecular chaperone important for the activity of many client prot

170 pports its role as the putative disaggregase chaperone in chloroplasts.

171 inding that farnesylated DNAJA1 is a crucial chaperone in maintaining mutp53 stabilization, and by us

172 role of BCL2-associated athanogene family co-chaperones in managing the folding status of NPC1 varian

173 rones alone, in line with the release of the chaperones in the bacterial cytoplasm after the dissocia

174 ates in a distinct fashion compared to other chaperones in the OMP biogenesis network.

175 nt expression of striatum-enriched HspBP1, a chaperone inhibitory protein.

176 logs and provides insight into how substrate-chaperone interactions direct the outcome of remodeling.

177 ogical tools facilitates the study of myosin-chaperone interactions in mechanistic detail.

178 he Hsp100/Clp family are a type of molecular chaperones involved in disassembling protein aggregates.

179 obulin binding proteins (BiPs) are molecular chaperones involved in normal protein maturation and ref

180 sociated with up-regulation of 24 heat shock chaperones involved in protein folding and with the up-r

181 Hsp40 Sis1, providing the first evidence for chaperone involvement in MAD.

182 e new insights into the variability of Hsp70 chaperone involvement with a nuclear PQC degradation pat

183 The chaperone is also critically important, however, to the

184 Taken together, HSP70 chaperone is important for IKKepsilon activation, and ME

185 gnaling, whereby coreceptors activate SHH by chaperoning it from a latent extracellular complex to it

186 (atp), and low-density lipoprotein receptor chaperone (ldlr), that are under the regulation of Foxo

187 Loss of the Hsp104 molecular chaperone leads to the growth of prion particles until t

188 des dense granule protein GRA45, which has a chaperone-like domain, is critical for correct localizat

189 sion of the full-length 7TM mMOR-1 through a chaperone-like function.

190 is further enhanced by CpeZ (a homolog of a chaperone-like protein first characterized in Fremyella

191 approved cystic fibrosis protein trafficking chaperone, lumacaftor, has been proposed as novel therap

192 of CGEP upregulated the chloroplast protein chaperone machinery and 70S ribosomal proteins, but othe

193 udy, however, we report that the Hsp70/Hsp90 chaperone machinery and an F-box protein, MEC-15, have o

194 the functional specificity of the mtHsp70 co-chaperone machinery and providing resilience to mitochon

195 zation will further our understanding of how chaperones maintain the proteome.

196 Chaperone-mediated autophagy (CMA) is a selective type o

197 lly, HO2 is degraded by the lysosome through chaperone-mediated autophagy, distinct from other HRM-co

198 accharomyces cerevisiae Rnq1 amyloid reduces chaperone-mediated disassembly of Sup35 amyloid, promoti

199 irst, we discuss new molecular insights into chaperone-mediated histone variant deposition.

200 The chaperone-mediated sequestration of misfolded proteins i

201 together, our findings reveal mechanisms of chaperone-mediated stabilization and secretion of two di

202 2Fe-2S] cluster on a scaffold protein; Hsp70 chaperone-mediated trafficking of the cluster and insert

203 An intracellular chaperone, microsomal triglyceride transfer protein (MTP

204 s aeruginosa, respectively, reveals that Eag chaperones mimic transmembrane helical packing to stabil

205 However, how the chaperone model applies to diverse sHSPs and what proces

206 DotL ATPase, the DotM and DotN proteins, the chaperone module IcmSW, and two previously uncharacteris

207 Hsp70 is regulated by a suite of co-chaperone molecules that bring "clients" to the primary

208 The mitochondrial HSP70 chaperone mortalin (HSPA9/GRP75) is often upregulated an

209 on by studying the role of a cotranslational chaperone, nascent polypeptide-associated complex (NAC),

210 ts on neuronal differentiation, and that the chaperones negatively regulate neuronal morphogenesis an

211 The less efficient chaperone network of differentiated neural progeny may c

212 The chaperone network of NSPCs is more effective than that o

213 erase (UGGT) 1 and 2 are central hubs in the chaperone network of the endoplasmic reticulum (ER), act

214 We find that the NSPC chaperone network robustly maintains misfolded protein s

215 Chaperone networks are required for the shearing and gen

216 d protein that extend to many clients within chaperone networks.

217 mechanistic insights into the enzyme repair chaperones of the highly diverse CO(2) fixation machiner

218 protein receptor (SNARE) proteins, and SNARE chaperones of the Sec1/Munc18 (SM), Sec17/alpha-SNAP, an

219 c RQaQbQc complexes between membranes; SNARE chaperones of the SM, Sec17/alphaSNAP, and Sec18/NSF fam

220 Chaperone oligomerization is often a key aspect of their

221 Irrespective of whether chaperone oligomers act as reservoirs for active monomer

222 ins from other bacteria, which typically use chaperones or initiator proteins to initiate amyloid ass

223 as not detected in a mutant that lacked both chaperones, perhaps due to misfolding or instability.

224 expression of both wild-type and mutant Clp chaperone (PfClpC) variants revealed a functional chaper

225 Heat shock protein 70 (HSP70) chaperones play a central role in protein quality contro

226 distribution of Hsp82 is regulated by its co-chaperone Ppt1.

227 rone (PfClpC) variants revealed a functional chaperone-protease interaction.

228 increased the expression of the pneumococcal chaperone/protease HtrA.

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

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

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

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

233 The chaperone protein SmgGDS promotes cell-cycle progression

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

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

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

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

238 ion and as an antioxidant and is believed to chaperone Q(6) from its site of synthesis to the respira

239 s mediated by an extensive network of >1,000 chaperones, quality control factors, and trafficking mec

240 A delicate interplay between HSP70s and co-chaperone recruitment is thought to determine substrate

241 Deletion of these chaperones reduces the ER-resident MR1 pool and hampers

242 gomerization, and interactions with cellular chaperones remain poorly understood.

243 rization of one novel RNA pair bound by both chaperones revealed that while Hfq is required for RNA s

244 ixation into the biosphere, by its molecular chaperone Rubisco activase (Rca) is essential for photos

245 erm balancing selection in the heat-shock co-chaperone sacsin We conducted a genome-wide association

246 Here, we found host co-chaperones Sba1, Cpr6 and Cpr7 inhibited hHsp90alpha fun

247 nt capacity of cellular degradative systems, chaperone shortage or high levels of mistranslation by r

248 its potential to serve as a matchmaking RNA chaperone, significant gaps remain in our understanding

249 f a virus hijacking a function of a cellular chaperone, since simian immunodeficiency virus T antigen

250 by which Munc13-1 and Munc18-1 cooperatively chaperone SNARE folding and assembly, thereby regulating

251 Tethering factors play a key role in chaperoning SNARE assembly; however, the underlying mole

252 that involvement of the budding yeast Hsp70 chaperones Ssa1 and Ssa2 in nuclear PQC degradation vari

253 ctants, but also serve as effective chemical chaperones stabilizing protein functionality.

254 rther validation reveals the central role of chaperones, stress response proteins and transport pumps

255 defined by their affinities for specific co-chaperones such as HSPH2.

256 s the expression of well-conserved molecular chaperones, such as those that are part of the heat shoc

257 The periplasmic chaperone SurA plays a key role in outer membrane protei

258 zation, and present the effects on the Hsp90 chaperone system at the levels of conformational steady

259 ively how JG98 alters the Hsp70 chaperone/co-chaperone system to adjust the spatial covariance (SCV)

260 hase (nNOS), a client of the Hsp90 and Hsp70 chaperone system, we have established that inactivation

261 h translation, growth, reproduction, and the chaperone system.

262 otein sequence and a selection of designated chaperone systems and chromatin remodelling complexes th

263 ation of proteins unless they are guarded by chaperone systems.

264 ere effectively engaged by fewer periplasmic chaperones than their urea-denatured counterparts.

265 We conclude that MANF is an ER chaperone that enhances protein folding and myocyte viab

266 ence of its substrate, as a potent molecular chaperone that exhibits anti-aggregation activity agains

267 with 4-phenylbutyrate, a well-known chemical chaperone that improves trafficking of several transmemb

268 omerase and turns it into a potent molecular chaperone that inhibits protein misfolding.

269 AIPL1 is a photoreceptor-specific co-chaperone that interacts with HSP90 to facilitate the st

270 UNC-45B is a multidomain molecular chaperone that is essential for the proper folding and a

271 eptor (S1R) is an endoplasmic reticulum (ER) chaperone that not only regulates mitochondrial respirat

272 Thus, the PAT complex is an intramembrane chaperone that protects TMDs during assembly to minimize

273 n-like 1 (AIPL1) is a photoreceptor-specific chaperone that stabilizes the effector enzyme of phototr

274 ctional, endoplasmic reticulum (ER)-resident chaperone that, translocated to the external microenviro

275 ll heat-shock proteins (sHsps) are molecular chaperones that facilitate the folding of proteins or ta

276 (sHSPs) are ubiquitously expressed molecular chaperones that inhibit amyloid fibril formation; howeve

277 er they are injected, due to the activity of chaperones that keep the effectors in a structural state

278 ther DEAD-box proteins, as ATP-dependent RNA chaperones that limit the condensation of RNA, analogous

279 Ps) are a class of ATP-independent molecular chaperones that play vital roles in maintaining protein

280 ut in other cases, they can act as molecular chaperones that prevent protein aggregation, even under

281 RNA chaperoned the evolution of protein folding from the ver

282 ine thresholding mechanisms utilizing NTPase chaperones (the MoxR-vWA couple), GTPases and proteolyti

283 sitively charged linker histone H1.0 and its chaperone, the negatively charged prothymosin alpha.

284 ned by the antagonism between MEC-15 and the chaperones; this antagonism regulates TRN development, a

285 Therefore, a balance between the UPS and the chaperones tightly controls neuronal differentiation.

286 eveals that nuclear-localized IPMK acts as a chaperone to inhibit LLPS of TFEB to negatively control

287 and requires a high concentration of luminal chaperones to function.

288 t is processed and targeted via a network of chaperones to its dependent enzymes.

289 coordinates with mitochondrial proteases and chaperones to maintain the mitochondrial proteome.

290 stress and are proposed to act as molecular chaperones to protect other proteins from stress-induced

291 ve receptor and BBB transporter for the iron chaperone transferrin.

292 in vitro using dexamethasone or the chemical chaperones TUDCA and 4PBA attenuated MMP9 expression and

293 The myosin-directed chaperone UNC-45B is essential for sarcomeric organizati

294 ts delineate the scope and limitations of S1-chaperoned unfolding of structured RNAs.

295 Genome sequencing enabled us to identify a chaperone-usher pili system (Kpi) in Kp3380.

296 SI+] variants arising in the absence of each chaperone were cured by restoring normal levels of that

297 To discern whether chaperones were directly involved in Ubr1-mediated ubiqu

298 Ssb1/2p and RAC chaperones were previously found to inhibit [PSI+] prion

299 and indicate pleiotropic effects from HSP70 chaperones, which are generally thought to suppress poly

300 position of CenH3 must be ensured by histone chaperones, which handle the non-nucleosomal CenH3 pool